ID A0A0F4GFK9_9PEZI Unreviewed; 445 AA.
AC A0A0F4GFK9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 28-JUN-2023, entry version 28.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000256|HAMAP-Rule:MF_03012};
DE Short=eIF3m {ECO:0000256|HAMAP-Rule:MF_03012};
GN ORFNames=TI39_contig4149g00016 {ECO:0000313|EMBL:KJX94945.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX94945.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX94945.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX94945.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC 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_03012}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03012}.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000256|ARBA:ARBA00008482}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000256|HAMAP-
CC Rule:MF_03012}.
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:KJX94945.1}.
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DR EMBL; LAFY01004108; KJX94945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GFK9; -.
DR STRING; 1047168.A0A0F4GFK9; -.
DR OrthoDB; 2786882at2759; -.
DR Proteomes; UP000033647; 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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; 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_03012; eIF3m; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR027528; eIF3m.
DR InterPro; IPR040750; eIF3m_C_helix.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; COP9 SIGNALOSOME COMPLEX SUBUNIT 7/DENDRITIC CELL PROTEIN GA17; 1.
DR PANTHER; PTHR15350:SF2; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT M; 1.
DR Pfam; PF18005; eIF3m_C_helix; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03012};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03012};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03012}; Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 197..365
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49639 MW; 69D2AB51F8DDA62C CRC64;
MPGISKLSLV EGAFEELSLE LATYLDNAKG EGSSLATDIT PLLADPEKSD RPTETDRDAV
LKKLVTASSI LNGAPERELQ AAYNLLIHLV SQAEDPDQYL PHICRYLTAP VTSSPHNGTG
IALGILSTLF NTLEPDDESR YHVLLAIINV IKNSGNYETL APQLKAVDSW VQEWELEPED
ARKLYLAIAD AANAAHESEQ SYSFLLKALR TTQNDASSAE ARELSVRALK LALQNEKHFD
FQDLTALDSI QALRKSDPTW FELLELFSSE NYDDFQDFKE GNDSFVSENS LDEDILDKKM
RQLTLASLAA QASSSRTLPY GHIAKALNIS TEDVEMWVID SIRSGLVEGK LSQQKQEFLV
HRSTYRVFGD NQWREVASRL ETWRSSLTNV LAVIRAQKED HAREKELEAS GHGASGGGQG
GFRNHNQRQR NDQQQRQQPQ AVEVE
//
