EIF3A_NEMVE
ID EIF3A_NEMVE Reviewed; 953 AA.
AC A7SK48;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 25-MAY-2022, entry version 60.
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=v1g190699;
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDO35952.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS469683; EDO35952.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001628015.1; XM_001627965.1.
DR AlphaFoldDB; A7SK48; -.
DR SMR; A7SK48; -.
DR STRING; 45351.EDO35952; -.
DR GeneID; 5507362; -.
DR KEGG; nve:5507362; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_2_1; -.
DR InParanoid; A7SK48; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; A7SK48; -.
DR Proteomes; UP000001593; 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 SMART; SM00088; PINT; 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..953
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366346"
FT DOMAIN 323..504
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..642
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 670..704
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 732..877
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 896..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 113352 MW; 22EEBDD6092BFFAF CRC64;
MPTYFQRPEN ALKRANEFIE VGKKEPALDA LYDVIKSKKH RTWQNKIHEP ILFKYLELCV
DLRRSHVAKE GLYQYKLICQ QVNIASLEDV IRYFLKLAES RAVEAQEDSR KEASAELDED
VDIEDLDQIQ TPESLLLSFV SGEDTQDRTD RVKLTPWVKF LWEAYRNVLE LLRNNVRVEK
LYHETAQQAF KFCLKYTRRT EFRKLCDNLR NHLNVTLKHQ GQPNSVNLNN PDSIQMHLET
RLAQLDSAIS MELWQEAFKA VEDVYGLMQL SKRPPKPQVM ANYYQKVALV FLKAGNFLYH
ACTQQRLYLL MREQKKSITS EELQKMASHV LLATLSVPIQ VSLSNTEKYL ELDEVAREKS
KRLANLLNLQ NTPTRESLLQ DMLKANVLQY VNTKVHCLYQ LLEKDFRPLD LCAKVNEVCQ
YLESCDDADL CQYIKPIQNI AVTRLLKQVS QVFQTIEFSR LMALVPFMTE FQLERMIVDI
AKEKNLQVRL DHRTKSISFG LDLHVAHREE VPEGPYLQAM PSEGLRNQLT LMSVALQRSI
FTIQHDHIKA KKREEQEQMA QNYLRTARKE HKLMLERKTV IEARKEYLES VMQERERREY
EKIKKQKVEN QEAEQKRLDE ERRQREIQRR RQELQDIEKR QAMDKIAALK KTTVGAKALK
DLSPEEIDNM NADDIIAKQV EQLDKEKREL QTKLKTQEKK VDYFARAMRM EEIPLLNKQY
EEHLVADREF WENQEEERVR KAIEEHEKLV ETSARLQRMI PDKDAFINTL RESRTEEYQA
KFQAFQAKLE QVRKERLEVR RKRRIKDRKE RKKIEMEEAK KREQEEKERK KEEKERIERE
EREAKEREYA ERIAKQNEID RKRREKELEI ERRLEERAGV GQVQQIRCLF ITGWGDHEDG
GDRWRDERGG DRGPDRGGDK PGAWRPKWQR EEPDRGGDRW RGGDRRDGMI TMS
