ID A0A2H0ZFT2_CANAR Unreviewed; 421 AA.
AC A0A2H0ZFT2; A0A5Q7YMN4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:PIS49508.1};
GN ORFNames=B9J08_004531 {ECO:0000313|EMBL:PIS49508.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS49508.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS49508.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS49508.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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:PIS49508.1}.
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DR EMBL; PEKT02000009; PIS49508.1; -; Genomic_DNA.
DR STRING; 498019.A0A2H0ZFT2; -.
DR EnsemblFungi; B9J08_004531-t37_1; B9J08_004531-t37_1-p1; B9J08_004531.
DR VEuPathDB; FungiDB:B9J08_004531; -.
DR VEuPathDB; FungiDB:CJI96_0004620; -.
DR VEuPathDB; FungiDB:CJI97_004921; -.
DR VEuPathDB; FungiDB:CJJ07_005073; -.
DR VEuPathDB; FungiDB:CJJ09_004533; -.
DR VEuPathDB; FungiDB:CJJ09_004534; -.
DR VEuPathDB; FungiDB:QG37_03822; -.
DR OMA; YELTTIM; -.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd11592; Agmatinase_PAH; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR NCBIfam; TIGR01230; agmatinase; 1.
DR PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230249}.
SQ SEQUENCE 421 AA; 46406 MW; 7E7ABE65609D4BED CRC64;
MKLSIATLAA IAASQVGASA PEAQLSEIWG EAWPFQGINT FAHLPSHNCL ANRDLQYDIA
LVGVPFDTAV SYRPGARFGP RAIRAASQRQ TSLRGFNPRA LYNPYKEWAS VVDCGDIPVS
PMDNNLAFEQ MTTGFEELLF EHSSKNDVAA KPRYIALGGD HSVLLPHIRA LHKLYGPINI
IHFDAHLDTW KPDKYPSYWH SAQSEVTHGS MLWKAYEEGL TTKNNVHAGL RTKLSGAEDW
DDDDEQGWLR ISADDVWLQG ADHVIKQILK RIPKNSPTYI SVDIDVLDPA FASGTGTQEP
GGWQPRELIH ILRGIESLNI VGADVVEVSP AYDHAEVTAT NGAQVAYEII TSMAKSGPLK
LPTAKGLHAE YSRSKSAFEA VDDVEFGYDA GHKDTQEALS ERAMALEKRL AEIRELQKQN
A
//
