ID F9G270_FUSOF Unreviewed; 516 AA.
AC F9G270;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_12752 {ECO:0000313|EMBL:EGU76731.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU76731.1};
RN [1] {ECO:0000313|EMBL:EGU76731.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU76731.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU76731.1}.
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DR EMBL; AFQF01003186; EGU76731.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G270; -.
DR STRING; 660025.F9G270; -.
DR PaxDb; 5507-FOXG_09454P0; -.
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; 2.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..516
FT /note="Agmatinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383554"
SQ SEQUENCE 516 AA; 56584 MW; 1B8B1F44FED6D2A4 CRC64;
MKLLNVLALA GLATACAHDH DDKEWTKEEL DELEQKWGYE WPFAGINTFA HLNHVKCLTE
PTEPFDIAIV GAPFDTAVSY RPGARFGPRA IRSASARQTS MRGFNPRAGI NPYQNWAKIV
DCGDISITPI DNNIAREQMT QAFKQLGRRK TVSALAPKAR LVTLGGDHSL ALPALRALNE
IHGKPIQVLH FDGGLIVPFV NYLVKNLINT STTAHLDTWN PAAYPSWWGA TQFTHGSMFW
MANQEGLLSN SSSERSVHAG LRTRLSGNDF ADNEDDTSQG WVRFTADDID DLGTKGIIDG
ILKVLGTENP VYLSVDIDVL DPAFAPGTGT PEPGGWSTRE FIRILRGLEG LNLVGADVVE
VSPAYQNGGE ETALAAAQVV YEIISSMVKR GLQDGGKEGN GGNAAAGKDE LEDHKMNLLK
FNERVERNYL NDFVYKVSFI GDIFLVMQPH VVSKERVCAT GNGSREHSKA FESYGSQTYR
TLVSSLGELR SGTEMVELRC LQLNTQSFIS VRTIIG
//