ID A0A2B7X5E9_9EURO Unreviewed; 1070 AA.
AC A0A2B7X5E9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=GX51_02129 {ECO:0000313|EMBL:PGH06884.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH06884.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH06884.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH06884.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH06884.1}.
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DR EMBL; PDNC01000018; PGH06884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7X5E9; -.
DR STRING; 2060905.A0A2B7X5E9; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000224080; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000,
KW ECO:0000313|EMBL:PGH06884.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 622..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 122528 MW; 2AAFA562BA628B54 CRC64;
MPPPPHIRPE NVLRRAEELI AVGQQQAALT VLHEQVASKR SRNSPIASLE PVMILFVELC
VDLRKGKSAK DGLYQYKNIA QNSNVGTIEM VLKKFIELAE QKVTEAQAKA DEIQSSLESA
APSTNIEDLD AIETPETLLL ATVSGEQSRD RTDRAIVTPW LKFLWETYRT VLEILKNNAR
LEVMYQTTAL QAFQFCLKYT RKTEFRRLCE LLRNHVQNAA KYSSQMHAIN LSDPETLQRH
LDTRFQQLNV AVELELWQEG FRSVEDIHTL LNLSKRPAKN IMMANYYEKL TRIFLVSENY
LFHAAAWSRY YNLLRQSAAA VAAGQSPKKE NPVISEAEMT KTASFVLLSA LSIPVISTSR
SRGALVDVDE ARKNKNTRLT NLLGMSQAPT RAALFKDALN KGLLSRCRPE IRDLYNILEV
DFHPLSICKK ISPILTQIGA DPEMEKYVLP LQQVILTRLF QQLSQVYESV ELKFVHELAQ
FPEPFQVTRS MIEKFIMNGC KKGDLAIRVD HISGVLTFDS DIFSSAKAMH PGSAAGSAES
EVGSVQRLQS TPAEIARSQL TRLAKTLHLT CMYVDPSYNQ VRIQAKQIAF AKAKAGAAKE
HEETLARRIV IEKKKEAALE SLQRKQQEEE RQKRIRTQQL QDAEKRRLHD EHLERERKRL
QDEKDRIRQE ELKKQLEELK TGVKGIDVSE INLEELDSNS LRTIKLAQLE KEKNELNDRV
RITAKRIDHL ERAYRREELK HIPADYEAQR KRDLEIYEKN KADTLAAAKL KHQEDVALKH
RLSRLVPFFN DFRKNIQEKR HVEFEKNRKA AEREFENKKR QRIKEVQERL RRERMEREEE
ERRQREEQER IEQEEQEKAA RDAERRRQLA AEKAAREEER RILDEKAAIQ KKREEEAEAK
LKARKAGAGA VPVRMERTES TERTAPRLNL AGRTGPTWRE RQAAKEAEAA AAGSATPPTE
AAAPVANEEL PPPRTTGGYV PPQRRGAAPG RELSANGERM PERAPERERM PERMPPRFSR
EAVPPPKSLS RSPAPTSSSP APESREGSNP PAGGATQAWR PKFRQQQQQQ
//
