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EFT1

Gene
EFT1
Protein
Elongation factor 2
Organism
Encephalitozoon cuniculi (strain GB-M1)
Length
850 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
94.474 kDa
Sequence
MADFHISKVHELMMNQKNIRNISVIAHVDHGKSTLTDCLVIKAKIVSKDSGGGRYMDSREDEQQRGITIKSSAISLHFQVQKDVLEAYTKEGDTNGTEFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVDGICVQTETVLGQAMNERIIPTLVLNKLDRAILELEYPQEKLGEVLRRRVEGFNAKLSTLGYNFKVESLLPEKNEISFCSGLQGWGFTLRQFARFYLEKFNMNGFEGERKLTNFLWSHKVSCTSDDPFDASIKHIAKPNPARSPFVVYVLNPIYKVKELCNNGKVEEIKEYLKFYKVDFKGVVLTGSGKSLFKEVMKTWLPAADCILEQIALKLPSPLQSQKLRYDYLYEGPADDEVANAIKMCDGSDEAPVSMYVSKMIPSNDNRFIAFGRVFSGKIFPGMKIRVQEPGYSPGSEELSNTSLIHNKSVLRTVVMMGRGYKDVPNCPAGNIIGIIGIDDCLKKTGTITNREAAHNIRSMKFSVSPVVKVAVSAKRPEDLGKLQEGLNKLAQSDPLCVVERNDKGQNTIACAGSLHLEICLKDLQDQYAKVPIIADDPLVTYFEGISCAVSDSKMTKSANKHNRIYMTVEPLDQNIVDNLKDVKSDQAKTMATNFREKLDIRDDWIRKIWCYAPEVNPLNLLVDGTKGISIINEIKEHVNTGFRAAVNDGPLIGEVMRGLKFELKDAVLHADAIHRGINQLLQPVKNLCKGLLLAAGPILYEPIYEVEITTPNDYSGAVTTILLSKRGTAEDFKTLPGNDTTMITGTLPVKESFTFNEDLKSGSRGKAGASMRFSHYSILPGNLEDPNSLMFKTVEAVRKLKKMNPAPPTPDSFFDRL

Gene
EFT1
Protein
Elongation factor 2
Organism
Naumovozyma castellii (strain ATCC 76901 / CBS 4309 / NBRC 1992 / NRRL Y-12630)
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.172 kDa
Sequence
MVAFTVDQMRSLMDTVTNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGEARFMDTRKDEQERGITIKSTAISLYSEMPDEDVKDIAQNTEGNAFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVCINKVDRALLELQVSKEDLYQSFSRTVESVNVIISTYADEILGDVQVYPSKGTVAFGSGLHGWAFTIRQFAQRYAKKFGVDKVKMMERLWGDSYFNPKTKKWTNKETDADGKQLERAFNMFVLDPIFRLFAAIMNFKKDEIPVLLEKLEINLKGDEKDQEGKALLKTVMKKFLPAADALLEMIVMNLPSPVTAQAYRAEQLYEGPADDANCMAIKRCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVRSGQKVRIQGPNYVPGKKDDLFVKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKSGTLTTDETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMAETGEHIVAGTGELHLEICLQDLENDHAGVPLKISPPVVAYRETVETESSQTALSKSPNKHNRIYLKAEPIEEEVSLAIESGKINPRDDLKARARVMADEFGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGEQMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLAEPKIQEPVFLVEIQCPESAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWATLGSDPLDPTSKAGEIVTAARKRHGMKEVVPGWQEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Komagataella pastoris
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.469 kDa
Sequence
MVNFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLYSEMGDDDVKEIKQKTEGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVTKEDLYQSFARTVESVNVVIATYTDKTIGDNQVYPEQGTVAFGSGLHGWAFTVRQFATRYSKKFGVDRIKMMERLWGDSYFNPKTKKWTNKDKDAAGKPLERAFNMFVLDPIFRLFAAIMNFKKDEIPVLLEKLEINLKREEKELEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAETLYEGPSDDQFCIGIRECDPKAELMVYISKMVPTSDKGRFYAFGRVFSGTVKSGQKVRIQGPNYVPGKKEDLFIKAVQRTVLMMGRTVEPIDDVPAGNILGIVGIDQFLLKSGTLTTNEAAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYISESGEHIVAGTGELHLEICLQDLQDDHAGVPLKISPPVVTYRETVTNESSMTALSKSQNKHNRIYLKAQPIDEELSLAIEEGKVHPRDDFKARARIMADEYGWDVTDARKIWCFGPDGTGANLVVDQSKAVQYLHEIKDSVVAGFQLATKEGPILGENMRSVRVNILDVTLHADAIHRGGGQVIPTMKRVTYAAFLLAEPAIQEPIFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYLPVNESFGFTGELRQATAGQAFPQMVFDHWANMNGNPLDPASKVGEIVLAARKRQGMKENVPGYEEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Naumovozyma castellii (strain ATCC 76901 / CBS 4309 / NBRC 1992 / NRRL Y-12630)
