ID E9EFK9_METAQ Unreviewed; 1056 AA.
AC E9EFK9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=MAC_08657 {ECO:0000313|EMBL:EFY85301.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY85301.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY85301.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698582; EFY85301.1; -; Genomic_DNA.
DR RefSeq; XP_007814997.1; XM_007816806.1.
DR AlphaFoldDB; E9EFK9; -.
DR STRING; 655827.E9EFK9; -.
DR GeneID; 19252968; -.
DR KEGG; maw:MAC_08657; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; E9EFK9; -.
DR OMA; EHITNKR; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000002499; 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:EFY85301.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 338..522
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 120329 MW; D75D3C8391A8828C CRC64;
MPPPPHQKPE NVLKRAHELI GVNQAPAALN LLHEHVTSKR SRNVPIASLE PVMLLLVELS
VEQKKGKLAK DALYQYKNIS QNTNIGTIEL VLKKFIELAV EKVTAAQQKA DEVQSSIDAT
ATTNVDDLEA TETPESILLA TVSGEQSRDR TDRAIVTPWL KFLWEAYRTV LDILRNNARL
EVLYQSTAMQ AFDFCLKYTR KTEFRRLCEL LRNHVQTAAK YSSQMHAINL SDPDTLQRHL
ETRFQQLNVA VELELWQEAF RSVEDIHTLL SLSKRPPKNV MMANYYEKLT RIFLVGENYL
FHAAAWSRYY TLLRQSSVLV ASGQGKKADN PPASDADLQK AASFVLLSAL AIPVISTSRS
RGAMVDFDEA RKNKNSRLTH LLGMTQAPTR NRLFRDALSK SLLQRARPEI RDLFNILEVD
FHPLSICQKI SPILTKIGED AEMERYIVPL QQVILTRLFQ QLSQVYETVD LSFVETLAQF
PEPYQVTRGT IEKFIMNGNK KGDLAIRMDH ATGVLSFDND VFSSAKAGSA GSAESETGTV
QRLQSTPSDI VRSQLTRLAR SLYTTCHYID PNFNKERAAA RQAALQRAKA GAEQERQDIL
ARKETIQKRK EEASELQARR EKENARQKRL REQALQEAED KRLAAEQKER EAKRLQAERD
RVRKDELKKQ IAELKMSDKV LDIDLDDLDN LDTNRLRAMK LAQLEREKND VNEKLRITGK
RFDHLERAFR KEEVKKLGED YAKQVEVDRT IYEKVKAKTL KEAEEKHKES VELKHRLTRL
VSYYEDFRSS LHERRRDEFE KRRRDAEREL EKQIAARKKE FRDRRLREKR EREEKERELR
EAEERAAREK EEQRQREEAR KAELAKLKEQ RDKERQEMLE KAALQQRREE EALARRKAEK
GAGAAPLRTE TPEGRKPPVI GSGSWREREA SKNAAAAAAA GAASTSESRP GPAMERTDSN
DRPSGPPRLQ LAGSGNKPSW RDRQAAKGDA PSSSDNTPPP ATSRGFGGPR GAAPSMDRGG
SNRGDNGRTS SPAPQSESLP PRTAGKWVPP HLRNKA
//
