NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
DOI=10.1101/gr.1285603; PubMed=12840036 [NCBI, ExPASy, EBI, Israel, Japan]
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens.";
Genome Res. 13:1572-1579(2003).

Comments

FUNCTION: Hydrolyzes non-standard nucleotides such as XTP and dITP/ITP. Might exclude non-standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions (By similarity).
CATALYTIC ACTIVITY: NTP + H₂O = NDP + phosphate.
COFACTOR: Divalent cations (By similarity).
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the HAM1 NTPase 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

BA000035; BAC19210.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_739010.1; -.

3D structure databases

HSSP

P52061; 1K7K. [HSSP ENTRY / PDB]

ModBase

Q8FMU9.

Enzyme and pathway databases

BioCyc

CEFF196164:CE2400-MON; -.

Ontologies

GO:0017111;	Molecular function: nucleoside-triphosphatase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01405; -; 1.
PBIL [Tree]

InterPro

IPR002637; Ham1p_like.
Graphical view of domain structure.

PANTHER

PTHR11067; Ham1p_like; 1.

Pfam

PF01725; Ham1p_like; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00042; Ham1p_like; 1.

BLOCKS

Q8FMU9.

Genome annotation databases

1034567; -.

BA000035_GR; CE2400.

cef:CE2400; -.

fig|196164.1.peg.2400; -.

Phylogenomic databases

HOGENOM

Q8FMU9; -.

Genome annotation databases

CMR

Q8FMU9; CE2400.

Other

ProtoNet

Q8FMU9.

UniRef

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

Keywords

Complete proteome; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 221`	`221`		`Nucleoside-triphosphatase.`	`PRO_0000178158`

Sequence information

Length: 221 AA [This is the length of the unprocessed precursor]

Molecular weight: 23800 Da [This is the MW of the unprocessed precursor]

CRC64: CEFDF6BA87F9F8D5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNSSMHRRPP WESDMKLLVA SNNAKKLGEL QRILDQAGIE NVELLALADV PSYPEPVEDG 

        70         80         90        100        110        120 
RTFTENALIK ARAGASNTGL ITLADDSGLE VDALNGMPGV LSARWAGKHG NDQANNDLLL 

       130        140        150        160        170        180 
AQIADIPEEH RGAAFVSVCA IVTPDGREFV EEGRWHGTLL REPVGTNGFG YDPLFVPMEE 

       190        200        210        220 
SLIEGRDRSS AQLTAQEKDA LSHRGKALRA LVPAIAELAG Q

Q8FMU9 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