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Database: UniProt
Entry: A0A165EWA4_9APHY
LinkDB: A0A165EWA4_9APHY
Original site: A0A165EWA4_9APHY 
ID   A0A165EWA4_9APHY        Unreviewed;       481 AA.
AC   A0A165EWA4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   SubName: Full=CNDP dipeptidase {ECO:0000313|EMBL:KZT07902.1};
GN   ORFNames=LAESUDRAFT_724370 {ECO:0000313|EMBL:KZT07902.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07902.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT07902.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT07902.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; KV427617; KZT07902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165EWA4; -.
DR   STRING; 1314785.A0A165EWA4; -.
DR   InParanoid; A0A165EWA4; -.
DR   OrthoDB; 177966at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd05676; M20_dipept_like_CNDP; 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; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT   DOMAIN          213..372
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   481 AA;  52103 MW;  31054998506C95DB CRC64;
     MPAPDKFLSF IDEHADKFIK RLGEAVAIPS ISGDAAHRQD VFKMGNWLQG QLNTVGVQTK
     LVDLGKHVMD GQELQLPPAI LGRIGDDSKK KTVLIYGHYD VQPAELSDGW DTEPFKLVVD
     EASGRLIGRG ATDDKGPILG WLNVLEAHKT LGLELPVNLR FCFEGMEESG SEGLDDLIKS
     EVAKGKDGWF DGVDCVCISD NYWLNNRTPC ITYGLRGIAY FKVTVSGPTR DLHSGIFGRT
     VYEPMTALVA LMSKLVAPDG TILVPGVEDL VPNATDEEIA IYNKLDYSVQ DVEQAAGAPI
     AISSDKATVI MGRMRMPSLS LHGIEGAFSG AGGKTVIPAS VSGKFSIRLV PPQTPEDIAT
     LVEKYLKDEF AKLNTKATLK IENLHGGKPW VADHKHWNFE AAKIATRAVY NRDPDLTREG
     GSIPVTLTFA DSLGVNVLLL PMGRGDDGAH STNEKLDRSN FLKGSKLLGT YLYEVGAIAT
     A
//
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