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EIF3B_BOMMO
ID   EIF3B_BOMMO             Reviewed;         695 AA.
AC   Q1HDZ5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
GN   Name=eIF3-S9 {ECO:0000255|HAMAP-Rule:MF_03001};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang L.-L., Chen K.-P., Yao Q., Hu Z.-G., Gao G.-T.;
RT   "RNA binding proteins in Bombyx mori.";
RL   Submitted (APR-2006) 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_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC       Rule:MF_03001}.
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DR   EMBL; DQ497202; ABF55967.1; -; mRNA.
DR   RefSeq; NP_001037602.1; NM_001044137.1.
DR   AlphaFoldDB; Q1HDZ5; -.
DR   SMR; Q1HDZ5; -.
DR   STRING; 7091.BGIBMGA007114-TA; -.
DR   PRIDE; Q1HDZ5; -.
DR   GeneID; 733052; -.
DR   KEGG; bmor:733052; -.
DR   CTD; 733052; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_1_0_1; -.
DR   InParanoid; Q1HDZ5; -.
DR   OrthoDB; 1194797at2759; -.
DR   Proteomes; UP000005204; 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; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
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   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 2.130.10.10; -; 2.
DR   Gene3D; 3.30.70.330; -; 1.
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; PTHR14068; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   Repeat; RNA-binding; WD repeat.
FT   CHAIN           1..695
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363792"
FT   DOMAIN          60..144
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          164..205
FT                   /note="WD 1"
FT   REPEAT          295..335
FT                   /note="WD 2"
FT   REPEAT          338..373
FT                   /note="WD 3"
FT   REPEAT          444..486
FT                   /note="WD 4"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..43
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  80615 MW;  D0B664285DDADEA6 CRC64;
     MAKKKGDEKA NPAPQSDNEE QNFEEEPDFD DPEDFVEIPE EELLADILEQ KPKESDGYEN
     VVVVDGCPQV GPERLEKLQS VINKIFSKFG KIVNEYYPTT ENGLTTGYIF LEYSNPQNAA
     EAVKATNNCK LDKQHTFLVN LFTDFQKYSD IPKEWEPPAP QPFKVQSDLQ WYLMDPDAYD
     QFLVGIGTGV ALQVWQNALP EPLLLQERPN WTETYAVWSP LGTYLATFHW RGVALWAGPK
     FSQFQKFFHP EARFISFSPC ENYMVTFSPS GDRGDDKKWI IGDIRTGQEK RSFPPPDEYV
     TWPIFRWSKD DRFFARIGAD VLSVYETPGF GLLDKKSIKI PGIRDFSWSP SDNTLAYWVA
     EDKDVPARVT LLEIPNRTEV RSKNLFSVAD CKIHWQKSGD YLCVKVDRYS KVKKDKIDIK
     YSGMYYNFEI FHMREKEIPV DSVEIKEPIQ AFAWEPVGSK FSIIHGDPAN ISISFYQVNT
     GQAPTLLKKF ERKPFNHLFW SPSGQFIVLA NLGLTGGALE FLDTNDFTIM NVADHYQMSG
     IEWDPTGRYV VTGVSSLKCK MDCGYYIWSF QGKILRRVMK EGFAQFHWRP RPPTLLSEKQ
     QKEIKKNLKK YYSQFESKDR MRSSKASKEL VAKRTEQMKK FTEYRESKIQ EWNEQKPRRL
     ELRDYVDTDG LDTDAVNTVE EVIEFFVKEE QTVIE
 
 
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