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A0KHL9 (DNLJ_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA ligase
EC=6.5.1.2
Alternative name(s):
Polydeoxyribonucleotide synthase [NAD+]
Gene names
Name:ligA
Ordered Locus Names:AHA_1229
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length668 AA.
Sequence statusComplete.
Protein existenceInferred 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 processDNA damage
DNA repair
DNA replication
   LigandMagnesium
Manganese
Metal-binding
NAD
Zinc
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA ligase (NAD+) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668DNA ligase HAMAP MF_01588
PRO_0000313104

Regions

Domain590 – 66879BRCT
Nucleotide binding32 – 365NAD By similarity
Nucleotide binding81 – 822NAD By similarity

Sites

Active site1151N6-AMP-lysine intermediate By similarity
Metal binding4071Zinc By similarity
Metal binding4101Zinc By similarity
Metal binding4251Zinc By similarity
Metal binding4311Zinc By similarity
Binding site1131NAD By similarity
Binding site1361NAD By similarity
Binding site1731NAD By similarity
Binding site2891NAD By similarity
Binding site3131NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0KHL9 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 614F9D33C08EE547

FASTA66872,369
        10         20         30         40         50         60 
MSDILSRHRQ LCELLIEYGH QYYVLDNPTV PDAEYDRLMR ELIVLEAEHP ELKTPASPSV 

        70         80         90        100        110        120 
RVGGQPLTAF KQVRHEIPML SLDNVFSGEE LQAFEQRMRD RLKREVSFTF CCEPKLDGLA 

       130        140        150        160        170        180 
VSLLYVAGQL VQAATRGDGT TGEEITENVR TIKAIPLSLR GEGWPARLEV RGEVFMPKAG 

       190        200        210        220        230        240 
FEAMNAKALA AGEKVFVNPR NAAAGSLRQL DSRITASRPL AFYAYGVGVG GEQLGGSHFG 

       250        260        270        280        290        300 
RLNQLKEWGL PLSPEVKLKE GAAGCQAFHD DILARRGELP YEIDGVVYKV DAIPLQEELG 

       310        320        330        340        350        360 
FVARAPRWAT AHKFPAQEEM TELENVEFQV GRTGAVTPVA KLKPVFVGGV TVSNATLHNA 

       370        380        390        400        410        420 
DEIERLGVMI GDTVIVRRAG DVIPQIVAVV EAQRPADARA ILFPTECPVC GSAVERLEGE 

       430        440        450        460        470        480 
AVTRCSGGLF CEAQRKEAIK HFAARRAMDV DGLGDKIVEQ LVDKGLVKTP ADLFSLNAIQ 

       490        500        510        520        530        540 
LAGLERMGQK SALNLVAAID AARSTTLPRF LFALGIREVG EATALNLANH FLTLDALRAA 

       550        560        570        580        590        600 
SVEQLLEVAD VGDIVAKHVY YFLRQPHNIE VLEALLAAGI HWPAIEKKEA SEQPFAGKTF 

       610        620        630        640        650        660 
VLTGTLTTLS RNDAKAALQA LGAKVAGSVS AKTDVLVAGE AAGSKLVKAQ ELGITVWSEE 


ELQQALQG

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000462 Genomic DNA. Translation: ABK36968.1.
RefSeqYP_855770.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KHL9.
SMRA0KHL9. Positions 6-584.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KHL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4490605.
GenomeReviewsGene locus AHA_1229 in contig CP000462_GR.
KEGGaha:AHA_1229.
PATRIC20780012. VBIAerHyd135212_1236.
TIGRAHA_1229.

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA0KHL9.
ProtClustDBCLSK2516575.

Enzyme and pathway databases

BioCycAHYD196024:AHA_1229-MONOMER.

Family and domain databases

HAMAPMF_01588. DNA_ligase_A.
[Tree]
InterProIPR001357. 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]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01972.
PfamPF00533. BRCT. 1 hit.
PF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
PF03119. DNA_ligase_ZBD. 1 hit.
[Graphical view]
PIRSFPIRSF001604. LigA. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00278. HhH1. 4 hits.
SM00532. LIGANc. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
SSF50249. Nucleic_acid_OB. 1 hit.
SSF47781. RuvA_2_like. 1 hit.
TIGRFAMsTIGR00575. Dnlj. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS01055. DNA_LIGASE_N1. 1 hit.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_AERHH
AccessionPrimary (citable) accession number: A0KHL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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