vif

Virion infectivity factor

251 amino acids

Determines virus infectivity.

Belongs to the feline lentivirus group Vif protein family.

29.138 kDa

MSEEDWQVSRRLFAVLQGGVNSAMLYISRLPPDEREKYKKDFKKRLFDTETGFIKRLRKAEGIKWSFHTRDYYIGYVREMVAGSTTSLSLRMYIYISNPLWHSQYRPGLKNFNKEWPFVNMWIKTGFMWDDIEKQNICIGGEVSPGWGPGMVGIAIKAFSCGERKIEATPVMIIRGEIDPKKWCGDCWNLMCLRNSPPKTLQRLAMLACGVPAKKWRGCCNQRFVSPYRTPADLEVIQSKPSWNLLWSGEL

vif

Virion infectivity factor

251 amino acids

Determines virus infectivity.

Belongs to the feline lentivirus group Vif protein family.

29.171 kDa

MSDEDWQVSRRLFAVLQGGVYNAMLYISRLPQDEREKYKKDFKKRLLDTETGFIKRLRKAEGIKWSFHTRDYHVGYVREMVAGPTTPHSLRLYVYISNPLWHSQYRPGLVNFNKEWPFVNLWIKTGFMWDDIEKQNICIGGEVSPGWGPGMIGIAIKAFSCGERKIEATPVMIIRGEINPKKWCGDCWNLMCLRNSPPETLQRLAMLACGVQAKSWRGCCNQRFVSPYRTPADLEVIQSKPGWCMLWRGKL

vif

Virion infectivity factor

251 amino acids

Determines virus infectivity.

Belongs to the feline lentivirus group Vif protein family.

29.196 kDa

MSDEDWQVSRRLFAVLQGGVYSAMLYISSLPEMEQDKCKRSFKKRLSEKETGFIFRLRKAEGIRWSFHTRDYYIGYVREMVAGSSLPDSLRLYVYISNPLWHQSYRPGLTNFNTEWPFVNMWIKTGFMWDDIESQNICKGGEISHGWGPGMVGIVIKAFSCGERKIKITPVMIIRGEIDPTEWCGDCWNLMCLKYSPPNTLQRLAMLACGKEAKEWRGCCNQRFVSPFRTPCDLEVVQNKPKRNLLWTGEL

vif

Virion infectivity factor

238 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

28.169 kDa

MEREKLWVTRLTWRVSGEHIDKWKGIVKYHMRNRLQDWTYLMHYQCGWAWYTCSRFLIPLGGEGKIVVDCYWHLTPEQGWLSTYAVAISFENWQNTYKTEVTPDVADHMIHCHYFPCFTDRAIQQAIRGESFLWCTYKEGHVAENHWGQVRSLQFLALTVYTDFLRNGRRKRFQGKKTRMVRNLGSQQGAVGRMIKRHGSRTQSGSTTPFWERTPLPSMELLSGRRGKEWGTNDRKGL

vif

Virion infectivity factor

235 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

27.571 kDa

MNPNKEWVMRVTWKVPGDLITKWQGIVRYWMRQRNLKWNYYMHYQITWAWYTMSRYVIPIGKHGEICVDLYWHLTPEQGWLSTYAVGIQYVSNLESKYRTELDPATADSIIHGHYFNCFKERAIQQALRGHRFVFCQFPEGHKSTGQVPSLQYLALLAHQNGLRERSKRGKTRRSRNLGSKQGAVGQMAKRYVTRSQPGGEAAFWERTPVPSMELLSGGRRKTWYSHDGKGLQIL

vif

Virion infectivity factor

232 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

27.193 kDa

MSQEKHWVMRLTWKVQEEVITKWQGIVRYWMNKRNLKWEYKMHYQITWAWYTMSRYVIPLPGSGEIHVDIYWHLAPKQGWLSTYAVGIQYVSLVNDKYRTELDPNTADSMIHCHYFTCFTDRAIQQALRGNRFIFCQFPGGHKLTGQVPSLQYLALLAHQNGLRKRSQRGETRRTRNLGSQQGAVGRMAQRYGRRNQQRSQTAFWPRTPIPSMELLSGGRGETGKTHSGKGI

vif

Virion infectivity factor

232 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

27.378 kDa

MNQEKEWVMRVTWKVPEELITKWQGIVRYWMRTRKLDWKYRMHYQITWAWYTMSRYEIPLGQHGSIHVDLYWHLTPEKGWLSTYAEGIQYLSNRDPWYRTELDPATADSLIHTHYFTCFTERAIRKALLGQRFTFCQFPEGHKKTGQVPSLQYLALLAHQNGLRQRSQRSKTGGTRNMGFEQGAVGRMAKRHARRYQSGSQDAFWARAPVPSMELLSGGGRKESHSHARKGL

vif

Virion infectivity factor

230 amino acids

Belongs to the ovine/caprine lentivirus group Vif protein family.

