ID A0A0G2FZ76_9PEZI Unreviewed; 403 AA.
AC A0A0G2FZ76;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative mitochondrial {ECO:0000313|EMBL:KKY39412.1};
GN ORFNames=UCDDA912_g00623 {ECO:0000313|EMBL:KKY39412.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39412.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY39412.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39412.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY39412.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39412.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY39412.1}.
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DR EMBL; LCUC01000020; KKY39412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FZ76; -.
DR STRING; 1214573.A0A0G2FZ76; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000034680; 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:UP000034680};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002544719"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 43931 MW; D4819138A83A0F7D CRC64;
MRSGWAPLVL TALASLAEAC GGHKHDDRVW TAEEVAELEY KWGMEWPFAG IGSFAHLKHV
KCLTDPTELF DIAIVGAPFD TAVSYRPGAR FGPRAIRHAS SRQTSFRGFN PRANINPYQN
WAKIMDCGDI PIVPVDNAVA QRQMTEAFTE LGSRRPLSPL LEKPKLITLG GDHSLALPAL
RALNKIYGKP LRVLHFDAHL DTWHPAKYPS SWLTDQAHFN HGSMFWLAGS EGLLVNDTAR
PSVHAGLRTR LSGNGWDDFD DDTAQNWLRV VADDIDDLGT AGVVKAILDA IPPDDPVYLS
VDIDVLDPAF APGTGTPEPG GWTTRELIRI LRGLEGLNVV GADVVEVAPA YQGQGEETAL
AAAQVVYEMI SSIVKKGMTE MGKEDAAPEV EGVKAEEEVK DEL
//
