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EIF3A_PICGU
ID   EIF3A_PICGU             Reviewed;         891 AA.
AC   A5DHL9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE            Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE            Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Name=TIF32 {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=PGUG_02770;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC       Rule:MF_03000}.
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DR   EMBL; CH408157; EDK38672.2; -; Genomic_DNA.
DR   RefSeq; XP_001485041.1; XM_001484991.1.
DR   AlphaFoldDB; A5DHL9; -.
DR   SMR; A5DHL9; -.
DR   STRING; 4929.XP_001485041.1; -.
DR   EnsemblFungi; EDK38672; EDK38672; PGUG_02770.
DR   GeneID; 5127412; -.
DR   KEGG; pgu:PGUG_02770; -.
DR   VEuPathDB; FungiDB:PGUG_02770; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   HOGENOM; CLU_002096_2_1_1; -.
DR   InParanoid; A5DHL9; -.
DR   OMA; VMYQTTA; -.
DR   OrthoDB; 967904at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03000; eIF3a; 1.
DR   InterPro; IPR027512; EIF3A.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR14005; PTHR14005; 1.
DR   Pfam; PF01399; PCI; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..891
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366368"
FT   DOMAIN          326..508
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          604..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          72..121
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          593..849
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
SQ   SEQUENCE   891 AA;  102989 MW;  F868D81AC2AD5552 CRC64;
     MPPPHRNHNF RPENVLKRAE DLIAVDKREA ALETLYEFIT SKRIRYLQVE DLEPIALLLM
     ELAVDLRKGK LAKDALHQYK KNVQMSENGL ESVQVVVKRF VDLAEKKLND AQAKADIKID
     QDEDEDLETS QTPESILMSA VSNTDTADRT ERELVTPWLR FLWEAFRAVL DILRNNSKTE
     VTYSTIVNQA FQFCFRFNRK AEFRRLCELL RAHIQTVTTQ PKTAGTTNAI DLSDSETIQR
     YLDQRFSQLN ISVKLELWQE SFRSVDDVHT LITASKKTPK PVMMANYYEN LARIFAVSDN
     GLFHAAAWNK FFNLYSQSPN ATDDELSHYA SILVLSTLSI PQRSSNSNET VVDDHRAKNA
     KLSSLLNLSH VPTRDSLLKS IVSRQILSFV DPCVKKLFDV LGENNFHPLT IKKEIAALFK
     EIEADKDYKH YIKTLTEVVS VRIFQQVSQV YETVKLDFLV SLGIFEGTEY TLSALEVENL
     IAIATKEGHL ALTIDHESGV VTFKSSPFED SLSDSLTSRL QISPAELVRS QLQKFAYTLS
     KTVDTIDPEN ARRLEASREA AVKRAVAGIS EEQEEIANRV KVMDERKRVI DVAKRKQDEE
     AARLKSERLS AEQKAEQERM LAEQERRSLE KLEREKHLIR EREKRKIAEE INAKGIIKID
     LDNLENLDTD KLRIMQIEQL NKDKKNLEEK LRALSKKTDH TERAFRRYEL QYLEKDAEAQ
     IEQEAKNYEL VKANKIAKAK KDFEEAHALK ERFTRLVPDY SEFKSEINAK NKDKLKQLQA
     EAKAQLERAK QERIEQIKRE RIEELAQRKR EQIQAEQEEA RRRQKEEELA KLKEEIRLQR
     EKDAEMLKRR QNVEAEVASR KAAITPAAPA EAKPMTYAEK LKLKRQQAGR S
 
 
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