ID A0A0D2AIZ5_9PEZI Unreviewed; 412 AA.
AC A0A0D2AIZ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:KIV98903.1};
GN ORFNames=PV09_09349 {ECO:0000313|EMBL:KIV98903.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV98903.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV98903.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV98903.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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; KN847591; KIV98903.1; -; Genomic_DNA.
DR RefSeq; XP_016208773.1; XM_016363394.1.
DR AlphaFoldDB; A0A0D2AIZ5; -.
DR STRING; 253628.A0A0D2AIZ5; -.
DR GeneID; 27317322; -.
DR VEuPathDB; FungiDB:PV09_09349; -.
DR HOGENOM; CLU_039478_1_1_1; -.
DR InParanoid; A0A0D2AIZ5; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000053259; 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:SF26; AGMATINASE, MITOCHONDRIAL; 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:UP000053259};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002248844"
FT REGION 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 44653 MW; 61898A762861DF6B CRC64;
MVFNIGRWLL LSAVCSVYAS DDGTHHHHRE FSPQRLNDLS AKWGIDWGFS GISTFAHLPH
KRCLTDPGTE YDIAILGAPF DTSVSYRPGA RFGPRAIRAA SARQTSFRGY NPRAKINPYT
SWATIIDCGD IPVTPFDNAL ALRQLTEAFE ELGDRPPTAA AAASTKDYRR FPKLLTLGGD
HSIALAALRA LSSVYKQPIS VVHFDAHLDT WHPAKYPSAW FDEAVDGPEI QSYFNHGSMF
WIAGNEKLIA NGSSVHAGLR TRLAGDDEGD YADDDTQGWS RITTDDIDEI GVQGVIDRIM
THVGTERPVY LSVDIDVIDP GLAPGTGTPE PGGWTTRELI KILRGIEGLN VVGADIVEVS
PAYDGAGETT ALAAAQVGYE IISSMVKRGL SDKPVASVSR ESDSGAEAKD EL
//
