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Database: UniProt
Entry: A0A1Q8RVX7_9PEZI
LinkDB: A0A1Q8RVX7_9PEZI
Original site: A0A1Q8RVX7_9PEZI 
ID   A0A1Q8RVX7_9PEZI        Unreviewed;       458 AA.
AC   A0A1Q8RVX7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-JUN-2023, entry version 24.
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=CCHL11_01736 {ECO:0000313|EMBL:OLN88654.1};
OS   Colletotrichum chlorophyti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN88654.1, ECO:0000313|Proteomes:UP000186583};
RN   [1] {ECO:0000313|EMBL:OLN88654.1, ECO:0000313|Proteomes:UP000186583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTL11 {ECO:0000313|EMBL:OLN88654.1,
RC   ECO:0000313|Proteomes:UP000186583};
RA   Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT   "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT   herbaceous plants.";
RL   Submitted (NOV-2016) 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:OLN88654.1}.
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DR   EMBL; MPGH01000087; OLN88654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8RVX7; -.
DR   STRING; 708187.A0A1Q8RVX7; -.
DR   OrthoDB; 2786882at2759; -.
DR   Proteomes; UP000186583; 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:UP000186583}.
FT   DOMAIN          187..358
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          392..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  52277 MW;  D2C453A98E799D40 CRC64;
     MAAGAKQQAQ PQLLFVDGSF QELAREMADY LHIADEVKPL VDDEAKKEEV LAKLVRSSAA
     LSSVPEKEFT AASNLMIHLV LQSEDPKKHL PTLCQAFSKP ISSSPVNGVG LSLNALSTVF
     NLIEPENPIR FNVFMAILRF LKTHSMFDTV QPYLKHIPSW FEDWATSEDY QREMYELIAE
     VAKEAGKEEE SYEYILKALR TFGGDDNKDI GSEEAQKLSL RAVRDALLSS THFLFTDIRS
     IPSVQNLSET HPIYSQLLDI FAEQDLEDYN DFNDEHQGFL EKESLDHDKL HRKMRLLTFA
     SLAAQTTSRR IEYGAIAKAL QIPASDVEMW AIDVIRAGLV EGKLSQQDQV FLVHKVTYRV
     FGTRQWQELA TRLDSWKGTF VNLHDVIRKE QANAKAQKER EAQEAERKLQ NPGNEGGAGG
     RQQRQGRRDN QQREPREPRE PREPREPREP KERTDNDD
//
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