ID A0A3E2H562_SCYLI Unreviewed; 393 AA.
AC A0A3E2H562;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g7820 {ECO:0000313|EMBL:RFU28530.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU28530.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU28530.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU28530.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:RFU28530.1}.
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DR EMBL; NCSJ02000160; RFU28530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2H562; -.
DR STRING; 5539.A0A3E2H562; -.
DR OMA; CIDAGFV; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
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 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:SF30; AGMATINASE 1-RELATED; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 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:UP000258309};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..393
FT /note="Agmatinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017635900"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU28530.1"
FT NON_TER 393
FT /evidence="ECO:0000313|EMBL:RFU28530.1"
SQ SEQUENCE 393 AA; 42327 MW; 328D16A3A4CF9ACA CRC64;
MLSTLVTFGL LASGAIAHGD HENQVPIAGP HKALWYNALP GDGGTQADSV FSGISTFGRL
PYFPCLSSDE VAFDIAFIDQ VPVLGLQESD KVQDVSIYSS HRIGFSGGYN VPLDTNPFNS
WATVLDCGDI PVTSYDNTYA LHQIEEGHNA LLTRAPATDA KKKGPAKNDK TLPRIITLGG
DHTITLPLLR SINRAYGPVS VIHFDSHLDT WKPKVFGGSP SKVASINHGT YFYHASQEGL
LANDTNIHAG IRTTLSGPSD YENDGYCGFE IVEAREIDTI GMDGIIKKIK DRVGTTKPVY
LSLDIDTLDP AFAPATGTPE TGGWSTRELR TILRGLEGIN LIAADIVEVA PAYDTNAEHT
TMAAADALYE IMSLMVKKGP LSNMVSSEEK DEM
//