28.139 kDa

MLSSYRHQKKYKKNKAREIGPQLPLWAWKETAFSINQEPYWYSTIRLQGLMWNKRGHKLMFVKENQGYEYWETSGKQWKMEIRRDLDLIAQINFRNAWQYKSQGEWKTIGVWYESPGDYKGKENQFWFHWRIALCSCNKTRWDIREFMIGKHRWDLCKSCIQGEIVKNTNPRSLQRLALLHLAKDHVFQVMPLWRARRVTVQKFPWCRSPMGYTIPWSLQECWEMESIFE

vif

Virion infectivity factor

230 amino acids

Belongs to the ovine/caprine lentivirus group Vif protein family.

28.015 kDa

MLSSYRHQKKYKKNKAREIGPQLPLWAWKETAFSINQEPYWYSTIRLQGLMWNKRGHKLMFVKENQGYEYWETSGKQWKMEVRRDLDLIAQINFRNAWQYKSQGEWKTIGVWYESPGDYKGKENQFWFHWRIALCSCNKTGWDIREFMIGKHRWDLCKSCIQGEIVKNTNPRSLQRLALLHLAKDHVFQVMPLWRARRVTVQKFSWCRSPMGYTIPWSLQECWEMESIFE

vif

Virion infectivity factor

230 amino acids

Belongs to the ovine/caprine lentivirus group Vif protein family.

28.139 kDa

MLSSYRHQKKYKKNKAREIGPQLPLWAWKETAFSINQEPYWYSTIRLQGLMWNKRGHKLMFVKENQGYEYWETSGKQWKMEIRRDLDLIAQINFRNAWQYKSQGEWKTIGVWYESPGDYKGKENQFWFHWRIALCSCNKTRWDIREFMIGKHRWDLCKSCIQGEIVKNTNPRSLQRLALLHLAKDHVFQVMPLWRARRVTVQKFPWCRSPMGYTIPWSLQECWEMESIFE

vif

Virion infectivity factor

230 amino acids

Belongs to the ovine/caprine lentivirus group Vif protein family.

28.139 kDa

MLSSYRHQKKYKKNKAREIGPQLPLWAWKETAFSINQEPYWYSTIRLQGLMWNKRGHKLMFVKENQGYEYWETSGKQWKMEIRRDLDLIAQINFRNAWQYKSQGEWKTIGVWYESPGDYKGKENQFWFHWRIALCSCNKTRWDIREFMIGKHRWDLCKSCIQGEIVKNTNPRSLQRLALLHLAKDHVFQVMPLWRARRVTVQKFPWCRSPMGYTIPWSLQECWEMESIFE

vif

Virion infectivity factor

229 amino acids

Determines virus infectivity.

28.051 kDa

MQNSSRHQQKKRNKKPGPELPLALWIHIAESINGDSSWYITMRLQQMMWGKRGNKLQYKNEDREYENWEITSWGWKMHLRRVKQWIQDNRRGSPWQYKVGGTWKSIGVWFLQAGDYRKVDRHFWWAWRILICSCRKEKFDIREFMRGRHRWDLCKSCAQGEVVKHTRTKSLERLVLLQMVEQHVFQVLPLWRARRSSTTDFPWCRDTTGYTHAWSVQECWLMEYLLEDE

vif

Virion infectivity factor

228 amino acids

Belongs to the ovine/caprine lentivirus group Vif protein family.

