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Database: UniProt
Entry: I1RP27_GIBZE
LinkDB: I1RP27_GIBZE
Original site: I1RP27_GIBZE 
ID   I1RP27_GIBZE            Unreviewed;       746 AA.
AC   I1RP27;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
DE            Short=eIF3 p90 {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3, p90 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
GN   Name=FG05777.1 {ECO:0000313|EnsemblFungi:CEF87699};
GN   Synonyms=PRT1 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=FGRAMPH1_01T18739 {ECO:0000313|EMBL:CEF87699.1};
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF87699.1, ECO:0000313|Proteomes:UP000070720};
RN   [1] {ECO:0000313|EnsemblFungi:CEF87699, ECO:0000313|Proteomes:UP000070720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC   {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC   9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF87699};
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2] {ECO:0000313|EnsemblFungi:CEF87699, ECO:0000313|Proteomes:UP000070720}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC   {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC   9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF87699};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PH-1;
RA   King R., Urban M., Hassani-Pak K., Hammond-Kosack K.;
RT   "A revised Fusarium graminearum genomic reference sequence using whole
RT   shotgun re-sequencing.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CEF87699.1, ECO:0000313|Proteomes:UP000070720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC   {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC   {ECO:0000313|EMBL:CEF87699.1};
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [5] {ECO:0000313|EnsemblFungi:CEF87699}
RP   IDENTIFICATION.
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC   {ECO:0000313|EnsemblFungi:CEF87699};
RG   EnsemblFungi;
RL   Submitted (JAN-2017) to UniProtKB.
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis and, together
CC       with other initiation factors, stimulates binding of mRNA and
CC       methionyl-tRNAi to the 40S ribosome. {ECO:0000256|PIRNR:PIRNR036424}.
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:0000256|HAMAP-Rule:MF_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03001,
CC       ECO:0000256|PIRNR:PIRNR036424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001,
CC       ECO:0000256|PIRNR:PIRNR036424}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000256|HAMAP-
CC       Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424}.
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DR   EMBL; HG970334; CEF87699.1; -; Genomic_DNA.
DR   RefSeq; XP_011324366.1; XM_011326064.1.
DR   AlphaFoldDB; I1RP27; -.
DR   STRING; 229533.I1RP27; -.
DR   EnsemblFungi; CEF87699; CEF87699; FGRRES_05777.
DR   GeneID; 23552940; -.
DR   KEGG; fgr:FGSG_05777; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G18739; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; I1RP27; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000070720; Chromosome 3.
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:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR14068; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR   PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_03001,
KW   ECO:0000256|PIRNR:PIRNR036424};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03001,
KW   ECO:0000256|PIRNR:PIRNR036424};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070720};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          42..128
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   746 AA;  85247 MW;  E2D7DD01C92A4711 CRC64;
     MAPSFDHLRE ADLDDDEFND DDIDISDLRE RFEVSLDQGY DNFVVIDGLP QVTEDQKPKL
     VKFLLKKLNT VGKTREDSVH MPMGDDGKSL RFAFVEYSSP AEAAAATRQL DLTPLDKKHT
     LRVNKFTDIE RYGREGRIDE TYQPPQIEDF TEKEHLRWFL KDPSGRGRDQ FVMYRGDSVG
     IYWNNEKDQP ENIVERPFWT EAFIQWSPLG TYLTSVHAQG VQLWGGASWS RQARFAHPFV
     NMISFSPGEK YIVTWSNRPI SIPDEGHPAL SIDDHGKNYV IWDIATATPL RSFANLEPPK
     VEDGKPPPKM QWPAFKWSAD DKYVARLNPG QSISVYELPR MNLLDKTSIK IDGVVDFDWA
     PATPKRDGVK EYEQLFCYWT PEIGSNPAKV GLMSVPSKEV VRSLNLFSVS DAKLHWQSDA
     AYICVKVDRH SKSKKSQATT LEIFRVKEKG VPVEVVDTIK DTVINFAWEP KGDRFAIIST
     TEPVGVTAVA PKTAVSFFCP EKAKKGQQVG NFKHLRTLDK KNSNAIYWSP RGRFVVIATI
     ANTQSSDLDF FDLDFEGEKP ESDKDLTANL QAMNTADHYG VTDVEWDPSG RFVASWASAW
     KHSMENGYHI YDFKGEALRE EPLEKFKQFA WRPRPATLLT KEEQKAVRKN LREYSRVFEQ
     EDADRGASAD LAVVEARRRM LEEWHSWRES MEADVLEERE VLGLPKDPHA PLLEAYTKSL
     DTASDEDRVI EEIVEEVIEE SEEVLA
//
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