Reviewed, UniProtKB/Swiss-Prot Q73EM3 (DNLJ_BACC1)

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:	BCE_0335

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Magnesium or manganese By similarity.
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 – 669	669	DNA ligase HAMAP MF_01588		PRO_0000313123
Regions
	Domain	591 – 669	79	BRCT
	Nucleotide binding	34 – 38	5	NAD By similarity
	Nucleotide binding	83 – 84	2	NAD By similarity
Sites
	Active site	116	1	N6-AMP-lysine intermediate By similarity
	Metal binding	405	1	Zinc By similarity
	Metal binding	408	1	Zinc By similarity
	Metal binding	423	1	Zinc By similarity
	Metal binding	428	1	Zinc By similarity
	Binding site	114	1	NAD By similarity
	Binding site	137	1	NAD By similarity
	Binding site	171	1	NAD By similarity
	Binding site	287	1	NAD By similarity
	Binding site	311	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q73EM3-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 55BCE9699B572717	FASTA	669	75,258
	10 20 30 40 50 60 MSKEIAKKRI EELRDLLNTF NYQYHVLDNP SVSDAEYDRN MQELIKLEAE NPEFMSEDSP 70 80 90 100 110 120 SVRVGGTVLD IFEKVTHKSP MLSLGNAFNE GDLRDFDRRV RQGIDDVNVR YICELKIDGL 130 140 150 160 170 180 AVSLHYEKGR FIQGATRGDG VTGEDITQNL KTIKAIPLRL NEEVTLEARG EAYMPKRSFV 190 200 210 220 230 240 KLNEEKEQNG EDVFANPRNA AAGSIRQLDP KIAAKRNLSM FVYGLANVEE KTILSHSESL 250 260 270 280 290 300 DFLGELGFKT NPNRRTCETI EEVIAYVEEW QEKRPHLDYE IDGIVIKVDD VALQESLGTT 310 320 330 340 350 360 AKSPRWAIAY KFPAEEVVTR LTGIELSVGR TGVVTPTAEL EPVRVAGTIV RRASLHNEDL 370 380 390 400 410 420 IREKDIRIGD YVVVKKAGDI IPEVVNVIFD KRTGEEEEYH MPTHCPACES ELVRLEEEVA 430 440 450 460 470 480 LRCINPTCPA QIREGLIHFV SRNAMNIDGL GERVITQLFE ADYIRTFADL YSLTKEQLLQ 490 500 510 520 530 540 LERFGEKSAT NLVKAIENSK ENSLERLLFG LGIRHVGAKA ARTFAEHFET MDALVKATEE 550 560 570 580 590 600 ELKAINEIGE KMAQSVVTYF DNEDVLELLQ QFKEYGVNMT YKGMKIADLQ NVESYFAGKT 610 620 630 640 650 660 VVLTGKLEVM GRSEAKKKIE ALGGKVTGSV SKSTDLVVAG EAAGSKLAQA EKHNVEVWNE ERFLQELNK

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017194 Genomic DNA. Translation: AAS39271.1.
RefSeq	NP_976663.1.
3D structure databases
HSSP	HSSP built from PDB template 1B04 based on UniProtKB O87703.
ModBase	Search...
Protein-protein interaction databases
STRING	Q73EM3.
Genome annotation databases
GeneID	2751513.
GenomeReviews	Gene locus BCE_0335 in contig AE017194_GR.
KEGG	bca:BCE_0335.
NMPDR	fig|222523.1.peg.335.
TIGR	BCE_0335.
Phylogenomic databases
HOGENOM	Q73EM3.
OMA	YKFPAQE.
Family and domain databases
HAMAP	MF_01588. [Tree]
InterPro	IPR001357. BRCT. IPR018239. DNA_ligase_AS. IPR004150. DNA_ligase_OB. IPR001679. DNAligase. IPR013839. DNAligase_adenylation. IPR013840. DNAligase_N. IPR000445. HhH_motif. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR012340. NA-bd_OB-fold. 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. PF00633. HHH. 1 hit. [Graphical view]
PIRSF	PIRSF001604. LigA. 1 hit.
ProDom	PD003944. DNAligase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_BACC1

Accession

Primary (citable) accession number: Q73EM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 46 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)