ID A0A067PKL2_9AGAM Unreviewed; 390 AA.
AC A0A067PKL2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=JAAARDRAFT_38566 {ECO:0000313|EMBL:KDQ54400.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ54400.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
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DR EMBL; KL197729; KDQ54400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067PKL2; -.
DR STRING; 933084.A0A067PKL2; -.
DR HOGENOM; CLU_031812_1_1_1; -.
DR InParanoid; A0A067PKL2; -.
DR OrthoDB; 1074531at2759; -.
DR Proteomes; UP000027265; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
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:SF0; XAA-ARG DIPEPTIDASE; 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:UP000027265}.
FT DOMAIN 173..264
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 390 AA; 42024 MW; 801EA2A32AD5EE9E CRC64;
MKTIEERIDE LSPELRKLSL QIHDHPEIMF QEKYAHDTLT AFMSSHGFTV TKHFCSLPTA
WRAEYTYKTG GRTLGINSEM DALPEIGHAC GHNLIAISGV GVALAVKTAL EKHDVPGRVV
LLGTPAEEGG AGKVIMIEEG GYKGLDACIM CHPGPGPAHS VGLGSSLAVQ NIEVEYFGHT
AHASAAPWEG TNALDAAFLA YSSISVLRQQ IKPTHRVHGV IKGKDLAANV IPDYTKMLWL
VRAPTWAELE ILRERVKACL EAASLATSCK IAMSFGRGTY DLRQNSVLAS SFGDTIKARY
GWSTTDAEGA IGGSTDFGNV TYEMPAIHPS FAIPTEQNGG NHTRGFTAAA RTITAHEICL
TVTKSLALTG FRVINDDTFF HGAKQAFENS
//
