Q9YMV2 (DNLI_NPVLD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA ligase
EC=6.5.1.1

Alternative name(s):
Polydeoxyribonucleotide synthase [ATP]

Gene names

Name:	LIG
Ordered Locus Names:	LdOrf-22

Organism

Lymantria dispar multicapsid nuclear polyhedrosis virus (LdMNPV)

Taxonomic identifier

10449 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Baculoviridae › Alphabaculovirus

Virus host

Lepidoptera (butterflies and moths) [TaxID: 7088]

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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).
Cofactor	Divalent metal cations By similarity.
Sequence similarities	Belongs to the ATP-dependent DNA ligase family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication
Ligand	ATP-binding Metal-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	DNA ligation involved in DNA repair Inferred from electronic annotation. Source: InterPro DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (ATP) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	DNA ligase		PRO_0000059593
Sites
	Active site	198	1	N6-AMP-lysine intermediate By similarity
	Metal binding	250	1	Divalent metal cation 1 By similarity
	Metal binding	345	1	Divalent metal cation 2 By similarity
	Binding site	196	1	ATP By similarity
	Binding site	203	1	ATP By similarity
	Binding site	218	1	ATP By similarity
	Binding site	250	1	ATP By similarity
	Binding site	284	1	ATP By similarity
	Binding site	361	1	ATP By similarity
	Binding site	365	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YMV2 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 74F5A2A3CDC24419	FASTA	548	61,975
	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

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF081810 Genomic DNA. Translation: AAC70207.1.
PIR	T30369.
RefSeq	NP_047658.1. NC_001973.1.
3D structure databases
ProteinModelPortal	Q9YMV2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1488619.
Phylogenomic databases
ProtClustDB	CLSP2743283.
Family and domain databases
InterPro	IPR000977. DNA_ligase_ATP-dep. IPR012309. DNA_ligase_ATP-dep_C. IPR012310. DNA_ligase_ATP-dep_cent. IPR016059. DNA_ligase_ATP-dep_CS. IPR012308. DNA_ligase_ATP-dep_N. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. PF04675. DNA_ligase_A_N. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00574. Dnl1. 1 hit.
PROSITE	PS00697. DNA_LIGASE_A1. 1 hit. PS00333. DNA_LIGASE_A2. False negative. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLI_NPVLD

Accession

Primary (citable) accession number: Q9YMV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	May 1, 1999
Last modified:	September 21, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program