ID G0SB67_CHATD Unreviewed; 609 AA.
AC G0SB67;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123};
DE EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168};
GN ORFNames=CTHT_0049080 {ECO:0000313|EMBL:EGS19447.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS19447.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911; EC=3.5.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000227};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; GL988044; EGS19447.1; -; Genomic_DNA.
DR RefSeq; XP_006695269.1; XM_006695206.1.
DR AlphaFoldDB; G0SB67; -.
DR STRING; 759272.G0SB67; -.
DR GeneID; 18258946; -.
DR KEGG; cthr:CTHT_0049080; -.
DR eggNOG; KOG2965; Eukaryota.
DR HOGENOM; CLU_514928_0_0_1; -.
DR OMA; TICNCWE; -.
DR OrthoDB; 161483at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01229; rocF_arginase; 1.
DR PANTHER; PTHR43782; ARGINASE; 1.
DR PANTHER; PTHR43782:SF3; ARGINASE; 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 Arginine metabolism {ECO:0000256|ARBA:ARBA00022503};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 66432 MW; 410D00B2935A377A CRC64;
MSPSVLDDRA PAGAAPATTK TANGNGTSAP APATYTVDSN TPLNTSMTPS KFLSHPHDLG
IVAVGFAGGQ GKAGVDAAPS ALIEAGLLAS LHDDLGYNLH GHDAVHNYSD LIPASPELDP
PYRGMKNPRA VSAVTRRIAE QVYSHAREGR MVLTLGGDHS IAIGTIAGSA QAVKERLGKE
IAVIWVDAHA DINTPESSPS GNIHGMPLAF LTGLAKEDKE EFFGWIKEEQ RLNIKKLVYI
GLRDVDPVEK RILRENGVKA FSMFDVDRYG IGRVMEMALA HIGADTPIHL SFDVDALDPM
WAPSTGTPVR GGLTLREGDY ICESVHLTGQ LVAVDLVEVN PKLAPETDLG AHETIRTGCS
LLPPAVPPDG DPKHNVNVQD SKQAWEQSHD CGRTFSNEHH DPLTDPAVAD AAVPAGIMAS
TVTSGSSSLV YERRVVERVH RYHWPAIQLN FWMLIMLAAS CLIIGVFATF VETLHVLEQP
IPWYYPYYIT VACLTIAFIF LLLWLIFQRR LLPSIVMVGA FIIFVMWLVG LVVISIQLWG
PRNSISSRCN IYVFGRDPKP KGESDVTRSW LQQKSVCQSW QAVFAFGLIG QIFLFWIMVM
AYSVFVDDA
//