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Database: UniProt
Entry: A0A4Z1IVH6_9HELO
LinkDB: A0A4Z1IVH6_9HELO
Original site: A0A4Z1IVH6_9HELO 
ID   A0A4Z1IVH6_9HELO        Unreviewed;       423 AA.
AC   A0A4Z1IVH6;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   28-JUN-2023, entry version 12.
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=BOTNAR_0078g00280 {ECO:0000313|EMBL:TGO65401.1};
OS   Botryotinia narcissicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botryotinia.
OX   NCBI_TaxID=278944 {ECO:0000313|EMBL:TGO65401.1, ECO:0000313|Proteomes:UP000297452};
RN   [1] {ECO:0000313|EMBL:TGO65401.1, ECO:0000313|Proteomes:UP000297452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL2120 {ECO:0000313|EMBL:TGO65401.1,
RC   ECO:0000313|Proteomes:UP000297452};
RA   Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA   Valdes J.H., Van Kan J.A.L.;
RT   "Comparative genomics of Botrytis spp.";
RL   Submitted (DEC-2017) 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:TGO65401.1}.
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DR   EMBL; PQXJ01000078; TGO65401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z1IVH6; -.
DR   STRING; 278944.A0A4Z1IVH6; -.
DR   Proteomes; UP000297452; 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:UP000297452}.
FT   DOMAIN          180..351
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          383..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  48275 MW;  975836B3AAEC4DD2 CRC64;
     MAPATQQVFI DGTFEDLAQE LAEYLEIGPE VQPLLAGKQK DEALKKLVTA SEKLNSSPEK
     EFTAAYNLLV YLCNQSPNVN MYLPRICDNL AKPITTSPLN GPGLALNVLT TIFNLLQPDN
     ETRFNVFQAV LKLIKNSGNY EMLRPQLKKL DTWIVEWQIE EEEQRKLFEM IAEVADDSGE
     EEESYQYILK ALRTFDGKDE KAIASESAQK LAIKALRTAI LSNTHFDFHD LTSLPAVQAL
     SDSHAIYSEL LEIFAEKELE DYNDFQDEHD GFVEKENLDN SKLHRKMRLL TLASLAASTH
     TRELEYKRIS KALQVAPEDV EMWVIDVIRA GLVEGKLSQQ KQVFLIHRTT YRVFGEKQWR
     EVATRLDQWK ESLRGVKEVI SRERQAAETQ KEKEIQEADK KVSGTQGMRA GRRSDNMVEM
     GTD
//
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