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EF1A_SULAC
ID   EF1A_SULAC              Reviewed;         435 AA.
AC   P17196; Q4JAW4;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE   AltName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=Saci_0685;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RA   Auer J., Spicker G., Mayerhofer L., Puehler G., Boeck A.;
RT   "Organisation and nucleotide sequence of a gene cluster comprising the
RT   translation elongation factor 1-alpha from the extreme thermophilic
RT   archaebacterium Sulfolobus acidocaldarius: phylogenetic implications.";
RL   Syst. Appl. Microbiol. 14:14-22(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
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DR   EMBL; X52382; CAA36608.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY80065.1; -; Genomic_DNA.
DR   PIR; S12818; EFUC1A.
DR   RefSeq; WP_011277567.1; NC_007181.1.
DR   AlphaFoldDB; P17196; -.
DR   SMR; P17196; -.
DR   STRING; 330779.Saci_0685; -.
DR   EnsemblBacteria; AAY80065; AAY80065; Saci_0685.
DR   GeneID; 3472531; -.
DR   KEGG; sai:Saci_0685; -.
DR   PATRIC; fig|330779.12.peg.653; -.
DR   eggNOG; arCOG01561; Archaea.
DR   HOGENOM; CLU_007265_3_5_2; -.
DR   OMA; AIRDMGM; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..435
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090993"
FT   DOMAIN          4..229
FT                   /note="tr-type G"
FT   REGION          13..20
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          69..73
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          90..93
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          152..155
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          193..195
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         90..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         152..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   435 AA;  48200 MW;  A012AF564624803F CRC64;
     MSQKPHLNLI VIGHVDHGKS TLIGRLLMDR GFIDEKTVKE AEEAAKKLGK DSEKYAFLMD
     RLKEERERGV TINLSFMRFE TRKYFFTVID APGHRDFVKN MITGASQADA AILVVSAKKG
     EYEAGMSAEG QTREHIILSK TMGINQVIVA INKMDLADTP YDEKRFKEIV DTVSKFMKSF
     GFDMNKVKFV PVVAPDGDNV THKSTKMPWY NGPTLEELLD QLEIPPKPVD KPLRIPIQEV
     YSISGVGVVP VGRIESGVLK VGDKIVFMPV GKIGEVRSIE THHTKIDKAE PGDNIGFNVR
     GVEKKDVKRG DVAGSVQNPP TVADEFTAQV IVIWHPTAVG VGYTPVLHVH TASIACRVSE
     ITSRIDPKTG KEAEKNPQFI KAGDSAIVKF KPIKELVAEK FREFPALGRF AMRDMGKTVG
     VGVIIDVKPR KVEVK
 
 
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