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Database: UniProt
Entry: A0A218V728_9PASE
LinkDB: A0A218V728_9PASE
Original site: A0A218V728_9PASE 
ID   A0A218V728_9PASE        Unreviewed;       777 AA.
AC   A0A218V728;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:OWK61915.1};
GN   Synonyms=EIF3S9 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=RLOC_00007162 {ECO:0000313|EMBL:OWK61915.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK61915.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK61915.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK61915.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OWK61915.1}.
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DR   EMBL; MUZQ01000034; OWK61915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218V728; -.
DR   STRING; 299123.ENSLSDP00000001420; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000197619; 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; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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:UP000197619};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          148..231
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..88
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  89249 MW;  82590E4252FACD68 CRC64;
     MQDTEETPAA AAPPGALGPA EQPELTDAPA PPAEPPQEPE PEPEEKEDEE REGGGESQAP
     PEEPEQPRPP SGRQSPAQAE PQPEPEPAAG AEPGAAQQDG EAAPAAPAEP EDEISFSDPE
     DFVDDISDEE LLGDILKDQP QEADGIDSVI VVDNVPQVGP DRLEKLKNVI HKIFSKFGKI
     INEFYPEADG KTKGYIFLEY MSPSHAVDAV KNADGYKLDK QHTFRVNLFT DFDKYMTISD
     EWEIPEKQPF KDLGNLRYWL EDPDCRDQYS VIFESGDRTS IFWNDIKEPV QIEDRARWTE
     TYVRWSPKGT YLATFHQRGI ALWGGEKFKQ IQRFSHQGVQ LIDFSPCERY LVTFSPLMDT
     QDDPQAIIIW DILTGQKKRG FHCENSAHWP IFKWSHDGKF FARMTSDTLS IYETPSMGLL
     DKKSLKINGI RDFSWSPGGN IIAFWVPEDK DIPARVTLMQ LPSRQEIRVR NLFNVVDCKL
     HWQKNGDYLC VKVDRTPKGT QGVVTNFEIF RMREKQVPVD VVEMKESIIA FAWEPNGSKF
     AVLHGETPRI SVSFYHVKNN GKIELIKTFD KQQANTIFWS PQGQFVVLAG LRSMNGALAF
     VDTSDCTMMN IAEHYTASDV EWDPTGRYIV TSVSWWSHKV DNAYWLWTFQ GRLLQKNNKD
     RFCQLLWRPR PPTLLSEDQI KQIKKDLKKY SKIFEQKDRL SQSKASKELV ERRRTMMEEF
     RKYRKMAQEL YMEQRNERLE LRGGVDTDEL DSNVDDWEEE TVEFFINEEI ITLAEPE
//
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