ID W9YJG4_9EURO Unreviewed; 418 AA.
AC W9YJG4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:EXJ93047.1};
GN ORFNames=A1O3_01603 {ECO:0000313|EMBL:EXJ93047.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ93047.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ93047.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ93047.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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:EXJ93047.1}.
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DR EMBL; AMGY01000001; EXJ93047.1; -; Genomic_DNA.
DR RefSeq; XP_007729937.1; XM_007731747.1.
DR AlphaFoldDB; W9YJG4; -.
DR STRING; 1182542.W9YJG4; -.
DR GeneID; 19165737; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_1_1; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000019478; 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 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:UP000019478};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004934587"
SQ SEQUENCE 418 AA; 45108 MW; 08F9ADEA7A8A3644 CRC64;
MLSFSTSLPL SLLLLLPFSW ASFYDNPEFD LPPESGTPLD ELKAKWDTDW GFSGISTFAH
LRHVKCLTTP YEPFDIGIIG APFDTAVSYR PGARFGPRAI RAASARQTTF RGFNHRAGIN
PYASWPAVLD CGDIPITPFD NALALHQMTS AYLELLSRRP LSYTNPPSHK HPKLITLGGD
HSIALPALRA LEKTYGQPIA VLHFDAHLDT WHPGSYPSAW ANTPTQADFT HGTMFWVASE
EGLIANGSSV HAGLRTRLGG ADWGDYENDE NQGFLRIEAD DIDAVGVSGI IDAIMDRMGT
ERPVYLSVDI DVIDPGLAPG TGTPEPGGWT TRELIGILRG IEGLNLVGAD LVEVAPAYDG
NGEGTALAGA QVVYEILTSM VKRGLKERGE EVVLQKPGKH IAAAAAAKAK AKTARDEL
//
