[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1006/viro.1998.9469; PubMed=9887315 [NCBI, ExPASy, EBI, Israel, Japan] Kuzio J., Pearson M.N., Harwood S.H., Funk C.J., Evans J.T., Slavicek J.M., Rohrmann G.F.; "Sequence and analysis of the genome of a baculovirus pathogenic for Lymantria dispar."; Virology 253:17-34(1999).
[2]	CHARACTERIZATION. PubMed=9765460 [NCBI, ExPASy, EBI, Israel, Japan] Pearson M.N., Rohrmann G.F.; "Characterization of a baculovirus-encoded ATP-dependent DNA ligase."; J. Virol. 72:9142-9149(1998).

Comments

FUNCTION: Able to ligate a double-stranded synthetic DNA substrate containing a single nick and inefficiently ligated a 1 nucleotide gap but did not ligate a 2 nucleotide gap. It is able to ligate short, complementary overhangs but not blunt-ended double-stranded DNA. May be implicated in DNA repair and recombination.
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

AF081810; AAC70207.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T30369; T30369.

RefSeq

NP_047658.1; -.

3D structure databases

ModBase

Q9YMV2.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0003910;	Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from InterPro).
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 InterPro).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from InterPro).
GO:0006260;	Biological process: DNA replication (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
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.
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

Q9YMV2.

Genome annotation databases

GeneID

1488619; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 548`	`548`	`DNA ligase.`	`PRO_0000059593`
`ACT_SITE`	`198 198`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 548 AA [This is the length of the unprocessed precursor]

Molecular weight: 61975 Da [This is the MW of the unprocessed precursor]

CRC64: 74F5A2A3CDC24419 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENHDSFYKF CQLCQSLYDA DDHQEKRDAL ERHFADFRGS AFMWRELLAP AESDAAADRE 

        70         80         90        100        110        120 
LTLIFETILS IERTEQENVT RNLKCTIDGA AVPLSRESRI TVPQVYEFIN DLRGSGSRQE 

       130        140        150        160        170        180 
RLRLIGQFAA GCTDEDLLTV FRVVSDHAHA GLSAEDVMEL VEPWERFQKP VPPALAQPCR 

       190        200        210        220        230        240 
RLASVLVKHP EGALAEVKYD GERVQVHKAG SRFKFFSRTL KPVPEHKVAG CREHLTRAFP 

       250        260        270        280        290        300 
RARNFILDAE IVMVDGSGEA LPFGTLGRLK QMEHADGHVC MYIFDCLRYN GVSYLNATPL 

       310        320        330        340        350        360 
DFRRRVLQDE IVPIEGRVVL SAMERTNTLS ELRRFVHRTL ATGAEGVVLK GRLSSYAPNK 

       370        380        390        400        410        420 
RDWFKMKKEH LCDGALVDTL DLVVLGAYYG TGRNCRKMSV FLMGCLDRES NVWTTVTKVH 

       430        440        450        460        470        480 
SGLADAALTA LSKELRPLMA APRDDLPEWF DCNESMVPHL LAADPEKMPV WEIACSEMKA 

       490        500        510        520        530        540 
NIGAHTAGVT MRFPRVKRFR PDKDWSTATD LQEAEQLIRN SQENTKKTFA RLATTYDGPS 


PNKKLKLN

Q9YMV2 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