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Database: UniProt
Entry: A0A166L8Q7_9PEZI
LinkDB: A0A166L8Q7_9PEZI
Original site: A0A166L8Q7_9PEZI 
ID   A0A166L8Q7_9PEZI        Unreviewed;       417 AA.
AC   A0A166L8Q7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Peptidase m20 {ECO:0000313|EMBL:KZL63236.1};
GN   ORFNames=CI238_07427 {ECO:0000313|EMBL:KZL63236.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL63236.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL63236.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL63236.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:KZL63236.1}.
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DR   EMBL; LFIW01002839; KZL63236.1; -; Genomic_DNA.
DR   STRING; 1573173.A0A166L8Q7; -.
DR   OrthoDB; 5487978at2759; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02697; M20_like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   417 AA;  44832 MW;  B0C7F4B3299883EE CRC64;
     MSNSAAPTDY QHLDAWIDAH FDEEVEFLQT LVRVPTDTPP GNNAPHAERT ADLLQSFGFA
     AERHPVPEAE VHAYGMESIT NLIVRRRYGA GGRTVALNAH GDVVPPGEGW TRDPYAALVE
     DGVLYGRAAA VSKSDFATFT FAVRALESLG ASLRGAVELH FTYDEEFGGE LGPGWLLRQG
     LTKPDLLIAA GFSYEVVTAH NGCLQMEVTV HGKQAHAAIP DTGVDALKGA VAILNALYAL
     NAGYLQVSSE VEGITHPYLN VGRIEGGTNT NVVPGKVVFK LDRRMIPEEN PAEVEAEIRQ
     TISDAAATVP GILVDIRRLL LANSMRPLPG NKPLVEAIQA HGGEIFGKPV LAMGTPLYTD
     VRLYAEAGVP GVVYGAGPRT VLESHAKRAD ERLQLDDLRR ATKVIARSLR DLLAGEE
//
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