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Database: UniProt
Entry: A0A2B7WWA1_9EURO
LinkDB: A0A2B7WWA1_9EURO
Original site: A0A2B7WWA1_9EURO 
ID   A0A2B7WWA1_9EURO        Unreviewed;       475 AA.
AC   A0A2B7WWA1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-JUN-2023, entry version 17.
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=AJ79_08088 {ECO:0000313|EMBL:PGH00837.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH00837.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH00837.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH00837.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-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:PGH00837.1}.
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DR   EMBL; PDNB01000180; PGH00837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7WWA1; -.
DR   STRING; 1447875.A0A2B7WWA1; -.
DR   OrthoDB; 2786882at2759; -.
DR   Proteomes; UP000223968; 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:UP000223968}.
FT   DOMAIN          211..380
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          431..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  51668 MW;  D721BC1381682166 CRC64;
     MASLPNTLLI EGSFAELADE LAQYIDAIHK SDKGVHAEIT PALEALRQKE LLEGEPNEAQ
     KQQILAQRDE VLKKIVVAAA ALNAAPEKEI TAAYNLLIHL IRQSSSVDMF LPRICGYLAK
     PFTSSPQHGS SLALTILSTI FNTLAPQDTG RYHVFLAILA VIRSASPSAF SALKPQLDTQ
     LPTWLSSWDL DEEDLQRLHL AISDVASDSG DRDLAHKHLV SALQAIPASD ASTPEAHSIA
     LRALLSALTS PSVFDFTPLT SSDAIQALRT SEPQLFELLE IFSADTLDAY EDSIATTPLS
     SIHNLAESAE ALQTKMRLLT LASLSASTPS RSLPYDTIAS ALRIDRADVE KWVIDTIRAG
     LVEGKLSQLK GEFLVHRATY RVFGEKQWAE VQGRLMVWRR SLENVLGVVR AEREKFVREE
     MVAASAAANA IEGGAGGQGQ RGGERRRGGG HHGGRQQRDQ EREQPREVDL VGGGD
//
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