ID A0A084Q8L7_STAC4 Unreviewed; 476 AA.
AC A0A084Q8L7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=S40285_07695 {ECO:0000313|EMBL:KFA60302.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60302.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA60302.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60302.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR037242-3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KL660937; KFA60302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084Q8L7; -.
DR STRING; 1283841.A0A084Q8L7; -.
DR MEROPS; M20.017; -.
DR HOGENOM; CLU_029469_3_0_1; -.
DR InParanoid; A0A084Q8L7; -.
DR OMA; HITIPGF; -.
DR OrthoDB; 177966at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
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; IPR017153; CNDP/DUG1.
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 PIRSF; PIRSF037242; CNDP_dipeptidase; 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 Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 214..366
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 195
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 228
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 343
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 417
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT SITE 228
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ SEQUENCE 476 AA; 52484 MW; 1F86B735C316A9A1 CRC64;
MAPQLDSFFK QVDSSADAFI ERLRKAVAIP SISAEDARRP DVVRMGEFLA DELKSLGASV
ELRPLGKQPH KEHLDLPPVV IARYGNDKNK RTILVYGHYD VQPAEKSDGW ATNPFELTVD
DKGRMFGRGS TDDKGPVLGW LNAIEAHQKA GVDFPVNLLM CFEGMEEYGS EGLDDFIHAE
AKKYFADAEA VCISDNYWLG TEKPCLTYGL RGCNYYSIEV SGPGADLHSG VFGGTAQEPM
TDLVRVMGSL VDTNGKIQIP GIQEQVAPVT EEEDGLYENI SFTMDNIYES LGSKTTVFED
KKSTLMARWR NPSLSLHGIE GAFSSPGAKT VIPAKVIGKF SIRTVPDMEI DKTNAAVQKY
VEEQFAKLGS KNTLKVYPQH CGKWWVASPK HWNFSAAAKA VERVWGVEPD YTREGGSIPV
TLTFEEATGK NCLLLPMGSS TDGAHSINEK LDKRNYIEGI KLLGAYLHYV AEEPQV
//
