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Database: UniProt
Entry: M7B821_CHEMY
LinkDB: M7B821_CHEMY
Original site: M7B821_CHEMY 
ID   M7B821_CHEMY            Unreviewed;      1266 AA.
AC   M7B821;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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};
DE   AltName: Full=eIF-3-theta {ECO:0000256|HAMAP-Rule:MF_03000};
GN   Name=EIF3A {ECO:0000256|HAMAP-Rule:MF_03000};
GN   Synonyms=EIF3S10 {ECO:0000256|HAMAP-Rule:MF_03000};
GN   ORFNames=UY3_11192 {ECO:0000313|EMBL:EMP31690.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP31690.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC       EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC       EIF3M. {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; KB544240; EMP31690.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7B821; -.
DR   STRING; 8469.M7B821; -.
DR   Proteomes; UP000031443; 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   ECO:0000313|EMBL:EMP31690.1};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03000}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT   DOMAIN          315..498
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          828..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          558..634
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT   COILED          667..701
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT   COMPBIAS        867..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1073..1208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1225..1266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1266 AA;  151596 MW;  619F9251CF93EE98 CRC64;
     MPVYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD
     LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK TEAAKEESQQ MVLDIEDLDN
     IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ
     AFKFCLQYTR KAEFRKLCDN LRMHLGQIQR HHNQSTAINL SNPESQSMHL ETRLVQLDSA
     ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYHKVS TVFWKSGNAL FHASTLHRLY
     HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG
     LQAPPTRISL INDMVRFNVV QHVVPEVKEL YNWLEVDFHP LKLCDRVTKV LNWVRDQVEK
     EPELQLYVPH LQNNTILRLL QQVAQIYQTI DFSRLTTLVP FVDAFQLERA IVDAARHCDL
     QVRLDHTSRT LSFGSDLNYS TREDAPLGPQ LQSMPSEQIR NQLTAMSSAL AKALEVIKPP
     NIVQEKEEQH QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
     LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
     LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KTAYEEQRIR
     DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDKDLF VSRLMAARQS VYQEKLKQFE
     ERLAEERHNR LEERKRQRKE ERRISYYREK EEEEQRLQEE KMLKELEEKE RIEREKREQE
     QREYQERVRK LEEVERKKRQ RELEIEERER RREEERRGLD DPLSRRESRW GDRDSDSTWR
     RTAEPESEWR RAPPEREWRR GEGRDDERPF RRGDDLLRRG GAEEKEPSSQ EANEDRAPKR
     DVDKDGEPRR DEDGEPKRGV NGEPRRGVDE DGEPRQEEDR EPRQDDDRGP RRGLDDDRIS
     RRDEDRGPWR SADEDRLSRR DDDRGPWRGG DDDRGPRRGD DSRPGPWRPF GKPGGWRERE
     KAREDSWGPP RDSRPSEDCE LDRDKDCDEN EKDREIDKER DLDRDDRFRR PRDEAPWRRG
     PAEEASSWRD SNRRDEWDRG GRDMRDRRGD DRDRRGLPIR TDREETSSWR RGDERKEERG
     EEHETTRRAA PAPTPVPAAA PPPPISKDRE RDAESEKGSW RTEKERESLR RTKNETDEDG
     WTTVRR
//
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