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Q5HBM5 (SURE_EHRRW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5'-nucleotidase surE

EC=3.1.3.5
Alternative name(s):
Nucleoside 5'-monophosphate phosphohydrolase
Gene names
Name:surE
Ordered Locus Names:Erum3050, ERWE_CDS_03100
OrganismEhrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]
Taxonomic identifier254945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates By similarity. HAMAP MF_00060

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060

Cofactor

Binds 1 divalent metal cation per subunit By similarity.

Subcellular location

Cytoplasm Potential HAMAP MF_00060.

Sequence similarities

Belongs to the surE nucleotidase family.

Sequence caution

The sequence CAI26804.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function5'-nucleotidase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2522525'-nucleotidase surE HAMAP MF_00060
PRO_0000235615

Sites

Metal binding81Divalent metal cation By similarity
Metal binding91Divalent metal cation By similarity
Metal binding421Divalent metal cation By similarity
Metal binding941Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HBM5 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 9ACBA0F99EE3B957

FASTA25227,644
        10         20         30         40         50         60 
MRVLLSNDDG FHANGIKALK EIVIKSGIAS EIWVVAPLNN CSGSGRSVGL NVKVQVSKVS 

        70         80         90        100        110        120 
DTEFIVDSTP STSVFLALRK IMNYKPDLIL SGINHGVNIG NDVWYSGTVA AAAEGAAINI 

       130        140        150        160        170        180 
PSIAISQEYD NKSGEINWVN PQRFLKQIIE MLMNVSFWNK STVMNVNFPL MPAKGIKFTD 

       190        200        210        220        230        240 
QGKYVPCNEI EKNESSDDSN VSYTITRITP NKKNRAQCDG SIKAIDEGYI TITPLKFDMT 

       250 
DFDVLTSLNS LK 

« Hide

References

[1]"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number."
Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. expand/collapse author list , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A.
Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed: 15637156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.
[2]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed: 16547041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR767821 Genomic DNA. Translation: CAH58022.1.
CR925678 Genomic DNA. Translation: CAI26804.1. Different initiation.
RefSeqYP_180169.1. NC_005295.2.
YP_197186.1. NC_006832.1.

3D structure databases

ProteinModelPortalQ5HBM5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HBM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3232734.
3260818.
GenomeReviewsGene locus Erum3050 in contig CR767821_GR.
Gene locus ERWE_CDS_03100 in contig CR925678_GR.
KEGGeru:Erum3050.
erw:ERWE_CDS_03100.
PATRIC20580412. VBIEhrRum92411_0328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0496.
HOGENOMHBG600532.
PhylomeDBQ5HBM5.
ProtClustDBCLSK749108.

Enzyme and pathway databases

BioCycERUM254945-1:ERUM3050-MONOMER.
ERUM254945:ERWE_CDS_03100-MONOMER.

Family and domain databases

HAMAPMF_00060. SurE.
[Tree]
InterProIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
Gene3DG3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit.
KOK03787.
PfamPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMSSF64167. SurE-like_Pase/nucleotidase. 1 hit.
TIGRFAMsTIGR00087. SurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSURE_EHRRW
AccessionPrimary (citable) accession number: Q5HBM5
Secondary accession number(s): Q5FEB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 40 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