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.172 kDa
Sequence
MVAFTVDQMRSLMDTVTNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGEARFMDTRKDEQERGITIKSTAISLYSEMPDEDVKDIAQNTEGNAFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVCINKVDRALLELQVSKEDLYQSFSRTVESVNVIISTYADEILGDVQVYPSKGTVAFGSGLHGWAFTIRQFAQRYAKKFGVDKVKMMERLWGDSYFNPKTKKWTNKETDADGKQLERAFNMFVLDPIFRLFAAIMNFKKDEIPVLLEKLEINLKGDEKDQEGKALLKTVMKKFLPAADALLEMIVMNLPSPVTAQAYRAEQLYEGPADDANCMAIKRCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVRSGQKVRIQGPNYVPGKKDDLFVKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKSGTLTTDETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMAETGEHIVAGTGELHLEICLQDLENDHAGVPLKISPPVVAYRETVETESSQTALSKSPNKHNRIYLKAEPIEEEVSLAIESGKINPRDDLKARARVMADEFGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGEQMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLAEPKIQEPVFLVEIQCPESAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWATLGSDPLDPTSKAGEIVTAARKRHGMKEVVPGWQEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Komagataella pastoris
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.469 kDa
Sequence
MVNFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLYSEMGDDDVKEIKQKTEGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVTKEDLYQSFARTVESVNVVIATYTDKTIGDNQVYPEQGTVAFGSGLHGWAFTVRQFATRYSKKFGVDRIKMMERLWGDSYFNPKTKKWTNKDKDAAGKPLERAFNMFVLDPIFRLFAAIMNFKKDEIPVLLEKLEINLKREEKELEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAETLYEGPSDDQFCIGIRECDPKAELMVYISKMVPTSDKGRFYAFGRVFSGTVKSGQKVRIQGPNYVPGKKEDLFIKAVQRTVLMMGRTVEPIDDVPAGNILGIVGIDQFLLKSGTLTTNEAAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYISESGEHIVAGTGELHLEICLQDLQDDHAGVPLKISPPVVTYRETVTNESSMTALSKSQNKHNRIYLKAQPIDEELSLAIEEGKVHPRDDFKARARIMADEYGWDVTDARKIWCFGPDGTGANLVVDQSKAVQYLHEIKDSVVAGFQLATKEGPILGENMRSVRVNILDVTLHADAIHRGGGQVIPTMKRVTYAAFLLAEPAIQEPIFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYLPVNESFGFTGELRQATAGQAFPQMVFDHWANMNGNPLDPASKVGEIVLAARKRQGMKENVPGYEEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.546 kDa
Sequence
MVAFTVDQIRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLFSEMSEEDVKDIKQKTEGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQSFSRTVESVNVIISTYADEVLGDVQVYPQKGTVAFGSGLHGWAFTIRQFANRYSKKFGVDREKMMERLWGDSYFNPKTKKWTNKDRDADGKPLERAFNMFVLDPIFRLFAAIMNFKKDEIPVLLEKLEIALKSDERDLEGKALLKVVMRKFLPAADALLEMIIMHLPSPVTAQNYRAEQLYEGPSDDPACIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFSGTVKSGQKVRIQGPSFTVGKKEDLFIKAIQRAVLMMGRFVEPIDDCPAGNIVGLVGIDQFLLKTGTLTTFESAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEICLQDLENDHAGIPLKISPPVVAYRETVEGESSQVALSKSPNKHNRIYLKAQPIDEEVSLAIEGGKINPRDDFKARARVMADEYGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVSAFQWATKEGPIFGEQMRSVRINLLDVTLHADAIHRGAGQIMPTMRRATYAGFLLAEPKIQEPVFLVEIQCPEQAVGGIYSVLNRKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWATLGTDPLDPTTKAGEIVVEARKRHGLKENVPGWQEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.329 kDa
