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Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.UniRule annotation

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.UniRule annotation
A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.UniRule annotation
(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.UniRule annotation

Cofactori

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Divalent metal cationUniRule annotation
Metal bindingi10 – 101Divalent metal cationUniRule annotation
Metal bindingi40 – 401Divalent metal cationUniRule annotation
Metal bindingi93 – 931Divalent metal cationUniRule annotation

GO - Molecular functioni

  1. 3'-nucleotidase activity Source: UniProtKB-HAMAP
  2. 5'-nucleotidase activity Source: UniProtKB-HAMAP
  3. exopolyphosphatase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-HAMAP
  5. nucleotide binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYPES349746:GHPB-961-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
5'/3'-nucleotidase SurEUniRule annotation (EC:3.1.3.5UniRule annotation, EC:3.1.3.6UniRule annotation)
Alternative name(s):
ExopolyphosphataseUniRule annotation (EC:3.6.1.11UniRule annotation)
Nucleoside monophosphate phosphohydrolaseUniRule annotation
Gene namesi
Name:surEUniRule annotation
Ordered Locus Names:YpAngola_A0961
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2542545'/3'-nucleotidase SurEPRO_1000092052Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi349746.YpAngola_A0961.

Structurei

3D structure databases

ProteinModelPortaliA9R116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0496.
HOGENOMiHOG000122500.
KOiK03787.
OMAiLGSNMGE.
OrthoDBiEOG68WR45.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

A9R116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRILLSNDD GISAPGIQTL ASALRGFAQV QIVAPDRNRS GASNALTLDS
60 70 80 90 100
ALRITTLSNG DIAVQQGTPT DCVYLGVNAL MRPRPDIVVS GINAGPNLGD
110 120 130 140 150
DVIYSGTVAA AMEGRHLGYP ALAVSLNGHQ HYDTAAAVTC RLLRALQRKP
160 170 180 190 200
LRTGKILNIN VPDLPLAEIK GIRVTRCGSR HPAEQVFCQQ DPRGQDLYWI
210 220 230 240 250
GPPGEKYDAG PDTDFAAVEQ GYVSITPLQV DLTAYMAQEV VESWLANTEV

DGEW
Length:254
Mass (Da):27,231
Last modified:February 5, 2008 - v1
Checksum:i99C139F3E5D4E4F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX85503.1.
RefSeqiYP_001605525.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX85503; ABX85503; YpAngola_A0961.
GeneIDi5799424.
KEGGiypg:YpAngola_A0961.
PATRICi18570956. VBIYerPes97331_1273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX85503.1.
RefSeqiYP_001605525.1. NC_010159.1.

3D structure databases

ProteinModelPortaliA9R116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349746.YpAngola_A0961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX85503; ABX85503; YpAngola_A0961.
GeneIDi5799424.
KEGGiypg:YpAngola_A0961.
PATRICi18570956. VBIYerPes97331_1273.

Phylogenomic databases

eggNOGiCOG0496.
HOGENOMiHOG000122500.
KOiK03787.
OMAiLGSNMGE.
OrthoDBiEOG68WR45.

Enzyme and pathway databases

BioCyciYPES349746:GHPB-961-MONOMER.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiSURE_YERPG
AccessioniPrimary (citable) accession number: A9R116
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 7, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.