28.027 kDa

MLSSYRNQKKYKQNKIREVGPQLPLWAWKEIAFSINQEPYWYSTIRLQGLMWNKRGHKLIFVKEENGYEYWETTNKQWRMELRRDLRLIAQINFRNAWQYKSQEKWNIIGIWYDSPGEYRDKEKQFWFHWRIAMCSCKKERWDIRDFMVGKHRWDLCKSCIQGEIVRHTEPRSLQRLALLHIVRNHVFQIMPLWRARRVTVQRFPWSGTEGLYDTLVYTGLLGHGINI

vif

Virion infectivity factor

219 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

26.087 kDa

MEREKQWIVRVVWRVSERQISRWRGIVTYKIRNKQLPWEYRHHWQVQWQFWTYSQFIIPLSKDDYIEVNIYHNLTPERGWLSSHGVGLSYYHQKGYKTEVDPGTADRMIHLYYFNCFTDRAIQQAIRGEKYTWCTFKEGHKGQVQSLQLLALVAYTNGIRKRSKRTFTRMAGNLGSRQGAMGRMATRHAQGSKRRSQKALWNEHANPSMELLCRGGKET

vif

Virion infectivity factor

216 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.165 kDa

MEEEKDWIVVPTWRIPGRLERWHSLIKYLKYRTGELQQVSYVPHHKVGWAWWTCSRIIFPLNKGAWLEVQGYWNLTPERGFLSSYAVRLTWYERNFYTDVTPDVADQLLHGSYFSCFSANEVRRAIRGEKILSYCNYPSAHEGQVPSLQFLALRVVQEGKNGSQGESATRKQRRRNSRRSIRLARKNNNRAQQGSGQPFAPRTYFPGLAEVLGILA

vif

Virion infectivity factor

216 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.091 kDa

MEEEKNWIAVPTWRIPCRLERWHSLIKYLKYRTKDLQQVSYVPHHKVGWAWWTCSRVIFPLKEGAHLEVQGYWNLTPERGFLSSYAVRLTWYERSFYTDVTPDVADRLLHGSYFSSFTANEVRRAIRGEKILSHCNYPSAHTGQVPSLQFLALRVVQEGKDGSQGESTTRKQRRRNSRRGIRMARDNIRTSQQSSSQSLAQGTYFPGLAEVLGILA

vif

Virion infectivity factor

216 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.143 kDa

MEGEKNWIVVPTWRIPGRLEKWHSLVKYLKHRTKELQQVSYVPHHKVGWAWWTCSRVIFPLKEEAYLEVQGYWNLTPERGFLSSYAVRLTWYKRSFYTDVTPDVADQLLHGSYFSCFTANEVRRAIRGEKILSYCNYPSAHEGQVPSLQFLALRVIQEGKDGSQGESATRKQRRRNNRRSIRLARKNNNRAQQGSSQPLAPRTHFPGLAEVLGILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.312 kDa

MEEDRNWIVVPTWRVPGRMEKWHALVKYLKYRTKDLEEVRYVPHHKVGWAWWTCSRVIFPLQGKSHLEIQAYWNLTPEKGWLSSHAVRLTWYTEKFWTDVTPDCADILIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHKAQVPSLQYLALVVVQQNDRPQRKGTARKQWRRDHWRGLRVAREDHRSLKQGGSEPSAPRAHFPGVAKVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.321 kDa

MEEGKSWIAVPTWRVPGRMEKWHSLVKYLKYKTGDLEQVCYVPHHKVGWAWWTCSRVIFPLRGDSRLEIQAYWNLTPEKGWLSSYAVRMTWYTEKFWTDVTPDCADTLIHSTYFSCFTAGEVRRAIRGEKLLSCCKYPRAHRSQVPSLQFLALVVVQQNDRPQRDRTTRKQWRRDYRRGLRLARQDSRSYKQRGSESPAPGAYFPGVAKVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.101 kDa

MEEGKNWIVVPTWRVPGRMERWHSLVKHLKYRTKDLEEVRYVPHHKVGWAWWTCSRVIFPLEGESHLEIQAYWNLTPEKGWLSSHSVRLTWYTEKFWTDVTPDCADSLIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHKAQVPSLQYLALVVVQQNGRPQRKGAARKQWRRDHWRGLRVARQDYRSLKQGGSEPSAPRAHFPGVAKVLGILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.612 kDa

MEEGKNWIVPTWRVPGRRMERWHSLVKYLKYRTRDLEEVRYVPHHKVGWAWWTCSRVIFPLKGESHLEIQAYWNLTPEKGWLSSHSVRITWYTERFWTDVTPDYADILIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHKVQVPSLQYLALVVVQQNDRPQRKGTARKQWRRDHWRGLRVARQDYRSLKQRGSEPSAPRAHFPGVAKVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.133 kDa

