ID A0A1I7S220_BURXY Unreviewed; 985 AA.
AC A0A1I7S220;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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};
GN ORFNames=BXYJ_LOCUS2870 {ECO:0000313|EMBL:CAD5212338.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0704900.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0704900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:CAG9090311.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5212338.1};
RA Kikuchi T.;
RL Submitted (AUG-2020) 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: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 EMBL; CAJFDI010000001; CAD5212338.1; -; Genomic_DNA.
DR EMBL; CAJFCV020000001; CAG9090311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7S220; -.
DR WBParaSite; BXY_0704900.1; BXY_0704900.1; BXY_0704900.
DR eggNOG; KOG2072; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
DR Proteomes; UP000582659; Unassembled WGS sequence.
DR Proteomes; UP000659654; 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; -; 2.
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:UP000659654};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 329..511
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 684..715
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 810..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 116325 MW; 7C40272A0ADF138F CRC64;
MNNRYSTVQR PEAALQRAND FISVGKEADA LNALYEVIKD RRSRQWSETY EEIMMKYVEL
CVRLRNTALA KDGLFQYRVF TQQVSVTSLK SVIEHFLGLA EQKTEEAQKE SMERVEEIDD
LDSADAPENL LLSVVSGAVT QDRMDRTVLS PWLRFLWDSY RNCLDMLRNN VIVEEIYHWV
ARKSFEFCAK YKRRNEFRKL CDLLRIHLAQ IQKSQTSVSE PRTNDYRVKL SSIDSLQFMQ
DTRLHQLNTA IQMELWQEAY KSAEDLHNIM QLSKDKDRRM VKPASYVNYF DKLAMIFWKG
GNTLFHAAAL LQKFIICKDM KKTFTGEEAT DQATRVLLAT LTIQDGADQP STLTKLLDIE
DQHLTNIRVL SSLLRLPIAP TRAGLLKEIA WLNIPELAIE PARQIYKNLE LEFQPLKLAS
VIQGGIDNLN KLEKPEYSQY SDELKFVVAT KVLRQLSIIY GSLSLSRFQK IIPFFSRVEL
EHFLVESAKH RSIKASVSHR DDCVVFSALD LTLAGGLDAS VDVEAASNGI EYIREHLIQL
HNHCQNAVFE LEGAKVESEI ASKLGEQVKT YLYHKDEDYS RILSRCRKIE DYKEVSEHQR
REKIQIAQEE YQKREEQRRQ AELRRLEEEN QENEKKRQQA EKDEIVRRQK AEQLKRFQSN
PIYQQIVKEK GEEAMQTMDP ELVLKEQRER MDVERRELQN KLRQHEKKYD YVVRAFHLEE
IKHYKKMSED YLENAPSRFK ECEDRRIQNA IEEHERSIQT YERMNKIRAD AEEFLGRLIE
RNAEDLERRR KEWKIRLEEE KRRRLIERKE QRKVDRKRQE QQRKKEEEDR IKEQAERDKM
EKFEKDRQDH RQMMERIREK ERQTSGFPPR RDRNDQGGGR YGDRERNGPT DGDGGKFVPS
RVRREVDFSR ADTDSNWRRG GPPAREERES APAHQESQPS SGAWVPSRQR QQQNQDSGSN
SNAYRPPAAR RDRDQGRAAP ENSWR
//
