ID A0A1L0DSN9_9ASCO Unreviewed; 475 AA.
AC A0A1L0DSN9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=CIC11C00000001822 {ECO:0000313|EMBL:SGZ55374.1};
GN ORFNames=SAMEA4029010_CIC11G00000001822 {ECO:0000313|EMBL:SGZ55374.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ55374.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ55374.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ55374.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; LT635760; SGZ55374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0DSN9; -.
DR STRING; 45354.A0A1L0DSN9; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000182334; Chromosome v.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF28; HYPOTHETICAL ARGINASE FAMILY PROTEIN (EUROFUNG); 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000182334};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012792288"
SQ SEQUENCE 475 AA; 52217 MW; D320CC792097348D CRC64;
MNWPLILSLV LLIAASPTFN AYESAQEVVF VENSPQLPEE SYIDQLYGEV VLTPESEALK
LQLLSEGLDE PQKLVSYFVD ETQLVGSPWQ IALALQSITE NHDKAKRQRA HDGYLKIRLK
LRLPSDDDTE DLSEVSFLGG IITFGHFESF NCFDPNLFEK PIDVAIVGAP FDTGTSYRPG
ARFGPEAIRL GARRLGQGYT PVRGNGPDSK LGKIDPYDPT NHNFTIIDCG DVPMTPFDNR
VALNQLYRGQ RAIHNHTVSG KASLIEHTKV ITMGGDHTVT LMALRSAYEK FGKLAVLHFD
SHIDTWDPKV LGGGISDYMS LNHGTFLHYA AEKGYLAKDH CFHLGLRAPY ISAEYDIKHD
RECGFQTITA RDLDRLGKQA IIDKVKESVG NMPVYISVDI DVLDPANAPG TGTMEIGGWT
GRELLSVLDG LEGINLVGGD VVEVSPPFDS NSEITSLAAT AVIDLMLGLI IVQDF
//