MEEGERWIVVPTWRVPGRMEKWHSLVKYLKHRTKDLEGVCYVPHHKVGWAWWTCSRVIFPLQGNSHLEIQAYWNLTPEKGWLSSYAVRITWYTERFWTDVTPDCADSLIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHRSKVPLLQFLALVVVQQNGRPQKNSTTRKRWRSNYWRGFRLARKDGRGHKQRGSEPPASGAYFPGVAKVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.321 kDa

MEEGKRWIVVPIWRVPGRMERWHSLVKYLKYRTKDLEKVCYVPHHKVGWAWWTCSRVIFPLKENSHLEIQAYWNLTPEKGWLSSHSVRITWYTEKFWTDVTPDCADTLIHSTYFSCFTAGEVRRAIRGEKLLSCCKYPRAHRSQVPSLQFLALVVVQQNDRSQGNSATRKQRRGDYRRGLRMARQDSRGYKQRGSESPPTRAHFPGLAEVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.512 kDa

MEEDKRWIVVPTWRVPGRMEKWHSLVKYLKYKTKDLEKVCYVPHHKVGWAWWTCSRVIFPLKGNSHLEIQAYWNLTPEKGWLSSYSVRITWYTEKFWTDVTPDCADVLIHSTYFPCFTAGEVRRAIRGEKLLSCCNYPRAHRAQVPSLQFLALVVVQQNDRPQRDSTTRKQRRRDYRRGLRLAKQDSRSHKQRSSESPTPRTYFPGVAEVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.242 kDa

MDQGKRWIAVPTWRVPGRMEKWHSLIKYLKYRTKDLEQVRYVPHHKVGWAWWTCSRVIFPLKGNSHLEIQAYWNLTPEKGWLSSYSVRMTWYSEGFWTDVTPDCADTLIHSTYFSCFTAGEVRRAIRGEKSLSCCNYPQAHKSKVPSLQFLALVVVQQNDKPQRDNTTRKQWRRNYRRGLRLARQDGRSHKQRGSEPPAQGAYFPGVAKVLEILA

vif

Virion infectivity factor

215 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.355 kDa

MEEGKRWIAVPTWRVPGRMERWHSLIKYLKYRTGDLEKVCYVPHHKVGWAWWTCSRVIFPLKGESHLEIQAYWNLTPEKGWLSSYSVRLTWYTEKFWTDVTPDCADSLIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHKYQVPSLQFLALVVVQQNGRPQRDNTTRKQWRRNYRRGLRVARQDGRSHKQRGSEPPAPRAYFPGVAKVLEILA

vif

Virion infectivity factor

214 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.253 kDa

MEEEKRWIAVPTWRIPERLERWHSLIKYLKYKTKDLQKVCYVPHFKVGWAWWTCSRVIFPLQEGSHLEVQGYWHLTPERGWPSTYAVRITWYSRDLLDRCNTRLCRHFSCIALISLFTAGEVRRAIRGEQLLSCCKFPRAHRYQVPSLQYLALKVVSDVRSQGENPTWKQWRRDNRRGLRMAKQNSRGDKQRGGKPPTKGADFPGLAKVLGILA

vif

Virion infectivity factor

214 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.14 kDa

MEEEKNWIVVPTWRIPERLERWHSLIKHLKYNTKDLQMACYVPHHKVGWAWWTCSRVIFPLRDETHLEVQGYWNLAPEKGWLSTYAVRITWYSRNFWTDVTPDYADTLLHSTYFPCFSEGEVRKAIRGEKLLSCCKFPKAHKNQVPSLQYLALTVVSHVRSQGEDPTWKQWRRNNRKGLRMAKQNSRRNKQGSSKSPAEGANFPGLAKVLGILA

vif

Virion infectivity factor

214 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.125 kDa

MEEEKNWIVVPTWRIPGRLEKWHSLIKHLKYNTKDLQKACYVPHHKVGWAWWTCSRVIFPLKDEAHLEVQGYWNLTPEKGWLSTYAVRITWYSRNFWTDVTPDYADTLLHGTYFPCFSEGEVRRAIRGEKLLSCCKFPKAHKNQVPSLQYLALTVVSHVRSQGENPTWKQWRRNNRRGLRLARQNSRRNKQGSSESFAEGTNFPGLAKVLGILA

vif

Virion infectivity factor

214 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

25.329 kDa

MEEEKRWIVVPTWRIPERLERWHSLIKYLKYKTKDLQKACYVPHHKVGWAWWTCSRVIFPLQEGSHLEVQGYWNLTPERGWLSTYAVRITWYSKDFWTDVTPEYADILLHSTYFPCFTAGEVRRAIRGERLLSCCRFPRAHKHQVPSLQYLALRVVSHVRSQGENPTWKQWRRDNRRSLRVAKQNSRGDKQRGGKPPTEGANFPGLAKVLGILA

vif

Virion infectivity factor

198 amino acids

Determines virus infectivity.

