EIF3A_MONBE
ID EIF3A_MONBE Reviewed; 1052 AA.
AC A9V549;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
GN ORFNames=33388;
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154;
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; CH991560; EDQ87212.1; -; Genomic_DNA.
DR RefSeq; XP_001747825.1; XM_001747773.1.
DR AlphaFoldDB; A9V549; -.
DR SMR; A9V549; -.
DR STRING; 81824.XP_001747825.1; -.
DR PRIDE; A9V549; -.
DR EnsemblProtists; EDQ87212; EDQ87212; MONBRDRAFT_33388.
DR GeneID; 5893067; -.
DR KEGG; mbr:MONBRDRAFT_33388; -.
DR eggNOG; KOG2072; Eukaryota.
DR InParanoid; A9V549; -.
DR OMA; VMYQTTA; -.
DR Proteomes; UP000001357; 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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1052
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366372"
FT DOMAIN 325..505
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 570..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 568..712
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 769..882
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 570..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 122105 MW; 6D071F6989FE8BFF CRC64;
MSMNKFFQPK NALKRAEDLE AVGKPNLALE TLHDLLNSSK HKKQWTAVHE EIMIKFLDLC
MQLKRAPEAK DGLYQFKIVT GTSAVNSLEK VVRYYLKTAE DKVAEAWQQS QLRDATNVND
EIDDLEEAQT PEQVLLAAVS ADGETERANR VQLMPWLRYL WEAYRAVLEL LRHHSKMEHA
YHATARQAMR FCHQYERRNE FRRLCNMLSL HLNQWRTPYQ SKSGQAGIDI NNPQTIQYSL
DTRFELISYA GKLEQWQEAF RAMEEVTGLL DSAPEKPSPP VWGIYYHKLA QIFWRSKDYA
FHAAAWHQMF DNAIRNAKSF NRDDIQYAAS AVLLASLTVP LANLDTMVKP MEGYLPEVRA
SRQQRLAGLL GLSRMPSRDE LLQYMFDLNV MTYVHPALKD LYNLVEDEFD PLQLSQKAAP
VLEFLKSHEQ FAQYVTPLKY ILLLRLLKQL SQLYSSLKLE RCFKLASFMT PEECEEVLVH
AVQDKVLQLR IDHARGSLHF NNNIFAFNER QVNDGPKLQN LQAEMMNGQL TTLSRRLYTA
INMIKPAVVQ ESQMGVKAIN RIKDEVAREH VSNLSRRDEI EKQKEELEQS RRRRHQEQMQ
KHHQNQMQVR QKMAEAVKKN QEELERQKLQ LQREEIERQK ALEALNDVSS SSAGQKVVQA
LNKSDLGTKI TAQDIHKMAY EQQKKDARER QERLRAEEKR LDHMERAKRL REIPRRKEHI
AAMSEQNAKW HTELQSARLE KARVDHAKAL GLKELLKAFA PDKDAYIEEK TAERRKEYMA
KLDDFKQRMQ EQKIRLEREE RERKREEKRR AEEEEQRRIK QEEEDRKQRE REAKREQERQ
EQLKLEEAER KKMEEATKLQ RQREEQVRAR EQEKLSNLSA QTSQPTWKRS ARSDAPTTAA
PSSMRVSSWK GDASDDSGRS QPFRPSRGGE RDSGRSFSGL GDRGDRAPRD TGRSFSGLGD
RGDRAPRDTG RSFSGLGDRA PRDFSGRSEP SRSGPRDFSG RSEAGRTSGE RRALHVPSGG
ADKPSGDNVW RSSRGAGSER RVNIPSRGDD KN
