ID A0A0A2JI98_PENEN Unreviewed; 540 AA.
AC A0A0A2JI98;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:KGO54526.1};
GN ORFNames=PEX2_070590 {ECO:0000313|EMBL:KGO54526.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54526.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54526.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54526.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO54526.1}.
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DR EMBL; JQFZ01000221; KGO54526.1; -; Genomic_DNA.
DR RefSeq; XP_016596897.1; XM_016744330.1.
DR AlphaFoldDB; A0A0A2JI98; -.
DR STRING; 27334.A0A0A2JI98; -.
DR GeneID; 27679750; -.
DR HOGENOM; CLU_009942_5_0_1; -.
DR OrthoDB; 147994at2759; -.
DR PhylomeDB; A0A0A2JI98; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642:SF19; AMIDOHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G01480); 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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 Hydrolase {ECO:0000313|EMBL:KGO54526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 51..533
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 540 AA; 58947 MW; F4776BC1A9D37759 CRC64;
MVTTIFTNGR ILCPGLWGTF VSTLVVEDNH IAHVGWDNEQ AVVKVQATAS TVDLKNRIVL
PGFIDGHVHI LNFGMSLQKL DLLPCKNLAD IRNSITSYAK SHPSDPRILC RGWVQSVTDG
NALATVLDDL DPRPIYIEAL DLHSTWCNTA ALKELEADSK PDPPGGKIHR CQNDAPSGLL
EEAAQFDIVW PFLDRVTSME KKVSAIDAAI GAHQRAGYTG LVDMAMGESE WTALNIYRNQ
RGGLPIHVAA HWLVPYSKCD ADICSHIDRA IELQQTFNRK SSPDFCINGI KLLCDGTVDG
CTAGLHQPYG GSAEIIDPIW PADALAAAIR RATDAGLQCA IHAIGDRTVQ QAIDCLSQIP
NLRSRRHRIE HLEITTPEDA KRLGQLGIVA SVQPVHLDPA TFDGWPEMLG IQRCKRAFAY
QEFVDAGAHL AFGTDAPTAE HHALPNIYVA TTRRSSINPS LQDTINPEFA VSLATAVSAA
TAGAAYASFS DSWTGSLRPG FDANFVVLDM IWDTESLLEA RVCQTWYKGK KVFDEEAGDR
//
