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CCT4

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Bos taurus
Length
542 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.206 kDa
Sequence
MPENVAPRTGPPAGAAGAAGGRGKSAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPEELSDRETLLNSAATSLNSKVVSQYSSLLSPMSVDAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYVQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHVDQFTADMLGSAELAEEVSLNGSGKLIKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCIRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEQVVQPLLVSVSALTLATETVRSILKIDDVVNTR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Homo sapiens
Length
539 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.924 kDa
Sequence
MPENVAPRSGATAGAAGGRGKGAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVVNTR

Gene
Cct4
Protein
T-complex protein 1 subunit delta
Organism
Mus musculus
Length
539 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.066 kDa
Sequence
MPENVASRSGAPTAGPGSRGKSAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVSLNGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Pongo abelii
Length
539 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.896 kDa
Sequence
MPENVAPRSGATAGAAGGRGKGAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVASQYSSLLSPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVVNTR

Gene
Cct4
Protein
T-complex protein 1 subunit delta
Organism
Rattus norvegicus
Length
539 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.099 kDa
Sequence
MPENVASRSGPPAAGPGNRGKGAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLNGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Arabidopsis thaliana
Length
536 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.775 kDa
Sequence
MAAVAAPMASKPRGSKAESFVDNKRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVLSVIDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAAGGPTRVENAKIAVIQFQISPPKTDIEQSIVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVTVR

Gene
cct4
Protein
T-complex protein 1 subunit delta
Organism
Takifugu rubripes
Length
536 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.716 kDa
Sequence
MPEGKATSSASNTGKNKGGAYQDRDKPAQIRYSNISAAKAVADAVRTSLGPKGMDKMIQDEKGDVTITNDGATILKQMQVLHPSAKMLVELSKAQDIEAGDGTTSVVVIAGALLDSCNRLLQRGIHPTIISESFQKAVDKGVEVLTAMSQPVQLGDRETLLNSATTSLCSKVVSQYSSLLAPMSVDAVMRVIDPATATSVDLHDIKIIKKLGGTIDDCELVEGLVLTQRVANSSVSRVEKAKIGLIQFCLSPPKTDMDNQIVVSDYTQMDRVLREERAYILNMVKQIKKAGCNVLFIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPIAHIDHFTPEMLGTAELAEEVSLDGSGKLVKITGCASPGKTVSIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAVRLAEYSRTLGGMEAYCVRAYSDALEVIPSTLAENAGLNPISTVTELRNRHAQGDKMAGINVRKGGISNIMEELVVQPLLVSISALTLATETVRSILKIDDVVNAR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
Length
533 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.629 kDa
Sequence
MAQSQVGKGSPSNATFRDKEKPQEVRKSNILAARAVSDAIRTSLGPKGMDKMIKTKNGEIIISNDGATILKHMAVLHPAARMLVDVSAAQDVEAGDGTTSVAILTGSLLGAAEKLLNKGIHPTLISESFQRAATRSAEVLLEMSHKISLDDKEALIRAASTSLSSKIVSQHSSLLSPLAVNSVLKVMNEEHTNVDLNDIRLIKKVGGTIDETELVNGVVLTQNVVKTAGGPVRVDKAKIALIQFQLSPPKPDMENNVVVNDYRQMDKILKEERAYLLNICKKIKKSKCNVLLIQKSILRDAVNDLALHFLSKLNIMVIKDIERDEIEFLSKATGCKPIADIDNFTEDRLGSADVVEEIESSGSRIVKIDGVSAKNVKPTVSIVCRGANQLVLDETERSIHDALCVVRCLVKEKALIAGGGAPEIEVSRVLMSEANKLSGVEQFVYQEFAQALEVIPTTLAENAGLNSINVVTDLRNRHANGEKNAGISVRRSGASNTYDEHVLQPVLVSSSAITLASECVKSILRIDDIAFSR

