ID   A0A1X2HY11_SYNRA        Unreviewed;       397 AA.
AC   A0A1X2HY11;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=BCR43DRAFT_484317 {ECO:0000313|EMBL:ORZ03988.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ORZ03988.1, ECO:0000313|Proteomes:UP000242180};
RN   [1] {ECO:0000313|EMBL:ORZ03988.1, ECO:0000313|Proteomes:UP000242180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORZ03988.1,
RC   ECO:0000313|Proteomes:UP000242180};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORZ03988.1}.
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DR   EMBL; MCGN01000001; ORZ03988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2HY11; -.
DR   STRING; 13706.A0A1X2HY11; -.
DR   InParanoid; A0A1X2HY11; -.
DR   OMA; MVHPDEV; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000242180; 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:UP000242180}.
FT   DOMAIN          173..267
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   397 AA;  43518 MW;  6C90A861E06CCA3A CRC64;
     MNKPVEKVID DTIAELSAEL RKISLQIHAN PELGNHEYKA SALLADYLES KGMDVTRHAD
     GMETAFIAEY SNGSGRRVGF CSEYDALPGI GHGCGHNLIA ISGVACALAI KALLERKLLQ
     GTVVLFGTPA EEEMGGKKIF VKKEEVQKRN DFNLMLHPYP GDVMYCNMLA VDTANVEFFG
     KAAHAGMAPW KGINALDALM QAWDNLAMFR QQTLPTNRIH GIIKDGGKRP NVIPDYASAQ
     FLCRSLTRNQ LVELKAKFEN CVRAAAVATK AECKITWDEN GMTEDVFMNE PLTETFKHFM
     GQEGVEYKPR AEEEKISSGS SDYGAISYVI PASHPHFGIG TRAANHTVEF TNAAATEYAH
     TCTIRASRCA AKTAAAVMLD QDLYTAVQAD FRKGKSQ
//