GenomeNet

Database: UniProt
Entry: G0SB67_CHATD
LinkDB: G0SB67_CHATD
Original site: G0SB67_CHATD 
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}.
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; 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
//
DBGET integrated database retrieval system