Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2NVM2

- SURE_SODGM

UniProt

Q2NVM2 - SURE_SODGM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Sodalis glossinidius (strain morsitans)
Status
Reviewed - 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

Binds 1 divalent metal cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Divalent metal cationUniRule annotation
Metal bindingi9 – 91Divalent metal cationUniRule annotation
Metal bindingi39 – 391Divalent metal cationUniRule annotation
Metal bindingi92 – 921Divalent 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

BioCyciSGLO343509:GJJC-553-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:SG0528
OrganismiSodalis glossinidius (strain morsitans)
Taxonomic identifieri343509 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis
ProteomesiUP000001932: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2532535'/3'-nucleotidase SurEPRO_0000235653Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi343509.SG0528.

Structurei

3D structure databases

ProteinModelPortaliQ2NVM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0496.
KOiK03787.
OMAiVCDLIPK.
OrthoDBiEOG68WR45.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2NVM2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHILLSNDDG IHAPGIQQLA EALRTLAFVQ IVAPDRDRSG VSNSLTLDAP
60 70 80 90 100
LRMQTHPNGD IAILSGTPTD CVYLGVNALM RPGPDIVVSG INAGPNLGDD
110 120 130 140 150
VIYSGTVAAA MEGRHLGYPA LAVSLNGTRH FATAAAVTCR LLRALTSTPL
160 170 180 190 200
RTGKILNVNV PDLPLSSLKG YKVTRCGSRH PASEVIRQTD PRGREMLWIG
210 220 230 240 250
PPAGSFDAGA DTDFDAVNRG YVSLTPLQVD LTASAALPVL SDWLGDTEGL

GSW
Length:253
Mass (Da):26,625
Last modified:February 7, 2006 - v1
Checksum:i78FCFAAAEC54A51A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008232 Genomic DNA. Translation: BAE73803.1.
RefSeqiYP_454208.1. NC_007712.1.

Genome annotation databases

EnsemblBacteriaiBAE73803; BAE73803; SG0528.
GeneIDi3868229.
KEGGisgl:SG0528.
PATRICi23647969. VBISodGlo61428_1308.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008232 Genomic DNA. Translation: BAE73803.1 .
RefSeqi YP_454208.1. NC_007712.1.

3D structure databases

ProteinModelPortali Q2NVM2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 343509.SG0528.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE73803 ; BAE73803 ; SG0528 .
GeneIDi 3868229.
KEGGi sgl:SG0528.
PATRICi 23647969. VBISodGlo61428_1308.

Phylogenomic databases

eggNOGi COG0496.
KOi K03787.
OMAi VCDLIPK.
OrthoDBi EOG68WR45.

Enzyme and pathway databases

BioCyci SGLO343509:GJJC-553-MONOMER.

Family and domain databases

Gene3Di 3.40.1210.10. 1 hit.
HAMAPi MF_00060. SurE.
InterProi IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view ]
Pfami PF01975. SurE. 1 hit.
[Graphical view ]
SUPFAMi SSF64167. SSF64167. 1 hit.
TIGRFAMsi TIGR00087. surE. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
    Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
    Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: morsitans.

Entry informationi

Entry nameiSURE_SODGM
AccessioniPrimary (citable) accession number: Q2NVM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 7, 2006
Last modified: October 29, 2014
This is version 58 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3