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Database: UniProt
Entry: A0A4T0WJ51_9PEZI
LinkDB: A0A4T0WJ51_9PEZI
Original site: A0A4T0WJ51_9PEZI 
ID   A0A4T0WJ51_9PEZI        Unreviewed;       296 AA.
AC   A0A4T0WJ51;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JUN-2023, entry version 10.
DE   SubName: Full=COP9 signalosome complex subunit 7a {ECO:0000313|EMBL:TID06771.1};
GN   ORFNames=CH35J_001170 {ECO:0000313|EMBL:TID06771.1};
OS   Colletotrichum higginsianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=80884 {ECO:0000313|EMBL:TID06771.1, ECO:0000313|Proteomes:UP000305883};
RN   [1] {ECO:0000313|EMBL:TID06771.1, ECO:0000313|Proteomes:UP000305883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TID06771.1,
RC   ECO:0000313|Proteomes:UP000305883};
RX   PubMed=31028389; DOI=.1093/gbe/evz087;
RA   Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA   Shirasu K.;
RT   "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT   Pathogenic Fungus Colletotrichum higginsianum.";
RL   Genome Biol. Evol. 11:1487-1500(2019).
CC   -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008482}.
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:TID06771.1}.
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DR   EMBL; MWPZ01000001; TID06771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4T0WJ51; -.
DR   EnsemblFungi; CCF33257; CCF33257; CH063_00941.
DR   Proteomes; UP000305883; Unassembled WGS sequence.
DR   InterPro; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR15350:SF5; COP9 SIGNALOSOME COMPLEX SUBUNIT 7; 1.
DR   PANTHER; PTHR15350; COP9 SIGNALOSOME COMPLEX SUBUNIT 7/DENDRITIC CELL PROTEIN GA17; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000305883}.
FT   DOMAIN          1..159
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          220..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  32417 MW;  47B260CF65A143E4 CRC64;
     MEQTKSLNAL EPFLALSKSA TSSRAAADLV TRATSNPNTF LFTELLETPQ IQALSQSPDF
     LPHLRLLEIF SHGTYTAYLA SGQQLPQLND AQTLKLRQLS LLTLARDRSN LTYAALQSAL
     DLPSARALED LVISAIYAGL LDATLDPHRQ AVQVNSLAAL RDLAPGAVPP MIRALHAWSS
     RCESTLEDLE SQIAGIREAA VRRQDDKAEQ DARLAKMVDE VRKDPEAGAG RKLAVGHGGG
     GERGTSFLGH TSRAQRYNKR GSTSMMDNTE ELDDEAMDVD EEDPEQEKKR ASRRKL
//
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