ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9RVC3

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PYRC_DEIRA
Primary accession number Q9RVC3
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 65)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: DR_1106
From
Deinococcus radiodurans [TaxID: 1299] [HAMAP proteome]
Taxonomy Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae; Deinococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1;
DOI=10.1126/science.286.5444.1571; PubMed=10567266 [NCBI, ExPASy, EBI, Israel, Japan]
White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1.";
Science 286:1571-1577(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE000513; AAF10679.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E75437; E75437.
RefSeq NP_294830.1; -.
3D structure databases
ModBase Q9RVC3.
Enzyme and pathway databases
BioCyc DRAD243230:DR_1106-MON; -.
Ontologies
GO
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from HAMAP).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00220; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
ProDom PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00857; pyrC_multi; 1.
PROSITE PS00482; DIHYDROOROTASE_1; FALSE_NEG.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q9RVC3.
ProtoNet Q9RVC3.
Genome annotation databases
GeneID 1797749; -.
GenomeReviews AE000513_GR; DR_1106.
KEGG dra:DR_1106; -.
NMPDR fig|243230.1.peg.1289; -.
TIGR DR_1106; -.
Phylogenomic databases
HOGENOM Q9RVC3; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   416  416     Dihydroorotase. PRO_0000147233
COMPBIAS   200   205  6     Poly-Ala. 
METAL   53    53        Zinc 1 (By similarity). 
METAL   55    55        Zinc 1 (By similarity). 
METAL   135   135        Zinc 1; via carbamate group (By similarity). 
METAL   135   135        Zinc 2; via carbamate group (By similarity). 
METAL   172   172        Zinc 2 (By similarity). 
METAL   225   225        Zinc 2 (By similarity). 
METAL   298   298        Zinc 1 (By similarity). 
MOD_RES   135   135        N6-carboxylysine (By similarity). 
Sequence information
Length: 416 AA [This is the length of the unprocessed precursor] Molecular weight: 44917 Da [This is the MW of the unprocessed precursor] CRC64: 087BCD29EA156BE7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTITITNIKR VGSEQTESLT IENGLIKGWN LPAEGEIFDG QGGTLAPALI ELHAHLREPG 

        70         80         90        100        110        120 
QTEKEDLASG LAAASAGGYG TVVCMPNTRP VIDDPALVRS LIEKARGLGF ARLRPAAAVT 

       130        140        150        160        170        180 
KGEKGEQLTE MSYLKEAGAV MFTDDGLTNE NARVLRLGME YAKSLGMVIS VHAEDDALRA 

       190        200        210        220        230        240 
GGVMNEGPVS ESLGLPGNPA AAAAARVARD MEIVALTGAR LHVQHLSTAR ELDIVRDAKR 

       250        260        270        280        290        300 
RGLPVTCEVC PHHLDLTDES LRTFDAMYKV APPLRTRADA DYLLEGLLDG SVDCIATDHA 

       310        320        330        340        350        360 
PHTRAEKERD LLDAPSGIAY IEIAFPIMWT RFGERLGLEK LIDLMTAGPA RVMGWPEPSL 

       370        380        390        400        410 
EAGAPADMVV LDLETEREVN PAEFKSKAKF TPWQGQKLRG FPLLTVVDGK VAYRRE
Q9RVC3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!