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Database: UniProt
Entry: A0A182Y7A9_ANOST
LinkDB: A0A182Y7A9_ANOST
Original site: A0A182Y7A9_ANOST 
ID   A0A182Y7A9_ANOST        Unreviewed;      1132 AA.
AC   A0A182Y7A9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000256|HAMAP-Rule:MF_03000};
DE            Short=eIF3a {ECO:0000256|HAMAP-Rule:MF_03000};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000256|HAMAP-Rule:MF_03000};
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI04345-PA, ECO:0000313|Proteomes:UP000076408};
RN   [1] {ECO:0000313|Proteomes:UP000076408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX   PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA   Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA   Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA   Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA   George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA   Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA   Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA   Sharakhov I.V., Tu Z.;
RT   "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT   stephensi.";
RL   Genome Biol. 15:459-459(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASTEI04345-PA}
RP   IDENTIFICATION.
RC   STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI04345-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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_03000}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000256|HAMAP-
CC       Rule:MF_03000}.
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DR   AlphaFoldDB; A0A182Y7A9; -.
DR   STRING; 30069.A0A182Y7A9; -.
DR   EnsemblMetazoa; ASTEI04345-RA; ASTEI04345-PA; ASTEI04345.
DR   VEuPathDB; VectorBase:ASTE010143; -.
DR   VEuPathDB; VectorBase:ASTEI04345; -.
DR   VEuPathDB; VectorBase:ASTEI20_035190; -.
DR   OMA; HQAFQFC; -.
DR   Proteomes; UP000076408; 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:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.860; -; 1.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   HAMAP; MF_03000; eIF3a; 1.
DR   InterPro; IPR027512; EIF3A.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR14005:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A; 1.
DR   PANTHER; PTHR14005; EUKARYOTIC TRANSLATION INITIATION FACTOR 3, THETA SUBUNIT; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_03000};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076408};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03000}.
FT   COILED          558..701
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
SQ   SEQUENCE   1132 AA;  132484 MW;  2E22847DB14B2CB7 CRC64;
     MSRYVQRPEN ALKRANEFID VGKKARALDT LQEVFRAKKW NYNWSESVIE PVMFKYLDLC
     VELKKSHIAK EGLFQYRNMF QLVNVGSLEN VIRGYLKMAE ERTEQAQQQS SQAILDIDDL
     DNLASPESIL MSAVCGEDAQ DRSDRTILLP WVKFLWESYC QCLELLKVNS HCETLYHDIA
     RMAFQFCLKY NRKMEFRKLC EKLRKHLEDI CKVSSQTANV SISKPETQQL NLETRLHQLD
     SAIQMELWLE AYKAIEDIHG LMALSKKTPL PKTMALYYTK LAMVFWKAGN QLFHASALLK
     LFQLSRDMKK NVTAEEIQRM TTHVLIATLA IPLPSAHPEF DRFIETDKSP MEKAQRLAFL
     LGLQQSPSRA LLLKELIRLN VLQLAAPQFR HLYQLLEVEF DPLNLCEQVQ KIVDDIEADP
     NSVYGQYVQA LKDVTLVRLV RQISQVYQTI EFPRLLELAK FADYHHLERI LVDCVRHNDM
     QITIDHRNGC VHFGTDLSES QREDHPDGPT LQSMPSEQIR SQLVNMSVVL HRAIATINPD
     RKKAERERLR GQMVHQYKEN ADKEHQRILQ RQKKIEDRKE YIERMNQERE EEELRQQEEQ
     ARMLKLAEQR RLEAENEERE RKRHENELQM MKERNMKEKI EQIKQTATGQ KLLKKLDEEE
     IRKLNTEEIA AREAEERLKE RKAHENNLKS QEKKIDYFER AKRLEEIPLI EKYLQDRSVQ
     DKEFWEKQEA SRIEAAIAER KNAEACQERL KRMLPDRDVY WQQLKNERGN QFAEKLKQFN
     QALEEERKRR LADRVVKRRE ERRMKWLKEK EEERRRIEEE IRKQKEEADR IERERRAEER
     RIADEKNRQL AEKQLAIAEE VERRRKEELE QKRTEETEAR RDWRTGGGGA GGGGAGGASA
     AASEPKPEDS WRRGPAAASA NASADEPKKN VWQGSGRYGP GPRDRAGAGE TGAKDKWRSG
     PEDHEKERDG GGMRRGGDMR RGQDDRGPIR RGGDDRGDRD DRGPMRRGVG GAPPSSGAPR
     RGDDRPGDRG FNRDRRDDRR DDRGPRGGDR DRDNTWRRGP AESNDENRRG PGQQRDEGRQ
     DTWRNTRQEP APKPKEERPQ REPRPQENGT KLNDQLLRHA TTPAQTTTDG RM
//
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