[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.; Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: 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 (By similarity).
CATALYTIC ACTIVITY: A 5'-ribonucleotide + H₂O = a ribonucleoside + phosphate.
CATALYTIC ACTIVITY: A 3'-ribonucleotide + H₂O = a ribonucleoside + phosphate.
CATALYTIC ACTIVITY: (Polyphosphate)(n) + H₂O = (polyphosphate)(n-1) + phosphate.
COFACTOR: Binds 1 divalent metal cation per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the surE nucleotidase family.

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

CP000880; ABX19983.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001569125.1; -.

3D structure databases

ModBase

A9MF31.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008254;	Molecular function: 3'-nucleotidase activity (inferred from electronic annotation from EC).
GO:0008253;	Molecular function: 5'-nucleotidase activity (inferred from electronic annotation from HAMAP).
GO:0004309;	Molecular function: exopolyphosphatase activity (inferred from electronic annotation from EC).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from HAMAP).
GO:0000166;	Molecular function: nucleotide binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00060; -; 1.
PBIL [Tree]

InterPro

IPR002828; SurE-like_Pase/nucleotidase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1210.10; SurE-like_Pase/nucleotidase; 1.

ProDom

PD005378; SurE; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00087; surE; 1.

Genome annotation databases

GeneID

5762022; -.

GenomeReviews

CP000880_GR; SARI_00029.

KEGG

ses:SARI_00029; -.

CMR

A9MF31; SARI_00029.

Other

ProtoNet

A9MF31.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Multifunctional enzyme; Nucleotide-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 253`	`253`	`Multifunctional protein surE.`	`PRO_1000075038`
`METAL`	`8 8`		`Divalent metal cation (By similarity).`
`METAL`	`9 9`		`Divalent metal cation (By similarity).`
`METAL`	`39 39`		`Divalent metal cation (By similarity).`
`METAL`	`92 92`		`Divalent metal cation (By similarity).`

Sequence information

Length: 253 AA [This is the length of the unprocessed precursor]

Molecular weight: 27008 Da [This is the MW of the unprocessed precursor]

CRC64: E92BC60D95F21C29 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRILLSNDDG IHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFDNGD 

        70         80         90        100        110        120 
IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA 

       130        140        150        160        170        180 
LAVSLNGYQH YDTAAAVTCA LLRGLSREPL RTGRILNVNV PDLPLAQIKG IRVTRCGSRH 

       190        200        210        220        230        240 
PADKVIPQED PRGNTLYWIG PPGDKYDAGP DTDFAAVDEG YVSVTPLHVD LTAHSAHDVV 

       250 
SDWLDSVGVG TQW

A9MF31 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools