[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=KOD1; DOI=10.1128/JB.182.22.6424-6433.2000; PubMed=11053387 [NCBI, ExPASy, EBI, Israel, Japan] Nakatani M., Ezaki S., Atomi H., Imanaka T.; "A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity."; J. Bacteriol. 182:6424-6433(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=KOD1; DOI=10.1101/gr.3003105; PubMed=15710748 [NCBI, ExPASy, EBI, Israel, Japan] Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."; Genome Res. 15:352-363(2005).

Comments

FUNCTION: This protein seals, during DNA replication, DNA recombination and DNA repair, nicks in double-stranded DNA.
CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
COFACTOR: Magnesium.
COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8.0;
Temperature dependence: Still active at 100 degrees Celsius. Thermostable;
SUBUNIT: Monomer.
MISCELLANEOUS: Can also use NAD, but less efficiently than ATP.
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

AB042527; BAB15949.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP006878; BAD86329.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_184553.1; -.

3D structure databases

SMR

Q9HHC4; 1-558.

ModBase

Q9HHC4.

Enzyme and pathway databases

BioCyc

TKOD69014:TK2140-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003910;	Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from HAMAP).
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; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q9HHC4.

Genome annotation databases

3235455; -.

AP006878_GR; TK2140.

tko:TK2140; -.

fig|69014.3.peg.2141; -.

Phylogenomic databases

HOGENOM

Q9HHC4; -.

Genome annotation databases

CMR

Q9HHC4; TK2140.

Other

ProtoNet

Q9HHC4.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 559`	`559`	`DNA ligase.`	`PRO_0000059615`
`ACT_SITE`	`249 249`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 559 AA [This is the length of the unprocessed precursor]

Molecular weight: 63749 Da [This is the MW of the unprocessed precursor]

CRC64: 91AB32542E03D20D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRYSELADLY RRLEKTTLKT LKTKFVADFL KKTPDELLEI VPYLILGKVF PDWDERELGV 

        70         80         90        100        110        120 
GEKLLIKAVS MATGVPEKEI EDSVRDTGDL GESVALAIKK KKQKSFFSQP LTIKRVYDTF 

       130        140        150        160        170        180 
VKIAEAQGEG SQDRKMKYLA NLFMDAEPEE GKYLARTVLG TMRTGVAEGI LRDAIAEAFR 

       190        200        210        220        230        240 
VKPELVERAY MLTSDFGYVA KIAKLEGNEG LSKVRIQIGK PIRPMLAQNA ASVKDALIEM 

       250        260        270        280        290        300 
GGEAAFEIKY DGARVQVHKD GDKVIVYSRR LENVTRSIPE VIEAIKAALK PEKAIVEGEL 

       310        320        330        340        350        360 
VAVGENGRPR PFQYVLRRFR RKYNIDEMIE KIPLELNLFD VMFVDGESLI ETKFIDRRNK 

       370        380        390        400        410        420 
LEEIVKESEK IKLAEQLITK KVEEAEAFYR RALELGHEGL MAKRLDSIYE PGNRGKKWLK 

       430        440        450        460        470        480 
IKPTMENLDL VIIGAEWGEG RRAHLLGSFL VAAYDPHSGE FLPVGKVGSG FTDEDLVEFT 

       490        500        510        520        530        540 
KMLKPYIVRQ EGKFVEIEPK FVIEVTYQEI QKSPKYKSGF ALRFPRYVAL REDKSPEEAD 

       550 
TIERVAELYE LQERFKAKK

Q9HHC4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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