NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

Comments

FUNCTION: This protein seals, during DNA replication, DNA recombination and DNA repair, nicks in double-stranded DNA (By similarity).
CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
SIMILARITY: Belongs to the ATP-dependent DNA ligase 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

AE008384; AAM32410.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_634738.1; -.

3D structure databases

ModBase

Q8PTK1.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM2714-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003910;	Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from HAMAP).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0006310;	Biological process: DNA recombination (inferred from electronic annotation from HAMAP).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from HAMAP).
GO:0006260;	Biological process: DNA replication (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00407; -; 1.
PBIL [Tree]

InterPro

IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
IPR012308; DNA_ligase_A_N.
IPR016059; DNA_ligase_CS.
IPR012340; NA-bd_OB-fold.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.50.140; OB_NA_bd_sub; 1.

Pfam

PF04679; DNA_ligase_A_C; 1.
PF01068; DNA_ligase_A_M; 1.
PF04675; DNA_ligase_A_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00574; dnl1; 1.

PROSITE

PS00697; DNA_LIGASE_A1; 1.
PS00333; DNA_LIGASE_A2; FALSE_NEG.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8PTK1.

Genome annotation databases

GeneID

1481056; -.

GenomeReviews

AE008384_GR; MM_2714.

KEGG

mma:MM_2714; -.

NMPDR

fig|192952.1.peg.2714; -.

Phylogenomic databases

HOGENOM

Q8PTK1; -.

Genome annotation databases

CMR

Q8PTK1; MM_2714.

Other

UniRef

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

Keywords

ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nucleotide-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 568`	`568`	`DNA ligase.`	`PRO_0000059606`
`ACT_SITE`	`256 256`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 568 AA [This is the length of the unprocessed precursor]

Molecular weight: 63185 Da [This is the MW of the unprocessed precursor]

CRC64: D98B7C62AD2B6751 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSFREFAET CQAIEKISST IETTNKVADL LKKVDVEELP VATHFIMSEV FPAWSGEQLG 

        70         80         90        100        110        120 
IGTSLLYVSL SKASGMSIHS IESLVRTTGD IGDTALLILK EKRKNQVTFS SFFEEKPELS 

       130        140        150        160        170        180 
ITEVYRRFKI ASEASGKGSQ DIKVKNLQFL FTSSSPREAK YISRLALEEL RIGVGEGVVR 

       190        200        210        220        230        240 
DAIAKAFSVP AEIVEHSFMV TNDLGIVAAA AKKGGVEALE RLGIEINRPI KMMLSQISPD 

       250        260        270        280        290        300 
IDADIRAMKE VAIEWKFDGA RVQIHKDGNS VTLFSRKLEN VTSSLPDLVE IVRKHVKAES 

       310        320        330        340        350        360 
AILDGEAVAV DENGVPRAFQ EILKRFRRKY DVREKALGIP IQLNFFDIMY INGKTLIDLP 

       370        380        390        400        410        420 
LLERRKALES CVESSVEDSK SISVAEQVIT GDLELVEKIY REALKAGHEG VMVKNPNSVY 

       430        440        450        460        470        480 
SPGKRGKNWL KKKPLMDTLD LVIVGAEWGF GRRANLIGSY TVACYDPDTT RFLQVGKVGT 

       490        500        510        520        530        540 
GLTDDQLKEL TEILSGLMEG GEAGGVFAIR PKVVLEIAFE EIQKSPNYDS GFALRFPRFI 

       550        560 
RIRDDKDPEE ADTIQRIGRV YSQQLKRL

Q8PTK1 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