ID   DPEP1_ARTGP             Reviewed;         425 AA.
AC   E5R2Q7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Putative dipeptidase MGYG_00085;
DE            EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
DE   Flags: Precursor;
GN   ORFNames=MGYG_00085;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Hydrolyzes a wide range of dipeptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10073};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10073};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR   EMBL; DS989822; EFQ97041.1; -; Genomic_DNA.
DR   RefSeq; XP_003175993.1; XM_003175945.1.
DR   AlphaFoldDB; E5R2Q7; -.
DR   SMR; E5R2Q7; -.
DR   GeneID; 10031304; -.
DR   VEuPathDB; FungiDB:MGYG_00085; -.
DR   eggNOG; KOG4127; Eukaryota.
DR   HOGENOM; CLU_031404_4_2_1; -.
DR   InParanoid; E5R2Q7; -.
DR   OMA; WSGNVLR; -.
DR   OrthoDB; 5476406at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01301; rDP_like; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443:SF12; DIPEPTIDASE; 1.
DR   PANTHER; PTHR10443; MICROSOMAL DIPEPTIDASE; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   3: Inferred from homology;
KW   Dipeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..425
FT                   /note="Putative dipeptidase MGYG_00085"
FT                   /id="PRO_0000411211"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ   SEQUENCE   425 AA;  46723 MW;  8CF4ECF0EF852F64 CRC64;
     MAPERRSRLS ETAGLFVSLL ALTSIVPVQA VATVPQTDYA KRAERVLRSA PLIDGHNDLP
     YAIRKSTRDQ IYDGKLPFET SLKGHTDLPR MRKGRMGGQF WSVFIACPSD PNAPIDLPTF
     ATRDTLEQID VARRLVDKYS KDLMFCDNPG CAKRAFRQGK IGSFLGIEGG HQVGSSIAAL
     RQAFYAGARY MTITHNCDNA WATAASTVRA GKPDLGMTDF GPALIKEMNR LGMLVDLSHV
     SHQSMRDILK VTKAPVIFSH SSAYEVSKHL RNVPDDVLKT VAKNNGVVMV TFVRTFVNVD
     DPDSVDVNTI VKHIFHIAKV AGWDHVGLGG DYDGTTELPK GLEDVSKYPY LIEKVLEAGA
     TEEQARKLVG ENVLRVWTEV EQIAKKIQRS GALPVEEVWK GRNGTALSER STFIEGPAPL
     AYGCD
//