ID A0A0D7ANA9_9AGAR Unreviewed; 436 AA.
AC A0A0D7ANA9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=FISHEDRAFT_63374 {ECO:0000313|EMBL:KIY53350.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY53350.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY53350.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY53350.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
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DR EMBL; KN881618; KIY53350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7ANA9; -.
DR OrthoDB; 1074531at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR CDD; cd03887; M20_Acy1L2; 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:UP000054144}.
FT DOMAIN 214..305
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 436 AA; 47116 MW; D97D9B6FC23FAEE1 CRC64;
MSSNFQPGCI TGLFRPFHEN QFWLSSEALP PYTPQVDKVS DVASTVDHVL DNIDRELRCV
SLQIHSHPEL GFHENFAHDT LTKFLSKYDF KITKHYLGLQ TAFRAEFTHG TGGRVIGINA
EMDALPNGHS CGHNLIAASG VGVAVAIKAA LITHDIPGKV VVIGTPAEEG GGGKIILLER
GGMKDLDAVI MCHPSQGPAR AVNVGSSTAR QSLDVEYFGQ SAHAAEAPWE GVNALDASFI
AYSAISALRQ QMKPTHRVHG IVSGRDWSPN VIPDYAKMQF YVRAPTKDEM DAFTERVKAC
LESGALATGC RMEITYGTGY YELHQNNTLG EAFAEISESY GLTAAHEDTS ASTDFGNVTH
ELPALHPIFA IPAEKSNHSP QFAEAAATEE AHAAMLAISK VLAVLGCKFL QDSEFASEVK
SMMTFVDADR PVCDLL
//
