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Database: UniProt
Entry: C4JUA7_UNCRE
LinkDB: C4JUA7_UNCRE
Original site: C4JUA7_UNCRE 
ID   C4JUA7_UNCRE            Unreviewed;       761 AA.
AC   C4JUA7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=PRT1 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=UREG_06046 {ECO:0000313|EMBL:EEP81204.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP81204.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476617; EEP81204.1; -; Genomic_DNA.
DR   RefSeq; XP_002585357.1; XM_002585311.1.
DR   AlphaFoldDB; C4JUA7; -.
DR   STRING; 336963.C4JUA7; -.
DR   GeneID; 8438952; -.
DR   KEGG; ure:UREG_06046; -.
DR   VEuPathDB; FungiDB:UREG_06046; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; C4JUA7; -.
DR   OMA; LWGGPQF; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000002058; 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: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   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 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:UP000002058};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          62..148
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          719..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  86462 MW;  D790860A97EC6EB5 CRC64;
     MAPSFDTLSE QDLHEEEVEI DFSGTDRVSP SSTWDPSLTA CRAAILDLKA QYEVRLEEGL
     DAFVVIDGLP IVPEDSKPKL IKFLLKKLNT VGRTREDAIF MPLNEKGMSE GFAFVEYDTP
     EQAIAATKHL HGTPLDKKHT LAVNKLTDID RYGREGRIDE EYTPPKIEPF QEKEHLRSWL
     GDPNARDQFA MYRGDKVGVF WNMKNNPPEN VVDRDHWTQL FVQWSPLGTY LASVHPQGVQ
     LWGGPQFNKQ KQFPHPFVSL MEFSPGENYL TTWSSRPIQL DGPPGILSYE EEGKNIIIWD
     ITTGKPLRSF VSHELAAPAA DGDAAQAKKK VQWPAFKWSA DEKYVARMLP GQSISIYELP
     RMNLLDRTSV KIEGVMDFEW SPATVQREGV KQYEQLLSFW TPEVGNNPAK VGLMSVPSKE
     IVRTRNLFNV SDVKLHWQSQ GVYVCVKVDR HSKSKKSLAT NLEIFRVREK GVPVEVVDSL
     KDTVINFAWE PKGDRFVLIT TGEVPSGTAV PPKTAVSFFA PEKTKSGTAG NFKLVRTIEK
     KTSNGIYWSP KGRFVVVATV HSQQHFDIDF WDLDFEGEKP EGEKDLSANL QLMKSAEHFG
     VTDIDWDPTG RYVVSSASAW THSLENGYHI HTFSGTTLAE HAVEKFKQLI WRPRPPTFLS
     KEEQKKIRRN LREYSREFDE EDKYAVDIAN TAIVEMRKRL LSEWTAWLKK EKEIVEEERE
     ALGLPKVEEE PAAKPAPGAE DDTVVEEIVE EIIEESEEIM A
//
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