Reviewed, UniProtKB/Swiss-Prot Q8YW98 (DNLJ_ANASP)

Names and origin

Protein names

Recommended name:
    DNA ligase
    EC=6.5.1.2
Alternative name(s):
    Polydeoxyribonucleotide synthase [NAD+]

Gene names

Name:	ligA
Ordered Locus Names:	all1717

Organism

Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA By similarity. HAMAP MF_01588
Catalytic activity	NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Magnesium or manganese By similarity. HAMAP MF_01588
Sequence similarities	Belongs to the NAD-dependent DNA ligase family. LigA subfamily. Contains 1 BRCT domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Ligand	Magnesium Manganese Metal-binding NAD Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (NAD+) activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc 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 – 677	677	DNA ligase HAMAP MF_01588		PRO_0000313109
Regions
	Domain	599 – 677	79	BRCT
	Nucleotide binding	35 – 39	5	NAD By similarity
	Nucleotide binding	84 – 85	2	NAD By similarity
Sites
	Active site	117	1	N6-AMP-lysine intermediate By similarity
	Metal binding	414	1	Zinc By similarity
	Metal binding	417	1	Zinc By similarity
	Metal binding	432	1	Zinc By similarity
	Metal binding	437	1	Zinc By similarity
	Binding site	115	1	NAD By similarity
	Binding site	138	1	NAD By similarity
	Binding site	177	1	NAD By similarity
	Binding site	296	1	NAD By similarity
	Binding site	320	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YW98-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 282051173962C496	FASTA	677	75,792
	10 20 30 40 50 60 MIQTHSEVKR VEELRRLLQQ ASYAYYVSDA PIMEDAVYDQ LYRELQQLEI QHPELVTPDS 70 80 90 100 110 120 PTQRIGERPA TQFLSVRHNI PLYSLENAFN VEELQAWDQR WRRQVAPTEA EYVAELKIDG 130 140 150 160 170 180 SAIALTYQNG ILVRGATRGD GVTGEDITQN VRTIRSIPLR LNFDGIEKVE KVEVRGEAFL 190 200 210 220 230 240 PLEVFKQINE ERQKAGEQLF ANPRNAAAGT LRQLDSRIVA RRRLDFFAYT LHISGMDDAS 250 260 270 280 290 300 IANTQWEALE LLQKMGFRVN PNHKLCQSLA EVADYYKYWD TERLNLPYMT DGVVLKLNSF 310 320 330 340 350 360 KLQEQLGFTQ RFPRWAVALK YPAEEAPTRV ENIAVNVGRT GALTPLAQMR PVQLAGTTVS 370 380 390 400 410 420 RATLHNSDRI AQLDIRIGDT VIVRKAGEII PEVVRVIKEL RPADTQPFIM PTHCPVCGQP 430 440 450 460 470 480 VVRETGEAVT RCVNASCPAI LKGSIEHWVS RDALDIKGVG EKLVYQLVDK GLVHSVADLY 490 500 510 520 530 540 DLTTERLFAL ERMGEKSAQK LIEAIAQSKN QPWSRVLYGL GIRHVGSVNA QLLSEKYRAV 550 560 570 580 590 600 AELSSAKQSD IEGIYGIGAE IAQSVYQWFR INANQSLIER LQAAGLKLAN TEEIPVMNNG 610 620 630 640 650 660 ILKLNGKTFV VTGTLPTLKR DEVKALIQKA GGKVTDSVSK KTDYLVVGED AGSKLEKAQA 670 LGIAQLTETQ LLEILEE

References

[1]

"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000019 Genomic DNA. Translation: BAB78083.1.
PIR	AG2020.
RefSeq	NP_485757.1.
3D structure databases
HSSP	HSSP built from PDB template 1L7B based on UniProtKB P26996.
SMR	Q8YW98. Positions 7-322, 597-676.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8YW98.
Genome annotation databases
GeneID	1105309.
GenomeReviews	Gene locus all1717 in contig BA000019_GR.
KEGG	ana:all1717.
NMPDR	fig|103690.1.peg.2024.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0272.
HOGENOM	HBG620317.
OMA	IKHFASR.
PhylomeDB	Q8YW98.
Enzyme and pathway databases
BioCyc	NSP103690:ALL1717-MONOMER.
Family and domain databases
HAMAP	MF_01588. DNA_ligase_A. [Tree]
InterPro	IPR001357. BRCT. IPR018239. DNA_ligase_AS. IPR004150. DNA_ligase_OB. IPR001679. DNAligase. IPR013839. DNAligase_adenylation. IPR013840. DNAligase_N. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR010994. RuvA_2-like. IPR004149. Znf_DNAligase_C4. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF00533. BRCT. 1 hit. PF01653. DNA_ligase_aden. 1 hit. PF03120. DNA_ligase_OB. 1 hit. PF03119. DNA_ligase_ZBD. 1 hit. [Graphical view]
PIRSF	PIRSF001604. LigA. 1 hit.
SMART	SM00292. BRCT. 1 hit. SM00278. HhH1. 3 hits. SM00532. LIGANc. 1 hit. [Graphical view]
TIGRFAMs	TIGR00575. dnlj. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. PS01055. DNA_LIGASE_N1. 1 hit. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_ANASP

Accession

Primary (citable) accession number: Q8YW98

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)