[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827; Baikalov C.J., Slupska M.M., Miller J.H.; Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827; DOI=10.1073/pnas.241636498; PubMed=11792869 [NCBI, ExPASy, EBI, Israel, Japan] Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.; "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."; Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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).
SUBUNIT: Monomer (By similarity).
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

U82370; AAD00532.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE009789; AAL63064.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_558882.1; -.

3D structure databases

ModBase

O93723.

Enzyme and pathway databases

BioCyc

PAER178306:PAE0833-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

O93723.

Genome annotation databases

GeneID

1465293; -.

GenomeReviews

AE009441_GR; PAE0833.

KEGG

pai:PAE0833; -.

NMPDR

fig|178306.1.peg.572; -.

Phylogenomic databases

HOGENOM

O93723; -.

Genome annotation databases

CMR

O93723; PAE0833.

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`	`1 584`	`584`	`DNA ligase.`	`PRO_0000059611`
`ACT_SITE`	`251 251`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 584 AA [This is the length of the unprocessed precursor]

Molecular weight: 64568 Da [This is the MW of the unprocessed precursor]

CRC64: 7CB44E8A5B0DBA0A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQFGELVKAL AAIEATTQRT TMVKLLVSLF KKASPEEVGK IVYFILGDLR PPWEGVELGV 

        70         80         90        100        110        120 
AEKLCLRAVS KATGAAVSEL EALYKKTGDV GEAARRALAA SKRPGLLAFG SQKPLEVSEV 

       130        140        150        160        170        180 
YDTLLKVARA TGEGAQDMKV ALLSSLFARA TPEEGKYIAR FVVGKLRLGV ADMTIIEALS 

       190        200        210        220        230        240 
DAYGVNKEAL EKAYHIYPDL GRLAKHVAEG KPLDEIRITP GVPVLPMLAQ RLSSASEILA 

       250        260        270        280        290        300 
KLGGSAICEY KYDGERAQIH LTPGGVKIFS RRLEDITHAY PDVVKAVKEA VSAKEAILEG 

       310        320        330        340        350        360 
EIVAVDPDTG DMLPFQELMH RKRKHDVATA VELYPTVLYL FDVLYVDGED LTEEPLIYRR 

       370        380        390        400        410        420 
VRLSEIVCET DKVSIAKWRI FDNAEAVDVF FHESVSMGTE GLICKSPSSI YEMGARGWNW 

       430        440        450        460        470        480 
IKYKRDYRSE MIDTVDLVVV GAFHGRGKRA GLYGAFLLAA YDPSTDMFYT VCKVGSGFTD 

       490        500        510        520        530        540 
ADLKKMYEIL QPFKIPHRHP RVVSKMEADV WFVPQVVIEV IGAEITLSPL HTCCLGAVRP 

       550        560        570        580 
GVGLAVRFPR FTGRYRSDKS PEQATTVAEM LELYKRQKKV VQPE

O93723 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