EIF3A_CHAGB
ID EIF3A_CHAGB Reviewed; 1061 AA.
AC Q2H6G4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=CHGG_05751;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ89132.1; -; Genomic_DNA.
DR RefSeq; XP_001221846.1; XM_001221845.1.
DR AlphaFoldDB; Q2H6G4; -.
DR SMR; Q2H6G4; -.
DR STRING; 38033.XP_001221846.1; -.
DR EnsemblFungi; EAQ89132; EAQ89132; CHGG_05751.
DR GeneID; 4391313; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; Q2H6G4; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000001056; 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..1061
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366358"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 609..724
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 789..906
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 828..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 120569 MW; 3E819869C28CE223 CRC64;
MPPPPHQKPE NVLKRAHELI GVNQAPAALT LLHEHITSKR SRNVPIASLE PVMVLLVEQA
VEQKKGKLAK DALYQYKNIA QNTNVGTIEL VLKKFIELAA EKVTAAQQKA DEVQSSIEAT
TGSSSVEDLE ASETPESILL ATVSGEQSKD RTDRAIVTPW LKFLWEAYRT VLDILRNNAR
LELLYQSTAM QAFDFCLKYA RKTEFRRLCE LLRNHVQTAA KYSAQMHAIN LNDPDTLQRH
LETRFQQLNV AVELELWQEA FRSVEDIHTL LSLSKRPAKN IMMANYYEKL TRIFLVGENY
LFHAAAWSRY YNLLRQSAAM LATGQSKKSD SPPVSEADLQ KAATFVVLSA LSIPVISTSR
SRGAMVDFDE ARKNKNSRLT HLLGLSQAPT RSSLFRDVLS KALLRRASPQ IRDLYNILEV
DFHPLSICQK ISPILAQVGA DEEMQKYILP LQQVILTRLF QQLSQVYETV DLEFVQSLAQ
FPEPFQVTRG TIEKFIMNGN KKGDLAIRMD HATGVLSFDV DVFSSAKAVH AGSAAGSAEN
ESGSVQRLQS TPSQIVRSQL TRLAEVLYTT CRYIDPSFNE ARINARDAVL ARAKAGAEKE
HLEILSRKEV IQKRKDKASE IQAQKEKELA RKKMLQEQAL QQAEAQRLAE EQKIREQKRM
AAEREEIKKK EVEGMLKDMK LDDVELEDLD NLDSNKIRMI KLQQLEREKN TIAEKLRVTG
KRLDHLERAF RKEEAKKLPE DYAKQRERDI AAYELIKAQT LKEAELKHKE DVELKHRLTR
LMPFYESFRA DLHERRRDMF EKRRRDAERE LEKQVTLRRK EYRERKLREK REREEKERAL
REAEERAERE KEEEKQRQEA RKEELARLRE EREKERERAK EAQARQQQRE EEAMARRRAE
KAAAAAVPIR EREPFAATGS GPRLPLAGTK STWREREAAK AAGGGAPSDS GPPPARAAPP
PIERTDSRDR PAAGPPRLAL AGNKPSWRER EAAKNAAGGA PPPERSGPPP RVASGRGEPM
DRAGSGRGGD RDARDNNGPA PEPLKASGGP GKYVPKFRRE G
