ID A0A0D2BY70_9EURO Unreviewed; 1101 AA.
AC A0A0D2BY70;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 3 110 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03000};
GN Name=TIF32 {ECO:0000256|HAMAP-Rule:MF_03000};
GN ORFNames=PV07_11496 {ECO:0000313|EMBL:KIW23285.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23285.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23285.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23285.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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; KN847046; KIW23285.1; -; Genomic_DNA.
DR RefSeq; XP_016243501.1; XM_016398939.1.
DR AlphaFoldDB; A0A0D2BY70; -.
DR STRING; 569365.A0A0D2BY70; -.
DR GeneID; 27350690; -.
DR VEuPathDB; FungiDB:PV07_11496; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000054466; 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:KIW23285.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 341..525
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 622..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..123
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 828..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 124875 MW; CE6CFC1A2B86AB4B CRC64;
MPPPPHIRPE NVLRRAQELI AVDQTQAALN VLHEHVTSKR SRNSPISSLE PVMLLFVELC
VDLRKGKSAK DGLYQYKNIA QNTNVGTIEL VLKKFIELAE QKVQEAQAKA DQVQSSLESA
ASATALNVED LEATETPETI LLATVSGEQS KDRTDRAIVT PWLKFLWETY RTVLEILKNN
ARLEVMYQST AHQAFDFCLK YTRKTEFRRL CELLRNHVQN AAKYSSQMHA INLNEPDTLQ
RHLETRFRQL NVADELELWQ EAFRSVEDIH MLLTLSKRPA KNVMMANYYE KLTKIFLVSD
NFLFHAAAWN KYYNLLRQSA AAIASGQSPK RDNPAVTEDS LTKAASFVLL SALAIPVIST
SRSRGALVDV DEARKNKNNR LTNLLSMPFA PTRAGLFKDA LSKGLLKRVR PEIRDLYNIL
EVDFHPLSIC KKISPILAQI GADPEMEKYV LPLQQVILTR LFQQLSQVYE SVELSFVTRL
AQFPAPFEVT PAMIEKFIMN GCKKGDLSIR LDHISGILAF DSDVFSSAKA LHPGSAAGSA
ESEVGSVQRL QNTPAEIARS QLTRLAKTLH VTCMYVDPSY NQARLAARET ALARAEAGAE
QEHQETLERR VVIEKKKEAA SEAFQKRQRE EETRRRIRAQ QQAEAESQRL RDETRARELK
RVKDEQARIR RQEIEKQLAE LQSGMKIDLQ DVNIDELDSN QIRYLKLSQL EKDKKEKDER
IRITAKRLDH LERAFRREEL KYQQSDYEKQ REEDMKIYEQ NKELMLKEAQ EKHKEGLALK
HRLSRLVKEY DTFKGQITER RAAEFERLRK RAEREFEEEK RKRIKAYHEE KARQRAAQEA
EERRIREEEE RRQREDEEKA KAEEEKKRVA AERRAQAEAA RLEREEAARK QMQREEEAAA
RRAARKAEQG APVPAPAPFS RGGPREAPPM EARTESQEGP RTAPRLQLAG KAGGGWRERQ
AAKEASIPGG PGPVPAEASA PSQAAPSVQE PPARRQGGYV PPHLRESGSA RSGPDHPPAR
DYHHPPARDH HPPARNASAS PANGAQGGRY VPMHMRDGGR SLSREGAGSP AQGSGDEAAQ
RKPASGGPGR YVPPSMRSRQ Q
//