22.828 kDa

MERTLQSVVGRRRGSSNRGRGKNSLISTPSYALHPPPRFRYPRWEFVRQTEYSMTACVRKGKLVLTYQYAIWKRVWTIETGFTDPSLFMTPAGTHTTEEIGHLDLFWLRYCSCPHEMPPWLDFLRGTLNLRISCRRALQASVLTSTPRHSLQRLAALQLCTNACLCWYPLGRINDTTPLWLNFSSGKEPTIQQLSGHP

vif

Virion infectivity factor

197 amino acids

Determines virus infectivity.

Belongs to the lentiviruses Vif protein family.

22.937 kDa

MERTIQSPMGRRRGSSGRRKRNANIISPPAYAIYPAPQYRYPRWEFVMNDLYSQTARLQKEEIIITYRYAVWAREWKIQTGFLDLGYLMTPAGTHTTGELNELDLFWVRYTLCQHRSPKWRELLLGEMTHTSCRRTAQAAVVSHTKPHTLQRLAGLTLVCNQNLCWYPVGTVTRNSPLWMHFTTGKEPTIQQLSGHP

vif

Virion infectivity factor

193 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

23.048 kDa

MENRWQVMIVWQVDRMRIKTWNSLVKYHIYRSKKARGWFYRHHYDHPNPKVASEIHIPFRDYSKLIVTTYWALSPGERAWHLGHGVSIQWRLGSYVTQVDPFTADRLIHSQYFDCFAETAIRRAILGQLVAPRCEYKEGHRQVGSLQFLALKALISERRHRPPLPSVAKLTEDRWNKHQRTKVHQENLTRNGH

vif

Virion infectivity factor

193 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.956 kDa

MENRWQVMIVWQVDRMRIRTWNSLVKHHMYVSRRAKGWFYRHHYESRHPKVSSEVHIPLEDDSKLVIITYWGLHTGERDWHLGHGVSIEWRQKRYRTQVDPDLADQLIHLRYFDCFSESAIRNAILGHRVSPRCNYQAGHNKVGSLQYLALTALITPKKIKPPLPSVRKLVEDRWNNPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

193 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.832 kDa

MENRWQVMIVWQVDRMKIRTWNSLVKHHMYISKRAAGWFYRHHYESRHPRVSSEVHIPLEEDSKLVIITYWGLHTGERDWHLGQGVSIEWRQKRYRTQVDPGLADQLIHLHYFDCFSDSAIRKAILGQRVSPRCNYQAGHNKVGSLQYLALTALITPKKIKPPLPSVRKLVEDRWNNPQKTRGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.725 kDa

MENRWQVMIVWQVDRMRIKTWNSLVKHHMYVSRKARNWFYRHHYESNNPKISSEVHIPLGEAKLVITTYWGLTTGERAWHLGHGVSIEWRQRSYRTQIDPDLADQLIHLYYFDCFAESAIRKAILGQIVSPRCEYPTGHNKVGSLQYLALSTLIKSKPRRPPLPSVRKLAEDRWNNSQKTRDHKGNHIMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.625 kDa

MENRWQVMVVWQVDRMRVRTWNSLVKHHMYVSKKARGWFYRHHYETDNPKISSEIHIPLGEAKLVIVTYWGLMPGERPWHLGHGVSIEWRQGIYRTQIDPELADKLIHLYYFDCFTASAIRQAVLGRPVIPKCEYPAGHKQVGSLQYLALIAWVGVQKRRPPLPSVTKLTEDRWNRHQKIKDHRGSHTTNGL

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.723 kDa

MENRWQVMIVWQVDRMRIRTWHSLVKHHMYVSKKAKNWFYRHHYESRHPKVSSEVHIPLGDARLVVRTYWGLQTGEKDWHLGHGVSIEWRQKRYSTQLDPDLADQLIHLYYFDCFSESAIRQAILGHIVSPRCDYQAGHNKVGSLQYLALTALIAPKKTRPPLPSVRKLTEDRWNKPQQTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.488 kDa

