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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//