EIF3A_COCIM
ID EIF3A_COCIM Reviewed; 1029 AA.
AC Q1DXU0; A0A0D8JUS6; I9NNH6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=TIF32 {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=CIMG_04873;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; GG704914; KJF61057.1; -; Genomic_DNA.
DR RefSeq; XP_004446109.1; XM_004446052.1.
DR AlphaFoldDB; Q1DXU0; -.
DR SMR; Q1DXU0; -.
DR STRING; 246410.Q1DXU0; -.
DR EnsemblFungi; KJF61057; KJF61057; CIMG_04873.
DR GeneID; 4563021; -.
DR KEGG; cim:CIMG_04873; -.
DR VEuPathDB; FungiDB:CIMG_04873; -.
DR InParanoid; Q1DXU0; -.
DR OMA; VMYQTTA; -.
DR Proteomes; UP000001261; 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 HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1029
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366359"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 621..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..121
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 606..903
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 797..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 118130 MW; 3BC271E8752F64FF CRC64;
MPPIPHVRPE NVLRRAEELI AVGQPAAALS VLHEHVTSKR SRSSPIASLE PVMLLFVELC
VDLRKGKSAK DGLYQYKNIA QNTNVGTIEM VLKKFIELAE QKVTEAQAKA DEIQSSLESA
APTSNVEDLD AIETPETILL ATVSGEQSRD RTDRAVVTPW LKFLWETYRT VLEILKNNAR
LEVMYQATAL QAFQFCLKYT RKTEFRRLCE LLRNHVQNAA KYSAQMHAIN LSDPDTLQRH
LDTRFQQLNV AVELELWQEG FRSVEDIHTL LNLSKRQPKN IMMANYYEKL TKIFMVSDNY
LFHAAAWNRY YNLLRQSAIA LAAGQGSKKD SPSVTEADMT KAASFVLLSA LSIPVISTSR
SRGALVDVDE VRKNKNTRLT NLLGMPQPPT RASLFKDALN KGLLSRCRPE IRDLYNILEV
DFHPLSICKK ISPILKEIGA DPEMEKYVLP LQQVILTRLF QQLSQVYESV ELKFVHELAH
FPEPFQVTSS MIEKFIMNGC KKGDLAIRVD HVSGVLTFES DIFSSAKALH PGSAAGSAES
EVGSVQRLQS TPAEIARSQL ARLAKTLHVT CMYVDPSYNQ ARIKAKEAAH ARARAGAAKE
HEETLTRRAI IEKRKEALSD ALQKKQREEE NRKRARNQQL QEAEQQRLLD EHRERERKRM
KDEQDRIRQQ ELKKQLEELK TGVKGIDVNQ IDLEELDSNR LRAIKLAQLE KEKNDLNEKI
RITSKRIDHL ERAFRREELK HLPEDYETQK KQDLETYEQT KEETLKAARQ KHKEDVALKH
RLSRLVPYFN DFKKSVTEKR HEEFERRRKA ADREFEQKKK QRIKEVHERI RRERAEREAE
EQRRREEEER IAREEQERIA KEEERRRALA EEKAAREEQR RKLDEQAIRQ RQREEEAEQR
RAARKAGLAE PRGPAREASP ERTAPRLNLA GRTGTSWRDR QAAKAAASAG EQPAAAQEAT
PAPPAKAGSY LPPHLRATRD GPSDSRDLSH ARESAAPPRQ FSRSPVPPSG APSSQEKPGP
WRPRFKQQQ