MENRRQVMIVWQADRMRIRTWKSLVKHHMYISKKAKGRFYRHHYESTHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADHLIHLHYFDCFSDSAIRKAILGHRVSPICEFQAGHNKVGPLQYLALTALITPKKIKPPLPSVKKLTEDRWNKPQKTKGHRGSHTINGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.657 kDa

MENRWQVLIVWQIDRQKVKAWNSLVKYHKYMSKKAANWRYRHHYESRNPKVSSAVYIPVAEADIVVTTYWGLMPGEREEHLGHGVSIEWQYKEYKTQIDPETADRMIHLHYFTCFTESAIRKAILGQRVLTKCEYLAGHSQVGTLQFLALKAVVKVKRNKPPLPSVQRLTEDRWNKPWKIRDQLGSHSMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.699 kDa

MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAIRNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.611 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIKWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRRSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.556 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMYVSKKANRWFYRHHYDSHHPKISSEVHIPLGEARLVVTTYWGLHTGEKEWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFAESAIRKAILGHIVSPSCEYQAGHNKVGSLQYLALAALIAPKKIKPPLPSVRKLTEDRWNKPQKTKGRRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.366 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSKKAKGWFYRHHYESTHPRISSEVHIPLGDATLVVTTYWGLHTGEREWHLGQGASIEWRKKRYSTQVDPGLADQLIHTYYFDCFSESAIRNAILGNIVSPRCEYPAGHNKVGSLQYLALAALIKPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.687 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISRKAKGWFYRHHYESTHPRISSEVHIPPGDERLVITTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPDLADQLIHLYYFDCFSESAIRKPSLGHIVSPRCEYQAGHNKVGSLQYLALAALTTPKKIKPPLPSVKKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.679 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMNVSKKARKWLYRHHYDSNHPKISSEVHIPLGEAILVITTYWGLQTGERDWHLGQGVSIEWRQRRYRTQVDPGLADQLIHMCYFDCFSDSAIRKAILGQIVSPRCDYQAGHNKVGSLQYLALTALIRPKRRKPPLPSVQKLVEDRWNKPQKTTGHRESHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.869 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMNVSKKARQWLYRHHYDSRHPKISSEVHIPLGEARLVVTTYWGLQTGERDWHLGQGVSIEWRRKRYRTQVDPGLADQLIHMHYFDCFSDSAIRKAILGQIVSPRCDYQAGHNKVGSLQYLALTALIKPKRRKPPLPSVQKLVEDRWNKPQKTRDHRESHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.663 kDa

MENRWQVMIVWQVDRMRIRTWHSLVKHHMYVSKKARGWFYRPHYASRHPRVSSEVHIPLGDATLVVTTYWGLHTGEKDWQLGHGVSIEWRQRRYRTQVEPDLADHLIHLHYFDCFSDSAIRKAILGQIVSPRCEYQAGHNQVGSLQYLALKVLVTSKRSRPPLPSVTELAEDRWNKPQKTRGHRENPTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.798 kDa

MENRWQVMIVWQVDRMKIRTWNSLVKHHMYVSKKAQGWFYRHHYESRHSRVSSEVHIPLGEARLVVRTYWGLHTGEKDWHLGHGVSIEWRLKRYSTQVDPDLADHLIHLHYFDCFSESAIRRAILGQIVRPRCEYQAGHNKVGSLQYLALKALVTPTRAKPPLPSVKKLTEDRWNKPQKTRGHRGSRTLNRH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.589 kDa

MENRWQVMIVWQVDRMRIKTWNSLVKHHMYVSKKAKKWVYRHHYESTNPKTSSEVHIPVGDARLVITTYWGLHTGERDWHLGHGVSIEWRQERYSTQIDPDLADQLIHLHYFDCFSDSAIRKAILGHRVSPICDYQAGHRKVGSLQYLALTALISPKRTKPPLPSVRKLVEDRWNKPQKTRGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.629 kDa

MENRWQLMIVWQVDRMRINTWKSLVKYHMYVSKKAKGWSYRHHFQSRHPRVSSEVHIPLEEVKLVITTYWGLHPGEREWHLGQGVSIEWRQGKYRTQIDPGLADQLIHIYYFDCFSESAIRKAILGHRISPRCNYQAGHNKVGSLQYLALTALIAPEKTKPPLPSVQKLVEDRWNKPQETRGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.602 kDa

