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Database: UniProt
Entry: A0A397GS58_9EURO
LinkDB: A0A397GS58_9EURO
Original site: A0A397GS58_9EURO 
ID   A0A397GS58_9EURO        Unreviewed;       461 AA.
AC   A0A397GS58;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Guanine deaminase {ECO:0000256|ARBA:ARBA00014514};
GN   ORFNames=CDV56_106547 {ECO:0000313|EMBL:RHZ53119.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ53119.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ53119.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ53119.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHZ53119.1}.
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DR   EMBL; NKHU02000126; RHZ53119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397GS58; -.
DR   STRING; 41047.A0A397GS58; -.
DR   VEuPathDB; FungiDB:CDV56_106547; -.
DR   OrthoDB; 65153at2759; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000215305; Unassembled WGS sequence.
DR   GO; GO:0008892; F:guanine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11271; GUANINE DEAMINASE; 1.
DR   PANTHER; PTHR11271:SF6; GUANINE DEAMINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT   DOMAIN          79..459
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   461 AA;  50742 MW;  71777028C2D41020 CRC64;
     MNETPTATGL PLAFHGTIIH SLSPTDLQIL PNTFLLVDIT GKIQALVPNT DPSTINTLIA
     DNGYAPDVFP VKHLPKHSFL IPGFIDTHNH APQWAQRGVG RGISLLDWLE TVTFAHEAKF
     EDVEYAKRMY SAAVDGLLRQ GITTATYYAS KHLAATKTLA EVCREKGQRA LVGRCNMNRH
     APGWYRDLNA GVSVKETGEF IQWMREFNGG EERPLVNAVI TPRFAISCDE EVLSGLGALA
     AANPDLPIQT HFNEAEQEME FTRQLFPDFA HEAELYARFG LLNERSILAH CIFLREEEME
     TLARLRCGVA HCPIANTTMQ AFMVAPVREY LRRGIKVGLG TDSGGGHSIS MLEVMKQAFV
     VSTARATETR GADPALSVAE CFFLATLGGA QVCGLDERVG NFAVGKEFDA LEVRTGEEVV
     MDVMTPVEEG DSIEVIFEKF LMTGDDRNIA KVYVRGRAVK V
//
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