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Database: UniProt
Entry: A0A139HUC5_9PEZI
LinkDB: A0A139HUC5_9PEZI
Original site: A0A139HUC5_9PEZI 
ID   A0A139HUC5_9PEZI        Unreviewed;       381 AA.
AC   A0A139HUC5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Adenosine deaminase domain-containing protein {ECO:0000259|Pfam:PF00962};
GN   ORFNames=AC578_1405 {ECO:0000313|EMBL:KXT06070.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT06070.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT06070.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT06070.1,
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   -!- 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       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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:KXT06070.1}.
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DR   EMBL; LFZN01000008; KXT06070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HUC5; -.
DR   STRING; 321146.A0A139HUC5; -.
DR   OrthoDB; 2572796at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01430; aden_deam; 1.
DR   PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR   PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT   DOMAIN          32..376
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   381 AA;  43435 MW;  600740723AA7928D CRC64;
     MANVANALPI TNRLKLRESL KTTSDSFLLN LPKIELHVHI EGCLTPELKW KFSQRNKTPI
     LNARTGEKFK TLEQLQNSHN NNNNNEEKMM TNAEETLTFF EMYTSGFAIL ETQRDYYDLA
     MEYFTKASAQ KIVYAEIFFD AQGHKGKGKG KEMMEGFREA SIEAAKKEGL NVKSSWILCF
     LRDESPEAAM ECYETFALGE YRDMVLGVGL DSNEEGRAPN LFRGVFERAR RDGFRVTCHC
     DVGKAYPVEH VRQVVEDIEA DRIDHGLNVV EDERLMGVMR EKGLGMTICP WSYIRHQPFE
     QVFERIRVLI DNGLKISIGS DDPAFMEDAG ILENLRVLKK YCKLTNEDMV QLSKGAVEIS
     WAPPDLKKEL LGQLDKVAIA P
//
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