MENRWQVMIVWQVDRMRIRAWKSLVKHHMYISGKARGWFYRHHYESPHPRISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLYYFDCFSESAIRKAILGYRVSPRCEYQAGHNKVGSLQYLALTALITPKKTKPPLPSVKKLTEDRWNKPQKTKGHRGSRTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.349 kDa

MENRWQVMVVWQVDXMKIRTWNSLVKHHMYVSKKAKGWYYRHHYETKHPKTSSEVHIPVGXAXLVIVTYWGLTTGEQPWHLGHXVSIEWRQGKYKTQVDPEMADKLIHCYYFNCFTASAIRQAVLGRPVLPRCXYPAGHXQVGTLQYLAXTAXVGVKKRRPPLPSVTKLTEDRWNERQKTQGHRGNPIMNGP

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.603 kDa

MENRWQVMVVWQVDRMKIRKWNSLVKHHMYVSKKAKGWYYRHHYETHHPKISSEVHIPVGQARLVTVTYWGLTTGEQSWHLGHGVSIEWRLRKYKTQVDPEMADKLIHLHYFDCFTASAIRQAVLGRPVLPRCEYPAGHKQVGTLQYLALTAWVGAKKRKPPLPSVTKLTEDRWNEHQKMQGHRGNPIMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.572 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSKKASRWFYRHHYDSPHPKISSEVHIPLGEAMLVVKTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFSEAAIRKAILGHIVSHRCEYQAGHSKVGSLQYLALTALVAPKKIKPPLPSVRKLTEDRWNKPQKTKGHKGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.513 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.633 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMHISRKARGWFYRHHFESTHPRISSEVHIPLGEARLVITTYWGLNTGEREWHLGQGVSIEWRLKRYSTQVEPGLADQLIHMHYFDCFSESAIRKAILGRVVRPRCNYPAGHKQVGTLQYLALTALVAPKKIKPPLPSVRKLVEDRWNKPQKTRGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.762 kDa

MENRWQVLIVWQVDRMKIRTWNSLVKHHMYVSRRASGWYYRHHYESRHPKISSEVHIPLGEARLVIITYWGLQTGERDWHLGHGVSIEWRLRRYSTRVDPGLADQLIHMHYFDCFADSAIRKAILGHRVSSRCDYQAGHNKVGSLQYLALTALIKPKKIKPPLPSVKKLVEDRWNKPQKTRDRRGNHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.641 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMHISKKAKGWFYRHHFESRHPKISSEVHIPLETAELVITTYWGLLPGEREWHLGQGVSIEWRQGRYRTQIDPGLADQLIHIYYFDCFSESAIRKAILGHKISPRCNYQAGHNKVGSLQYLALTALIAPKKTKPPLPSVQKLVEDRWNKPQKTRGHRESHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.688 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMHISKKANRWYYRHHYESRHPKISSEVHIPLGDAELVVTTYWGLLTGERDWHLGQGVSIEWRLKRYRTQVEPDLADQLIHIYYFDCFSESAVRKAILGHRVSPRCECQAGHNKVGSLQYLALTALVAPRRPKPPVPSVKKLVEDRWNKPQKTRGHRGSQTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.571 kDa

MENRWQVMIVWQVDRMRINTWKSLVKYHMYVSKKANRWRYRHHYDSNHPKISSEVHIPLGDAELVVTTYWGLHTGEREWHLGQGVSIEWRLKKYRTQVDPGLADQLIHIYYFDCFSESAIRKALLGHRVSPRCEYQAGHTQVGSLQYLALTALIAPKKTKPPVPSVQKLVEDRWNKPQKTRGHRGSHTMSGQ

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.685 kDa

MENRWQVVIVWQVDRMRIRTWNSLVKHHMYVSKKAKGWFYRHHYESRHPRVSSEVHIPLRDATLVVRTYWGLHAGEKDWQLGHGVSIEWRQKRYSTQIDPNTADHLIHLYYFDCFSESAIRKAILGEIVSPRCEYPAGHNKVGSLQYLASKALVTPTRKRPPLPSVGKLAEDRWNKPQKTRDHRENPTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.46 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISKKAKGWFYRHHYESTHPRVSSEVHIPLGDAKLVITTYWGLHTGEREWHLGQGVAIEWRKKKYSTQVDPGLADQLIHLHYFDCFSESAIKNAILGYRVSPRCEYQAGHNKVGSLQYLALAALITPKKTKPPLPSVKKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.742 kDa

