ID W9ZNY5_9EURO Unreviewed; 488 AA.
AC W9ZNY5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 28-JUN-2023, entry version 35.
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=A1O1_01340 {ECO:0000313|EMBL:EXJ96214.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ96214.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ96214.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ96214.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ96214.1}.
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; AMWN01000001; EXJ96214.1; -; Genomic_DNA.
DR RefSeq; XP_007720443.1; XM_007722253.1.
DR AlphaFoldDB; W9ZNY5; -.
DR STRING; 1182541.W9ZNY5; -.
DR GeneID; 19156242; -.
DR eggNOG; KOG2753; Eukaryota.
DR HOGENOM; CLU_035254_0_1_1; -.
DR OrthoDB; 2786882at2759; -.
DR Proteomes; UP000019484; 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; 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 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:UP000019484}.
FT DOMAIN 213..381
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 421..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 53363 MW; 94BF16ED403B474A CRC64;
MPGPTNTLLI EGTFSELAEE FAQYLDALSK AEEGAGVQAE IADPLNIIRE AEQGEEAVEA
STIQPQKDEV LKKLVTKASI LNSAPEREFT PAYNLLISLS LQSPIYEQFF ARICQYLSEQ
PVTSSAVYGA SLALQSLTTV FNVLPPTSEA RYHVFLAILK VIKATSSSQA FEALIPQLET
NIPEWLAAWQ LDDEDARSLY TAVADVAAVS GNDDLSYAYL MKALETIPPE SAADGEAQEL
AKRTLRLALT NPSVTDFTAL TANDAIQAIR RADSNLFDLL EIFSSDDYSS YIDFLETNEL
SSLGIQEESG DVLSTKIRLL TLASIAATSQ TRSVSYSTIA SALQVPSEDV EMWVIDTIRA
GLVEGKLSQL KQEFLVQRAT YRVFGEKQWT EIQGRLLVWR RSLESVLSVV KAERERFLRE
GPTHADAGVN GWGDGGDNQR GHYGGDRQRR QGGGGGGGRR GGGGQYREHR EQREQQGPRE
VEAVGGGD
//
