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Database: UniProt
Entry: A0A1C1CBF0_9EURO
LinkDB: A0A1C1CBF0_9EURO
Original site: A0A1C1CBF0_9EURO 
ID   A0A1C1CBF0_9EURO        Unreviewed;       572 AA.
AC   A0A1C1CBF0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=dihydropyrimidinase {ECO:0000256|ARBA:ARBA00039113};
DE            EC=3.5.2.2 {ECO:0000256|ARBA:ARBA00039113};
GN   Name=PYD2 {ECO:0000313|EMBL:OCT45798.1};
GN   ORFNames=CLCR_01481 {ECO:0000313|EMBL:OCT45798.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT45798.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouracil + H2O = 3-(carbamoylamino)propanoate + H(+);
CC         Xref=Rhea:RHEA:16121, ChEBI:CHEBI:11892, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15901; EC=3.5.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00036696};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family.
CC       {ECO:0000256|ARBA:ARBA00008829}.
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:OCT45798.1}.
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DR   EMBL; LGRB01000019; OCT45798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1CBF0; -.
DR   STRING; 86049.A0A1C1CBF0; -.
DR   VEuPathDB; FungiDB:CLCR_01481; -.
DR   VEuPathDB; FungiDB:G647_03689; -.
DR   eggNOG; KOG2584; Eukaryota.
DR   Proteomes; UP000094526; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000094526}.
FT   DOMAIN          54..518
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          381..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  62250 MW;  BB6669E2D9A68042 CRC64;
     MDLDLIIKNA TIVTATEVLP PGLSIGIHGG KIVAIALSLP CTPSTRVIDA EGAYVTPGGV
     DSHVHLHQDN APTGDKWLSG SRSALCGGNT TILAFATQKR TDESLFPVVR DYHTRAAGQS
     FVDYGFHLIV SRPGPEILGG PAMTAKMGKE ADVNDRKDEN EGELKIMVEQ EGITSVKLYM
     TYPAYRLGDR EMLDVMMRCR EVGMTVMVHA ENADMIDMIT TRLLSSSHTQ PKYHAVARPQ
     IAETEATYRA ISLSTLTATP ILIVHMSSPA ALSHARKAQS KQMLPIHAET CPHYMFLKSE
     RLGATSHPFE GEDHSHAHLD GKLGEEVDEW AGARHICAPP LRHDDKDLQS VWDAVTNGTI
     TVISSDHAPS QYHNPLGKKK PVHEYESGKT TIPPSFANTP NGLPGIETRL PLLFSAATDA
     SVTASAARTL TLPKFVALTS TNPARMYGLA GRKGSIAPGY DADLVVWYPH SPRADDASRD
     KPTITITNDM LHHSIDYTPF EGFPVTNWPR YVLLRGQVKW DRDLELAEGP GKGILGRPGD
     GLFLKRAKGE VLVGRTGGEP EGMRLGETKS WM
//
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