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Database: UniProt
Entry: A0A167DUJ6_9PEZI
LinkDB: A0A167DUJ6_9PEZI
Original site: A0A167DUJ6_9PEZI 
ID   A0A167DUJ6_9PEZI        Unreviewed;       449 AA.
AC   A0A167DUJ6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=CI238_10779 {ECO:0000313|EMBL:KZL84364.1};
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:KZL84364.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL84364.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84364.1,
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
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:KZL84364.1}.
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DR   EMBL; LFIW01000876; KZL84364.1; -; Genomic_DNA.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05672; M20_ACY1L2-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF4; PEPTIDASE M20 DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT   DOMAIN          212..302
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   449 AA;  48072 MW;  785A6097AE98CBE6 CRC64;
     MGIHRFSRTL FVALGASSVA ASSVLPRQNN ETSGNASPYL EAVSEYIDSI VDDLWPINKE
     IHDNPELGYE EVKAHDLLTS FMESHDGWNV TRSIYNISTA FVAVFEGSGD GPVVSFNAEY
     DALPGLGHAC GHNLIATASI GGALATAEIM RTENLPGQVI LFGTPAEESL GGKVKLLEAG
     AFRDHNIDIS LITHPTAGGD SPYMITTSTD RFEVEYYGKE AHAAAQPWEG VNAQDALVLA
     NNAIALLRQQ TRSTDKIHGI ITSAGTRINV IPALAQASFQ IRSANDEALE EWTERVMKCF
     DAGSLATGAE LNVTMRPYGY SNMVSNDVLA GSYAKYFTEL GGELPDADVD KLRDPSGSTD
     QGNISHDFPT ISPYFGITNE NGSVPTGGTH TAAFEVAAGS RPAFDKAIMV AKSIAGVAVD
     VLTVDGMLDK IKEEFETTQS KRRKSRSVD
//
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