Gene
cct4
Protein
T-complex protein 1 subunit delta
Organism
Dictyostelium discoideum
Length
533 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
56.918 kDa
Sequence
MSAPAAAPAKVLPSRSDFDEKEKEKDVRTSNIVAARAVADAIRTSLGPKGMDKMIISPNNEVLISNDGATILQNLELRHPAAKMLAELAKAQDIEAGDGTTSVCVIAGSLLGAVSQLMAKGIHPSIISEAFNLALNKSLEVLVSMSVPVSLTDRVSLVKSATTSLNSKVVSQYTNLASIAVDAVLSVINPATAVNVNLKDIKLIKKLGGTIEDTELVQGLVFDQTASHTAGGPTRIQNAKIGLIQFCLSAPKTYMDNNIVVSDYSKMDKVIKEEPKLILEMCRKIQKSGCNVLLVQKSILRDAVNDLSLHYLAKLKILVIKDIERDDIEFICNTIGCQPVANIDSFTADKLGKADLVEEVGTSDGKIVKVTGIPNPGKTVTVLCRGSNKLVLDEAERSLHDALCVIRSLVKKKFLIAGGGAPEIEVSQQVTAFSKTLTGITSYCVRAYAEALEIIPYTLAENAGLHPISIVTELRNKHAQGEINSGINVRKGAITNILQENVVQPLLVSTSALTLATETVVMLLKIDDIATAR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Length
530 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.695 kDa
Sequence
MVSQAKQPSNATFKNREKPQEVRKANIIAARAVADAIRTSLGPKGMDKMIKTSRGDIIISNDGHTILKQMAILHPVAKMLVEVSGAQDVEAGDGTTSVVIMTGALLGAAEKLLNKGIHPTIIAESFQRAAERSVEILLNMSTKISLDDKEALVRAASTSLSSKIVSQHSSFLAPLAVDCVLSIASHDSTNVDLNDIRLIKKVGGTIDDTEMVNGVVLTQNAVKTAGGPTRIEKARIGLIQFQISPPKPDTENNIVVNDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSKLGIMVVRDIERDEVEFLSKSLGCKPISDVELFTEDRLGSADVVEEVESDGSNIVTITGVKTTNKNPTVSVVIRGANNMVLDETERSLHDALCVIRCLVKERALIAGGGAPEIEVSYRLMKEARTMEGVEAFVWQEYAEALEVIPTTLAENAGLNSLNVVTELRLRHENGESNSGISVRRSGTSNTYEDHILQPVLVSTSAIRLASECVKSILRIDDITFSR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
Length
529 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.361 kDa
Sequence
MPPKVSASNATFKNREKPQEVRKANIIAARAVADAIRTSLGPKGMDKMIKTARGEILISNDGHTILKQMAILHPVAKMLVEVSAAQDSEAGDGTTSVVILTGALLGAAEKLLAKGIHPTIIAESFQRAGQRAVEVLLGMSKRISLQDRAELVRAASTSLSSKIVSQYSTFLAPLAVDCVLSLTNEASTNVDLNDIRLVKKVGGTIDDTEMVDGVVLTQNIVKSAGGPVRMEKAKIGLIQFQISPPKPDTENNIVVNDYRQMDKILKEERAYLLKICKKIKKAKCNVLLIQKSILRDAVNELALHFLSKLNIVVIKDVERDEIEFLSKSLGCKPISDVELFTEDRLGSADLVEEIDSDGTKIVKITGIKTGNAKPTVSCIVRGANNVVLDETERSLHDALCVIRCLVKERALIAGGGAPEIEVSRTIMRESRAMQGVEAFVWQEFAEALEVIPTTLAENAGLNSIKVVTELRSRHESGETNAGISVRRSGTTNTYDEHILQPVLVSTSAITLAAECVKSILRIDDITFSR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Length
529 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.645 kDa
Sequence
MVAQKSVSNATFKNKEKPQEVRRANIVAARAVADAIRTSLGPKGMDKMIKTSRGEIIISNDGHTILKQMAILHPVAKMLVDVSAAQDSEAGDGTTSVVILTGALLGAADRLLNKGIHPTIIAESFQKAARRSVETLLEICHPVSLDDREDLIRAASTSLSSKIVSQYSSFLSPLAVDAVLSITEKDSKTVDLNDIRLVKKVGGTIGDTEMVDGVVLTQTVVKTAGGPTMKEKAKIGLIQFQISPPKPDTENNIVVSDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLAKLGIMVIKDIEREEIEFLSKSLGCKPISDVELFTEDRLGSADLVEEIDSDGTKIVKFSGVKGVNAKPTVSVIIRGANSMILDETERSLHDALCVIRCLVKERGLIAGGGAPEIEISRRLERESRSMEGVEAYIWQEFAQALEVIPTTLAENAGLNSIKVITELRSRHENGDVNEGISVRRSGTTNTYEEHILQPVLVSTSAITLASECVKSILRIDDITFSR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
528 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.604 kDa
Sequence
MSAKVPSNATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGEIIISNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALLGAAERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAASTSLSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTIDDTEMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIVNDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSKLNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLGSADLVEEIDSDGSKIVRVTGIRNNNARPTVSVVIRGANNMIIDETERSLHDALCVIRCLVKERGLIAGGGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTLAENAGLNSIKVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVSTSAITLASECVKSILRIDDIAFSR

