ID A0A139HIJ6_9PEZI Unreviewed; 613 AA.
AC A0A139HIJ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=AC578_5053 {ECO:0000313|EMBL:KXT02223.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT02223.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT02223.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT02223.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT02223.1}.
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DR EMBL; LFZN01000044; KXT02223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HIJ6; -.
DR STRING; 321146.A0A139HIJ6; -.
DR OrthoDB; 1445523at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 89..582
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 613 AA; 67352 MW; CBEE805BB41A8845 CRC64;
MARLGTYTIS AYLVSGPLVV VISMSAGELW EAATGDIVFQ NATILDGSGD VPRHIGCVLV
RDGKIHRVWN NHSPLAPGAI QQCQERGIQV IDCEDGKWHL CPGFIDMHAH SDLSLLHTPE
HLAKVTQGVT TEVIGQDGIS YSPVDDKSIA RIREQIAGWN GNPKDPPDFF DRWRSVKEYL
DVLDRERIAT NAAYLVPQGN LRILVKGWDS SRATPEELEQ MKKILVQALE DGAVGMSSGL
TYVPGMFAPD EEIAELCKVV KQYGGYYCPH TRSYGKGALK AYREMIELAK QIGVRLHLTH
ATMNYPENAG RANELITMID DAITAGVDIS LDTYPYLPGS TTLASTLPSW AASAENPASL
LDDPKTRAEI KRLALEEGTD GCHGCTLDWS ILEIGGTQNP ELASKYVGKT IAQIAKEQKR
DAFDTYIDIL KEDNFNSTIL SHCGHEANVR RIMRHPRHTG GSDGILTSTK PHPRGWGTFP
RYLGHYARDL PNGKSRDIYH STSSTVYDDV DAEKIFAGGL EEAVAHLTSR AAAVVRMKDR
GLVREGYRAD LVLFDKDEIR DAATYARPRQ AAKGIRAVMI NGFFAVEEAK ATGARVGRTV
RMVAGDGGEW VVR
//