ID A0A2B7XN91_9EURO Unreviewed; 408 AA.
AC A0A2B7XN91;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:PGH13244.1};
GN ORFNames=AJ79_03803 {ECO:0000313|EMBL:PGH13244.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH13244.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH13244.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH13244.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH13244.1}.
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DR EMBL; PDNB01000048; PGH13244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XN91; -.
DR STRING; 1447875.A0A2B7XN91; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000223968; 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:UP000223968};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013038635"
SQ SEQUENCE 408 AA; 44914 MW; 9E3FD3FF41059C85 CRC64;
MLPTSWTSIL TGLLLCLRPA YAHHGHGDEH EEIPIERREE LLKKWDQEWG FAGVSTFAHL
KHVKCLIEPD EQYDIAVLGA PFDTAVSYRP GARFGPRAIR AASARQLPAN SYNTRAAINP
YLNWARILDC GDIPVTPFDN GLAERQMYEA FLELGTRPVP NPIPGISNGK PKLVTLGGDH
SITLPALRAL YKIYGKPITV LHFDAHLDTW NPVRYAAYWT SDQSRFNHGS FFHTASREGL
ISNTSSAHAG LRTRLTGLDD GDYSNPGPEQ GFYRIHADDI DDVGPKGVID QIISRVGLSP
DEPVYLSLDI DVLDPGLAPG TGTPEPGGWT TRELIRILRG IEKLNLVGAD IVEVSPSYDS
VTENTALAAA QVAFELITSM VKLNAKENVG GWYGKKEEKV EGVKRDEL
//