Gene
cct4
Protein
T-complex protein 1 subunit delta
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
527 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
56.968 kDa
Sequence
MSKAATVPVAFQDREKPQEVRLSNIMAARSVADAIRTSLGPKGMDKMIQTGKGEVILTNDGATILKHLSVLHPAAKMLVDLSAAQDVEAGDGTTSVVILAGSMLACAEKLLKKGIHPTVIAESFQRAAGFTVDCMKENALAIELSDRESLLRAATTSLNSKIVSQYSNLLAPIAVDAVLKVIDPRVATNVDLKDIRIVKKLGGIIDDTELIPGLALTQTAVKSAGGPTRIEKANIALIQFQLSPPKPDMENQVVVNDYRQMDKILKEERQYLLNMCKKIKKAGANVILIQKSILRDAVNDLALHFLAKLKIMVIKDIERDEVEFICKSTGCKPIADIESFAEDKLGHADLVEETSSSGEKIVKFSGVKNAGKTVSILCRGANLLTLEEAERSLHDALCVIRCLVKQRALIAGGGSPEIEAAQRLLEHARQLEGREAICIRAFSEALEIIPVTLAENAGLNAIQVVTELRSRHANGEKTAGINVRKGIVTNILEENVLQPLLVNISAIQLAAETTKMIMKIDDITLAR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Yarrowia lipolytica (strain CLIB 122 / E 150)
Length
527 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
56.483 kDa
Sequence
MSVPTGTKSGFKNKEKPLEVRKSNILAARAVADAIRTSLGPKGMDKMIQTARGQVIISNDGNTILQHMAVMHPAAKMLVDLSASQDSVAGDGTTSVVILAGSLLGAADKLLKKGIHPSIIAENFQKAAQRAAEVVMDMSKPIDLSDRETLIRAASTSLNSKIVSQFSSTLAPMLVDAALQAAKKTPEGGLTLDLNDIRIIKSLGGTIEDTTLANGLVLNNYAVKNAGGPSRMEKAKIGLIQFQLSAPKPDMENHIVVNDYRQMDKILKEERQYILGLAKAIKKSKCNVLLIQKSILRDAVSELALHFLAKLNIMVIKDIERDDIEFISRSTGAKPVADIEAFTEDKLGSCDLVEEVESSGSKTVRFSSREGSNTVSILVRGANDLVIDETERSLHDALCVLRSLFRVPALVPGGGACEVQVAQVIGKESRAMDGASAICYEEFSNAMLVIPTTLAENAGLNPVNVVTELRVRHEKGEVNAGISVRRGTSIMVEEHVIQPALVTTSAITLAAECAKGLLRIDDIAFSR

Gene
CCT4
Protein
T-complex protein 1 subunit delta
Organism
Encephalitozoon cuniculi (strain GB-M1)
Length
484 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
52.842 kDa
Sequence
MATERLNQVRTSVFQASQSLLQTLSTSLGPRGLDKMVVKDKKTVVTNDGATILKYLNHHPIHGILSSMSATQDEECGDGTTSVVILAGCLLESISSLLERNVHPSVICDNLEIAKKIGLRYIDRVKMECSEKDLISNVTTALCSKIASSTGEMAVEAIRGMEYVNGDKKNIRVVKKIGGNLDDVKAYKSILLECDLKDIPKKAKVGVIQFCLSAPKTNMDSKILINDPALMEKIIQDERKYILEMCKKIKKSGCTLLVVQKSILRESLSDLASHFLKQLNILVVNSVDRKDVDYICSAMNIQPVSEVDLLSPASLVDVETGEVEGMLEIKGYGCTILLRGCDDMVVEEAERSLNDALCVVKCLKELPFLVPGGGSIEMGIALMLSESTEGNIYVLREIAKAFEGVPYFLARNAGLYPVEIVSELRSELKQNCCAGISVRSGHAGDMVRDDSVVQPAKVSISVVTLALETVSMILKIDDILPARR