ID A0A397HY83_9EURO Unreviewed; 473 AA.
AC A0A397HY83;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Agmatinase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV56_108728 {ECO:0000313|EMBL:RHZ66506.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ66506.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ66506.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ66506.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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:RHZ66506.1}.
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DR EMBL; NKHU02000011; RHZ66506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HY83; -.
DR STRING; 41047.A0A397HY83; -.
DR VEuPathDB; FungiDB:CDV56_108728; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000215305; 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 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:UP000215305};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..473
FT /note="Agmatinase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017309203"
SQ SEQUENCE 473 AA; 50661 MW; 9D49AFBDFF168078 CRC64;
MITSTLSLLA LSAIASAHSD HRQKAIAGPH QSLWYNTIPG DGGTQADSVF SGISTFGRLP
YFPCLSSEAE KYDIAFIGEF GSVTLATFEE CSQPQALPSI LAPHTDLVQD SARVASDKVP
AVLISSSRKL GFSGGYNVPL EANPFVSELK VLDCGDIPVT SYDNAWAIQQ IEEGHNSLLM
RKPFTDADAE GLSRAGKTLP RIITLGGDHT ITLPLLRSIN KAYGPVTVIH FDSHLDTWKP
KVFGGSPSQV AAINHGTYFY HAAMEGLLKN DTNIHAGIRT TLSGPSDYEN DGYCGFEIVE
AREIDTIGTE GIIKKIRDRV GTENPVYLSI DIDTLDPAFA PATGTPETGG WSTRELRTII
RGLDGLNFIG ADIVEVAPAY DTNAELSTMA AADVLYEVLT IMVKKGPLSI SKGHELLGEP
SRRGVLSRGD DFELFSPKDG DDGSSERYEI IGRIVGMGDG SASVFYTALT GLG
//
