ID A0A2V5I2X2_9EURO Unreviewed; 531 AA.
AC A0A2V5I2X2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Guanine deaminase {ECO:0000313|EMBL:PYI31049.1};
GN ORFNames=BP00DRAFT_425846 {ECO:0000313|EMBL:PYI31049.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI31049.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI31049.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI31049.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; KZ825507; PYI31049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5I2X2; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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:SF50; GUANINE DEAMINASE-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
FT DOMAIN 93..495
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 531 AA; 57200 MW; 1D85E2AF0C1523DA CRC64;
MVSPMYTLYV GTFIQLPRTT APDDKHELAI TRGALWVSAA DGKIKGFDWS IATESDLLTL
LKRHGWVLDG AGSRSSVRVK LVRAREDHNE FFFPGFIDTH IHAPQYPNTG LFGSATLLDW
LQTYTFPMEA SFASPASLPS LPPPTAYRAY SQVIARTLSH GTTTASYYAT IHVPATNLLA
SLAHQRGQRA LIGRVCMDNP ATCPTTLIDE SPEDSIHNTE AVIAHIHSLA PATSKETLVK
PILTPRFAPS CTPAALSGLA ALAKQYKPPL HIQTHIAENV NEIALVRQQF PACTDYASVY
DTAGLLTPRT ILAHAVHFSA AERSLVASRG AKVSHCPASN SALGSGICPV RWLRRGGVVV
GLGSDVSGGY SVGLLEAVRQ ACLVSRFVRF VHPADEEKGA DGVVSVEEAL YLATRGGAAV
VDLPDLIGGF DLGMAWDAQL IRLGRFTPAG LWGSAGAEGN VDVFGTESWT EKVHKWVWSG
DDRNVRAVWV QGRLVHGADG GDVKGRWGRW TWVWGLVGVG AAWVVVRRVH G
//