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Database: UniProt
Entry: A0A0D2BY70_9EURO
LinkDB: A0A0D2BY70_9EURO
Original site: A0A0D2BY70_9EURO 
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
//
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