GenomeNet

Database: UniProt
Entry: A0A151N230_ALLMI
LinkDB: A0A151N230_ALLMI
Original site: A0A151N230_ALLMI 
ID   A0A151N230_ALLMI        Unreviewed;       688 AA.
AC   A0A151N230;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
DE            Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=eIF-3-eta {ECO:0000256|HAMAP-Rule:MF_03001};
GN   Name=EIF3B {ECO:0000256|HAMAP-Rule:MF_03001,
GN   ECO:0000313|EMBL:KYO30705.1};
GN   Synonyms=EIF3S9 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=Y1Q_0008321 {ECO:0000313|EMBL:KYO30705.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO30705.1};
RN   [1] {ECO:0000313|EMBL:KYO30705.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO30705.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC       EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC       EIF3M. {ECO:0000256|HAMAP-Rule:MF_03001}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO30705.1}.
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DR   EMBL; AKHW03004154; KYO30705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151N230; -.
DR   STRING; 8496.A0A151N230; -.
DR   Proteomes; UP000050525; 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:UP000050525};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          34..117
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   688 AA;  80280 MW;  FA946348BC0587E5 CRC64;
     MRSDPEDFVD DISEEELLGD VLKDRPQEAD GIDSVIVVDN VPQVGPDRLE KLKNVIHKIF
     SKFGKIINEF YPEADGKTKG YIFLEYMSPA HAVDAVKNAD GYKLDKQHTF RVNLFTDFDK
     YMTISDEWEI PEKQPFKDLG NLRYWLEDPD CRDQYSVIFE SGDRTTIFWN DAKEPVQIEE
     RARWTETYVR WSPKGTYLAT FHQRGIALWG GEKFKQIQRF SHQGVQLIDF SPCERYMVSF
     SPLMDTQDDP QAIIIWDILT GQKKRGFHCE SSAHWPIFKW SHDGKFFARM TSDTLSIYET
     PSMGLLDKKS LKITGIKDFS WSPGGNIIAF WVPEDKDIPA RVTLMQLPSR QEIRVRNLFN
     VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE KQVPVDVVEM KEPIIAFAWE
     PNGSKFAVLH GETPRISVSF YHVKNNGKIE FIKTFDKQQA NTIFWSPQGQ FVVLAGLRSM
     NGALAFVDTS DCTMMNIAEH YTASDVEWDP TGRYLVTSVS WWSHKVDNAY WLWTFQGRLL
     QKNNKDRFCQ LLWRPRPPTL LSQDQIKQIK KDLKRYSKIF EQKDRLSQSK ASKELVERRH
     TMMEEFKKYR KMAQELYMEQ RNERLELRGG VDTDELDSNN RSSLIKPCTT ISCTEKRFVH
     FQKAYIIFGI FRPSSLTLDG ECATFSPF
//
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