EIF3A_CULQU
ID EIF3A_CULQU Reviewed; 1149 AA.
AC B0W6N3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-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 Name=eIF3-S10 {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=CPIJ002784;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) 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_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=EDS36707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231848; EDS36707.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001844367.1; XM_001844315.1.
DR AlphaFoldDB; B0W6N3; -.
DR SMR; B0W6N3; -.
DR STRING; 7176.CPIJ002784-PA; -.
DR EnsemblMetazoa; XM_038250124.1; XP_038106052.1; LOC6033979.
DR GeneID; 6033979; -.
DR KEGG; cqu:CpipJ_CPIJ002784; -.
DR VEuPathDB; VectorBase:CPIJ002784; -.
DR VEuPathDB; VectorBase:CQUJHB011721; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; B0W6N3; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000002320; Partially assembled 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:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
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 Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..1149
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366333"
FT DOMAIN 317..498
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 133631 MW; B0BED34CCFE0F40B CRC64;
MSRYMQRPEN ALKRANEFIE VGKPARALDT LQEVFRIKKW TYTWSEAVIE PIMFKYLDLC
VELKKSHIAK EGLFQYRNMF QMLNVGSLEN VIRGYLKMAE ERTEAAQQQS SQAILDIDDL
DNLATPESIL MSAVCGEDAQ DRSDRTILLP WVKFLWESYG QCLELLKVNS HCENLYHDIA
KMAFAFCLKY NRKMEFRKLC EKLRKHLDDI SKVSSQTANV SISKPETQQL NLDTRLNQLD
CAIQMELWLE AYKAIEDIHG LMTLSKKTPM PKTMALYYQK LAMVFWKAGN QLFHAAALLK
LFQLSRDMKK NVTQEEIQRM TSHVLIATLA IPLPSAHPEF DRFIETDKSP LEKAQKLAVL
LGLQQPPSRV SLLKEVLRLN VLQLAAPQFQ NLYKWLEVEF DPLNLCSRVQ GVIEEITADE
NSPYTQYTQA LQDVTLVRLV RQVSQVYQSI EFSRFLSLAK FANSFYLERI LVDCVRHNDM
QITIDHRNHS VHFGTDLSES QREDHPDGPT LQSMPSEQVR SQLVNMSVVL HRAIATINPN
RKKADRERLR NQMVKNYEEN MVKDHQRILQ RQKKIEDRKE YIERVNLERE ELEQRQLEEA
ARQQKLAEMR RLEQENEERE RKRHENEIQM IKERNMKDKI DQIKQSASGQ KLLKKIDEED
IKKMNAEEIA AKEAEERQKE RKAHDNNLKS QEKKIDYFER AKRLEEIPLI EKYLEDKLVQ
DKEFWEKQEA SRIEAAIAER KNAEQVQERL RRMQADRDVF WQKLKGERSN AFAEKLKVFN
AALEEERRRR LAERVIQRRE ERRQKWLREK EEERRRIEEE LRKQREEEER IERERRAEER
RIENEKQRVI MEKQRAKEEE IERKLAEEKE RLKERAPRGE KEERGGGGGG GGAWRGRGDT
AAPAESAAKP ESDWRNAREA REPAPESAGA SSAAAPAPKK DGVWQPSGRF REGRGAPGAD
RPPRGDDREP PAAAAGESKW RRGGGGADDD KDDGPRPRVG AGDRGPMRRG DGDRDDRGPM
RRGDRPPMRD GDRPGMRRDD RGDRREGGAP DRRDFGGRGG DRRDDRRDDR GPRREGGGER
GGDVWRRAPQ EDRRGGAAGG ESGGNWRNAR QAEPAKPREE RRGGEERPKE ARAAAGPDED
GWTDVKHHR
