ID R1GF03_BOTPV Unreviewed; 396 AA.
AC R1GF03;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative agmatinase 1 protein {ECO:0000313|EMBL:EOD50205.1};
GN ORFNames=UCRNP2_3029 {ECO:0000313|EMBL:EOD50205.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD50205.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; KB916005; EOD50205.1; -; Genomic_DNA.
DR RefSeq; XP_007582337.1; XM_007582275.1.
DR AlphaFoldDB; R1GF03; -.
DR STRING; 1287680.R1GF03; -.
DR KEGG; npa:UCRNP2_3029; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_1_1; -.
DR OMA; CIDAGFV; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000013521; 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 PIRSF; PIRSF036979; 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:UP000013521};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..396
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004349104"
SQ SEQUENCE 396 AA; 42610 MW; C8D1965D8AB3C8E4 CRC64;
MKTFAVAAGL AALAAAHGDH GHDQKPIEGP HKGLWYNSLP GDGGTQADSV FSGISTFGRI
QYSPCLSTDD VKYDIAFIGA PFDTGTSYRP GARFGPSGIR QGSRRLNLYG GYNVPLDANP
FNSWATVIDC GDIPVTSYDN GWAIKQIEEG HNSVLSRSPA TNSHMKGLSK KGKTLPRVIT
LGGDHTITLP LLRSINREYG PVSVIHFDSH LDTWRPKVFG GAPSEQASIN HGTYFYHAAQ
EGLLANDSNI HAGIRTTLSG LSDYENDGYC GFEIVEAREI DTIGIDGIIK KIRDRVGTEK
PVYLSIDIDT LDPAFAPATG TPETGGWSTR ELRTIVRGLD GINLIGADIV EVAPAYDTNA
EHTTMAAADT LYEVMTIMVK RGPLSLNTVG DNMEEL
//
