ID T1IIY3_STRMM Unreviewed; 1278 AA.
AC T1IIY3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR000837-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR000837-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) 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 EMBL; JH430212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1IIY3; -.
DR STRING; 126957.T1IIY3; -.
DR EnsemblMetazoa; SMAR000837-RA; SMAR000837-PA; SMAR000837.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_1_1_1; -.
DR OMA; DHMKNVV; -.
DR OrthoDB; 10990at2759; -.
DR PhylomeDB; T1IIY3; -.
DR Proteomes; UP000014500; 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:UP000014500};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 355..537
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 822..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 610..668
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 705..739
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 838..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 153219 MW; CE755322B8FF086A CRC64;
MYPQLPSKDD ATVRWDIDHA YLPVYHLPLL THAAIARPYN MPTYFQRPEN ALKRANEFID
VGKKQRALDA LYDVIKSKKH RTWQKIHEPI MNKYLELCVE LKKSHVAKEG LFQYRNICQQ
VNIKSLEDVV RGYLQLAEDK TELARDESQQ AVIDIDDLDN LLTPESLLLS AVSGEDAQDR
TDRVVLTPWV KFLWESYRQC LELLRNNSRV ERLYHDIAQQ AFKFCLKYNR KTEFRKLCDN
LRTHLSHIHK HQNQQTAINL NNPESQGMHL ETRLCQLDSG IQMELWQEAY KAIEDIHGLM
NLSKKPPKPQ LMANYYHKLA LVFWKAGNYL FHASALFRLF HLSREMKKNL TNEEVQRMAS
RVLLATLAVP IPPARNDIDK YLEVDETTMD KQRRLATLLG LSNPPNRSNL IKDLVRFTVI
QHVGLQLQDL YRWLEVEFHP LKLSVRIQQC FDFIEKNDDW AELKQYIVPL QDVTLTRLLK
QVSQVYQTIR FSRLLELAPF ADAFHLERVV VDAAKNNDLQ VRIDHRTKCL EFGMDLCVAQ
REDLPEGPNL QAMPSEQIRN QLVTMSSVLF RSIALIEPTK RKLERETIRQ AKVAEYHRTA
STKHLRVLAR RQIIEERKEL LENLNIQREE EERRVLEEQR KKQLLLEEER LQREADERER
QRRMEEHKEI KRKHVKDKIE QLKKTGCVKF FQEMDEEELE NLDADEIMAK QVEQLDRERK
ELQAKLKSQE KKVDYLERAK RLEEIPLLQN ALELKRIKAR QLWDQQEQER IKQLIEDRKT
ALQHCERLSR LKTDKEEFIE KLRAARASIH KAKLQEFETR LEAEKQKRSK QRKEERKRER
RIRYEQEKAE EEERKIEEEK RQRIEEEEKA REAKKAAEAA AYEARKQELD RQAAKQKARE
KEIEERRRQQ EEEQLNKGRE ARRGDGIRAR DEVRGGGGGG LSSKADEGDW RRKEDKGEKV
PAWKPRESTT TYWQQKDKES VDKWKPTNDE RRIDESRNDD RRMDDRRNDE RRIDDRRNDD
RRIDDRRNDD RRIDDRRTDD RRIDDRRADD RRIDDRRADD RRIDDRRSDD RRIDEGRSNR
DSRDGDNWRS HDQVVQDEEP ASRDDDDRFR RDTRDIREER RRFVPTRRGR DDLGPSRVDR
SRADEQMTWR RQDDQRGDDR RVTPKDDNRF DDGPRFDRDR EFRDKSPERG ADRNREKYQP
PRGQWNDDKR RRDPGPRDNK DRDSGAKDWG ALRRGADERK SREETEAKRP PVEKIIRKAE
PIKKREGPDE EGWTTVHR
//
