ID   A0A0A2K6W5_PENIT        Unreviewed;       586 AA.
AC   A0A0A2K6W5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Adenosine deaminase domain-containing protein {ECO:0000259|Pfam:PF00962};
GN   ORFNames=PITC_049610 {ECO:0000313|EMBL:KGO63579.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO63579.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO63579.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO63579.1,
RC   ECO:0000313|Proteomes:UP000030104};
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KGO63579.1}.
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DR   EMBL; JQGA01001632; KGO63579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2K6W5; -.
DR   STRING; 40296.A0A0A2K6W5; -.
DR   HOGENOM; CLU_022829_2_1_1; -.
DR   OMA; GHGYTIT; -.
DR   OrthoDB; 4403at2759; -.
DR   PhylomeDB; A0A0A2K6W5; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11409:SF39; ADENOSINE DEAMINASE 2; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..586
FT                   /note="Adenosine deaminase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002001454"
FT   DOMAIN          236..532
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   586 AA;  65551 MW;  B9DFC6F4057D5C63 CRC64;
     MRLLSLLGVA TLSISGVSAG LAIEGEPNVN ATLVKQHLRD REKLITLEKT HRQDHIFRQN
     LSPTAKQADE IVQAIRQDEI DNYWRVAGTP DGEEERFAGE VFPLARPYIS NTTLWKVIKR
     MPKGALLHAH LSAMLPFEKI VEIIIHTEGM VISASQPVDT DEAKQNATIT FAHNNGTLSS
     NQSRIDASDY VHGTEIPVKA AAASFEGGEA GFLEFIRSKT TISPEESIRH ELGVDEVWRK
     FQACFGPADT MVQYEPVVRK FYQKLFEDLA SDGINWVEIR SGGLSGKLVH NGDEDIDPDL
     DAWWHVLVEE IEKFKATEQG KNFLGARIIW SDARIKNRAA ITKSMKIALQ RKQNFPELFS
     GYDLVAQEDL GRPLSDLAPE LIWFREQTEA LNLTIPYFFH AGETLGDGNS TDSNLFDAVL
     FNTRRIGHGF SLYKHPNLIR QVIEQSVMIE VCPISNEVLR LNEDVLHHPL PAMIAHGIPT
     AISNDDPAIL GQDIAGLSYD FYETIQAFDN IGLAGLGALA QNSLRWANFE DQSDVNWVQD
     IVRGEDGTGT KAKHIQAWNS DWEDFCKWIV DEYGSKYGTA KIDSTI
//