MENRWQVLIVWQVDRQKVKAWNSLVKYHKYRSRKTENWWYRHHYESRNPRVSSSVYIPVGVAHVVVTTYWGLMPGERDEHLGHGVSIEWRYKKYKTQIDPETADRMIHLHYFTCFTASAVRKAILGQRVLTKCEYPTGHSQVGTLQLLALRAVVKARSRKPPLPSVQKLTEDRWNKHLRIRDQLKSPSMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.513 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.52 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHRMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPELADQLIHLHYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKVKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.346 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISGKAKGWSYRHHYESTNPRISSEVHIPLGDAKLVVTTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPGLADRLIHLYYFDCFSDSAIRKSILGHIVSPSCEYQAGHNKVGSLQYLALAALTTPRRIKPPFPSVTKLTEDRWNKPQKTKGHRGSHTMTGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.513 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.689 kDa

MENRWQVMIVWQVDRMRIKTWKSLVKHHMYVSKKANRWFYRHHYESPHPKISSEVHIPLGEARLVIKTYWGLHTGEREWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFSESAIRKAILGDIVSPRCEYQAGHNKVGSLQYLALTALIAPKQIKPPLPSVRKLTEDRWNKPQQTRGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.534 kDa

MENRWQVLIVWQVDRMKIRTWNSLVKHHMHISRRANGWVYRHHYDSRHPKVSSEVHIPLGEARLIIKTYWGLQTGERDWHLGHGVSIEWRLRSYNTQVDPGLADHLIHMHYFDCFAESAIRKAILGYRVSPRCDYQAGHNKVGSLQYLALTALIKPKKAKPPLPSVSKLVEDKWNKPQKTRGRRGNHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.513 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

192 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.443 kDa

MENRWQVMIVWQVDRMRIRTWNSLVKHHMYISGKAKGWIYKHHYESTNPRVSSEVQIPLGDARLVITTYWGLHTGERDWHLGQGVSMEWRTRRYSTQVDPDLADQLIHLYYFDCFSESAIRNAILGHIVSPRCEYQAGHSKVGSLQYLALTALIKPKKIKPPLPSVKKLTEDRWNKPQKTKGHRGSHTMNGH

vif

Virion infectivity factor

188 amino acids

Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.

Belongs to the primate lentivirus group Vif protein family.

22.159 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSKKASRWFYRHHYDSPHPKISSEVHIPLGEARLVVKTYWGLHTGERDWHLGQGVSIEWRKRRYSTQVDPGLADQLIHMYYFDCFSEAAIRKAILGHIVSHRCEYQAGHSKVGSLQYLALTALIAPKKIKPPLPSVRKLTEDRWNKPQKTKGHKGAIQ

vif

Virion infectivity factor

172 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity).

Belongs to the primate lentivirus group Vif protein family.

20.499 kDa

MERVERIVRLTWKVSSQRIEKWHWLVRRQMAWATANNEEGCWWLYPHFMAYNEWYTCSKVVIIINRDIRLIVRSYWHLQIEVGCLSTYAVSIEAVVRPPPFEKEWCTEITPEVADHLIHLHFYDCFMDSAVMKAIRGEEVLKVCRFPAGHKAQGVLSLQFLCLRVIYGPEER

vif

Truncated virion infectivity factor

132 amino acids

Counteracts the innate antiviral activity of human APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells (By similarity).

Belongs to the primate lentivirus group Vif protein family.

15.854 kDa

MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPR

vif

Virion infectivity factor

109 amino acids

Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology. Interacts with host ABCE1, which seems to be involved in lentiviruses capsid formation and displays RNase L inhibitor activity. This interaction may play a role in protecting viral RNA from damage during viral assembly. May interact with host SAT, which is a regulator of polyamine cell level. This interaction may be relevant since polyamines affect viral RNA properties (By similarity).

Belongs to the primate lentivirus group Vif protein family.

12.308 kDa

single

GVSIEWTKKRYSTQVDPDLADRLIHLYYFDCFSESAIRNAILGALVSGRCEYQAGHNKVGSLQYLALTALITPKKTKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH