ID Q9HJB2_THEAC Unreviewed; 303 AA.
AC Q9HJB2;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Agmatinase related protein {ECO:0000313|EMBL:CAC12186.1};
GN OrderedLocusNames=Ta1058 {ECO:0000313|EMBL:CAC12186.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC12186.1, ECO:0000313|Proteomes:UP000001024};
RN [1] {ECO:0000313|EMBL:CAC12186.1, ECO:0000313|Proteomes:UP000001024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC {ECO:0000313|Proteomes:UP000001024};
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL445066; CAC12186.1; -; Genomic_DNA.
DR RefSeq; WP_010901469.1; NC_002578.1.
DR AlphaFoldDB; Q9HJB2; -.
DR STRING; 273075.gene:9572278; -.
DR PaxDb; 273075-Ta1058; -.
DR EnsemblBacteria; CAC12186; CAC12186; CAC12186.
DR GeneID; 1456574; -.
DR KEGG; tac:Ta1058; -.
DR eggNOG; arCOG01700; Archaea.
DR HOGENOM; CLU_039478_0_2_2; -.
DR InParanoid; Q9HJB2; -.
DR OrthoDB; 7186at2157; -.
DR Proteomes; UP000001024; Chromosome.
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 GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd11593; Agmatinase-like_2; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01230; agmatinase; 1.
DR PANTHER; PTHR11358:SF43; AGMATINASE; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
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:UP000001024}.
SQ SEQUENCE 303 AA; 34489 MW; 66CAB41352B1FE8D CRC64;
MGDHGDAKDH ASELKDIFSL KKIADAKYSY EDSDYVIFGV PFDNTSSYRR GSKYAPDSIR
SAYVNLESFE FSYRFDLLRA RISDLGDMEE SEDVEYVVDQ VDRVTKMVFS DGKIPIMLGG
EHSITVGAVR NFPEDVHMVI VDAHSDFRDS YMGNKLNHAC VTKRALEILG PNRITSIGTR
SVSLEEYQDP DFEKVEFIPS FSVREYGIER FINDIERRPG RVYISIDMDG IDPAYAPAVG
TPEPFGLTDY EVRRLVERLS YKAIGMDINE FSPLYDNGNT SMLAGKLIQV FIASREKYRI
EHI
//