DNA ligase - Bacillus cereus (strain ZK / E33L)

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Reviewed, UniProtKB/Swiss-Prot Q63GS3 (DNLJ_BACCZ)

Last modified November 3, 2009. Version 41. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	BCE33L0279

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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...

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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_0000313125

Regions

Domain

591 – 669

BRCT

Nucleotide binding

34 – 38

NAD By similarity

Nucleotide binding

83 – 84

NAD By similarity

Sites

Active site

116

N6-AMP-lysine intermediate By similarity

Metal binding

405

Zinc By similarity

Metal binding

408

Zinc By similarity

Metal binding

423

Zinc By similarity

Metal binding

428

Zinc By similarity

Binding site

114

NAD By similarity

Binding site

137

NAD By similarity

Binding site

171

NAD By similarity

Binding site

287

NAD By similarity

Binding site

311

NAD By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q63GS3-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 24E3E273EBCE9971
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FASTA

669

75,182

        10         20         30         40         50         60 
MSKEIAKKRI EELRDLLNTF NYQYHVLDNP SVSDAEYDRN MQELIKLEAE NPEFMSEDSP 

        70         80         90        100        110        120 
SVRVGGTVLD IFEKVTHKSP MLSLGNAFNE GDLRDFDRRV RQGIDDANVR YICELKIDGL 

       130        140        150        160        170        180 
AVSLHYEKGR FIQGATRGDG VTGEDITQNL KTIKAIPLRL NEEVTLEARG EAYMPKRSFV 

       190        200        210        220        230        240 
KLNEEKEQNG EDVFANPRNA AAGSIRQLDP KIAAKRNLSM FVYGLANVEE KTIPSHSESL 

       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 GERVITQLFD ADYIRTFADL YSLTKEQLLQ 

       490        500        510        520        530        540 
LERFGEKSAT NLVQAIENSK ENSLERLLFG LGIRHVGAKA ARTFAEHFET MDALVKATEE 

       550        560        570        580        590        600 
ELKTINEIGE KMAQSVVAYF DNEDVLELLQ QFKEYGVNMT YKGIKIADLQ NVESYFAGKT 

       610        620        630        640        650        660 
VVLTGKLEVM GRSEAKKKIE ALGGKVTGSV SKSTDLVVAG EAAGSKLAQA EKHNVEVWNE 


ERFLQELNK

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References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis."
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P.

Gilna P.
J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	CP000001 Genomic DNA. Translation: AAU19960.1.
RefSeq	YP_081888.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q63GS3.
Genome annotation databases
GeneID	3023912.
GenomeReviews	Gene locus BCE33L0279 in contig CP000001_GR.
KEGG	bcz:BCZK0279.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63GS3.
OMA	YKFPAQE.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L0279-MON.
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...

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Entry information

Entry name

DNLJ_BACCZ

Accession

Primary (citable) accession number: Q63GS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 41 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents