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A6Q367 (RTPR_NITSB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable adenosylcobalamin-dependent ribonucleoside-triphosphate reductase

Short name=RTPR
EC=1.17.4.2
Gene names
Name:rtpR
Ordered Locus Names:NIS_0814
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O = ribonucleoside triphosphate + thioredoxin.

Cofactor

Adenosylcobalamin By similarity.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the class II ribonucleoside-triphosphate reductase family.

Ontologies

Keywords
   Biological processDNA replication
   DomainRedox-active center
   LigandCobalamin
Cobalt
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-triphosphate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650Probable adenosylcobalamin-dependent ribonucleoside-triphosphate reductase
PRO_0000326543

Sites

Active site3551 By similarity
Active site3571 By similarity

Amino acid modifications

Disulfide bond123 ↔ 366Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A6Q367 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 55ED17318FE61465

FASTA65074,398
        10         20         30         40         50         60 
MYVEHFFKLP SQTKELLQNT PYRFGFGLLS EVTFYRSYSR LKEDGTNEHW PDTVIRVTEG 

        70         80         90        100        110        120 
IFSIRKNHAL NYHLPWDEEQ AQIFAKEFAL SMLQLRWLPP GRGLWMMGTR YMYERGSAGL 

       130        140        150        160        170        180 
YNCAAVDTSN LAHAAEWAMD MLMVGAGVGF NTAWSGKATK PDKKHPKIYV IDDSKEGWVK 

       190        200        210        220        230        240 
SVRLLIQSYT DNGPFYRFDY SKIRPAGSPL KTFGGIAPGP EPLKRLHKKI EQILDDYLDK 

       250        260        270        280        290        300 
KIDKTRCVVD LFNNIGLCVV SGNIRRSAEI AIGRPGDKTF LHLKDYEKFP ERKEYGWISN 

       310        320        330        340        350        360 
NSVVIENLDD FHYIDAITSL IASNGEPGVL HLENMQKYGR FGEIVPDRAW LSNPCGEIAL 

       370        380        390        400        410        420 
ESYELCNLSE IFISKCSNEE DFQKLIEYAT FYASTVNLLP THRPETNEII ARNRRIGVSV 

       430        440        450        460        470        480 
SGVADAIEKF GLETIIKWLR KGYEKVRTVN ERLAKEAGIP VSLKVTCVKP SGTISILAGT 

       490        500        510        520        530        540 
SPGMHYPLAT YALRRIRIGK TSKLAKLLID SGLSFEEDIY DKNSYVFAFP IHYDNPRSIK 

       550        560        570        580        590        600 
EVDIYEQMLV LTMLQREWAD NMVSNTIQFD PTRYDAKDLS QIVKHFLPMI KSLTLLPEKE 

       610        620        630        640        650 
TIYPQMPFES IKKEEFEKRV TQLPKVEWNT LSGHHADSER FCSTQSCQID 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB155-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009178 Genomic DNA. Translation: BAF69926.1.
RefSeqYP_001356283.1. NC_009662.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387092.NIS_0814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF69926; BAF69926; NIS_0814.
GeneID5360169.
KEGGnis:NIS_0814.
PATRIC22683696. VBINitSp82229_0854.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000154224.
KOK00525.
OMAWISGTDY.
OrthoDBEOG68DCVH.

Enzyme and pathway databases

BioCycNSP387092:GHA5-851-MONOMER.

Family and domain databases

InterProIPR000788. RNR_lg_C.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRTPR_NITSB
AccessionPrimary (citable) accession number: A6Q367
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: August 21, 2007
Last modified: November 13, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families