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EIF3A_USTMA
ID   EIF3A_USTMA             Reviewed;        1024 AA.
AC   Q4P358; A0A0D1CHM7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   25-MAY-2022, entry version 75.
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=UMAG_11577;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003157; KIS66463.1; -; Genomic_DNA.
DR   RefSeq; XP_011391954.1; XM_011393652.1.
DR   AlphaFoldDB; Q4P358; -.
DR   SMR; Q4P358; -.
DR   STRING; 237631.Q4P358; -.
DR   PRIDE; Q4P358; -.
DR   EnsemblFungi; KIS66463; KIS66463; UMAG_11577.
DR   GeneID; 23567442; -.
DR   KEGG; uma:UMAG_11577; -.
DR   VEuPathDB; FungiDB:UMAG_11577; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   InParanoid; Q4P358; -.
DR   OrthoDB; 967904at2759; -.
DR   Proteomes; UP000000561; Chromosome 18.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR   GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR   GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
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   SMART; SM00088; PINT; 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..1024
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366369"
FT   DOMAIN          331..508
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          797..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          575..717
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          777..889
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        797..887
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1024 AA;  115537 MW;  E4C703ABCAD6D58C CRC64;
     MPPFAKPETV LKRSEELINV GQHQAALAAL NEIFTSRRFK QTPLQSLEPI MLRFVDLCVD
     LKKGRMAKEG LMQYKNVSQN TNAQSIELVI KHFIKLADAK VVEAQSKADA AVGEIDVDDL
     EESETPESML LGSVSADQNK DRTDRVLVTP WLKFLWEAYR TALDILRNNA RLEVPYQQIA
     NQALKFCLQY QRKTEFRRLC EVLRQHLQNV ARYSHHAHAI NLTDQDTLQR HLDTRFAQLN
     SAVELELWQE AFRSVEDIHN LLTMAKKAPR PAMMANYYEK LARIFMVSDN NLFHAAAWNR
     YYALARSIAK SEQEHTQIAS YVLISALAVP VISSNAPGTG NLHKSKSDFL QADHEARSRT
     GRLTSLLGLS RTPTRAGLLK EALNRDILKK ARPELRELYN ILEVEFHPLS ICAKIEPILA
     SISQDAEMAK YVKPLHSVVL TRLFQQLSQV YDAVKLSKVM QLVSAFKAPH SYTPAEIEKF
     CLNACKKGHL NIRIDHVAQA ITFQDDVFST DVHPAASASS EADNVGLQAS PSELVRTQLS
     RLATCLDTTL KTIDPTILAD AQAAKRHVFA RAVAAAEDEH KAAIARKALL ARRKELLEEM
     ATRKEREEAA ARAERARAAA EAEQKRIAEE QKKREQDRLN KEVEAVRIEE AKKMAKSLQE
     RGGLKLSEEE LANLDTDKLV QMQVEQIEKE KKELAERLRL IHRRMDHLER AYRREEAPLL
     SADYERQKQE DLQYHKAARI TLLQTSKDKH AADLEIKKRL TRILPDYQQL RSIIEDKRRG
     EFEERRRKAT EQIELEKERR RQQVRDERRR ERQEAEEAER RRVQEEQEAR ARAEEEERLA
     EQRRVEEAQR AELEAKKRAE IEERRAKFQA TADKQRQREE EAEANRRSRA AGTGAAPAQE
     LAAADATWRR ASGSPAPTQA ESQRPPIFGA ARTGGAGGWR ERLAAKEAAG GNATAAPSAP
     AAAPAPASSG AYRPGMFRAA AGAGAGGRTD RVAATPLPPA AAAAESDGFT EVKKNVYRPP
     GRRA
 
 
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