Sequence
MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGEARFMDTRKDEQERGITIKSTAISLYSDLPEEDVKEIPQKSDGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVCINKVDRALLELQVSKEDLYQSFSRTVESVNVIISTYSDEVLGDVQVYPSKGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKQKMMERLWGDSFFNPKTKKWTNKETDTDGKPLERAFNMFVLDPIFRLFAAIMNFKKDEIPTLLEKLEINLKSDEKDLEGKALLKVVMRKFLPAADALLEMIVMHLPSPVTAQNYRAEQLYEGPADDANCIAIKKCDPTADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKIRIQGPNYVPGKKDDLFLKAVQRVVLMMGSRVEPIDDCPAGNIVGLVGIDQFLLKTGTLTTSETAYNMKVMKFSVSPVVQVAVDVKNANDLPKLVEGLKRLSKSDPCVLTQMSESGEHIVAGTGELHLEICLQDLENEHAGIPLKISPPVVAYRETVEAESSQVALSKSPNKHNRIYLKAEPMDEEVSLAIEQGKINPRDDFKARARVMADEYGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVSAFQWATKEGPILGETMRSVRVNILDVTLHADAIHRGAGQIMPTMRRATYAGFLLAEPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWATLNSDPLDPTSKAGEIVTAARKRHGMKEEVPGWQEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.194 kDa
Sequence
MVAFTIEQIRELMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLYASMTDDDCKEIQQKTVGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALGERIKPVVIINKVDRALLELQVTKEDLYQSFSRTIESVNVIISTYVDSSLGDSQVYPDKGTVAFGSGLHGWAFTVRQFATRYSKKFGVDRIKMMERLWGDSYFNPKTKKWTNKDKDAEGKTLERAFNMFVLDPIFRLFSSIMNFKKSEIPTLLEKLEINLKAEEKELEGKALLKVVMRKFLPAADALLEMIVIHLPSPVTAQAYRAETLYEGPADDASCIAIKNCDPTADLMVYISKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYQVGKKDDLFVKAIQRTVLMMGRFVEAIDDCPAGNIVGLVGVDQFLLKSGTITTNEASHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTSMSESGEHIVAATGELHLEICLSDLQNDHAGIPLKISPPIVSYRETVNAESSMVALSKSPNKHNRIYVKAQPIDEEVSLDIEKGVINPRDDFKARARILADNHGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGENVRSVRVNILDVTLHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYLPVNESFGFSGELRQSTGGQAFPQLIFDHWANLNGDPTDPTSKVGTIVKEKRERQGMKPDVPGYEEYYDKL

Gene
EFT1
Protein
Elongation factor 2
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Length
842 amino acids
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Similarity
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mass
93.417 kDa
Sequence
MVAFTVDQIRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLFSEMSDDDVKDIKQKTDGNAFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQSLAERIKPVVVINKVDRALLELQVSKEDLYQSFSRTVESVNVIISTYADEVLGDVQVYPQRGTVAFGSGLHGWAFTVRQFANRYSKKFGVDREKMMDRLWGDSYFNPKTKKWTNKERDADGKPLERAFNMFVLDPIFRLFAAIMNFKKEEIPVLLEKLEINLKGDEKELEGKNLLKVVMRKFLPAADALLEMIILHLPSPVTAQNYRAEQLYEGPSDDPACIAIKNCDPKSDLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNFIPGKKEDLFIKAIQRAVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTFEGAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLVSMSESGEHIVAGTGELHLEICLQDLENDHAGIPLKISPPVVAYRETVEGESSQTALSKSPNKHNRIYLKAQPIDEEVSLAIEGGKINPRDDFKARARIMADEFGWDVTDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGEQMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLAEPKIQEPVFLVEIQCPEQAIGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPINESFGFTGELRQATGGQAFPQMVFDHWATLGTDPLDPSTKAGEIVLAARKRQGMKEEVPGWQEYYDKL