ID A0A093VDH5_TALMA Unreviewed; 318 AA.
AC A0A093VDH5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Putative agmatinase 1 {ECO:0000313|EMBL:KFX50245.1};
DE Flags: Fragment;
GN ORFNames=GQ26_0070160 {ECO:0000313|EMBL:KFX50245.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX50245.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX50245.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX50245.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX50245.1}.
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DR EMBL; JPOX01000007; KFX50245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VDH5; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_1_1; -.
DR Proteomes; UP000029285; 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 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}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFX50245.1"
SQ SEQUENCE 318 AA; 34665 MW; E6730578B155D032 CRC64;
WRYSGAPFDT GTSYRPGARF GPSGIRQGSR RLNLYGGYNV PLEANPFSSN IKVLDCGDIP
VTSYDNTWAL RQIEEGHNSV MMRRPFTDAD KQGLSKAGKT LPRVITLGGD HTITLPLLRS
INRAYGPVTV IHFDSHLDTW KPKVFGGAPS ETASINHGTY FYHAAMEGLL RNDTNIHAGI
RTTLSGPSDY DNDGYVGFEI VEAREIDTIG TDGIIKRIRD RVGTVNPVYL SIDIDTLDPA
FAPATGTPET GGWTTRELRT IVRGLDGLNF VGADIVEVAP AYDTNAELTT MAAADVLYEV
LTIMVKKGPL SLSGREEL
//
