Skip Header

Contribute Send feedback
Read comments (?) or add your own

B0C308 (DNLJ_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:AM1_1187
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length675 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 – 675675DNA ligase HAMAP MF_01588
PRO_0000340320

Regions

Domain598 – 67578BRCT
Nucleotide binding36 – 405NAD By similarity
Nucleotide binding85 – 862NAD By similarity

Sites

Active site1201N6-AMP-lysine intermediate By similarity
Metal binding4161Zinc By similarity
Metal binding4191Zinc By similarity
Metal binding4341Zinc By similarity
Metal binding4391Zinc By similarity
Binding site1181NAD By similarity
Binding site1411NAD By similarity
Binding site1781NAD By similarity
Binding site2981NAD By similarity
Binding site3221NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B0C308 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 3624639891C129AB

FASTA67574,771
        10         20         30         40         50         60 
MNTVSSSDQA RVQELRQLLQ KASYAYYGLD APLMEDAVYD QLYHELVDLE AQYPQLITPD 

        70         80         90        100        110        120 
SPTQRVGERP ATQFVSVQHR IPLYSLENAF DRGDMDTWDE RWHKLVPNLS QEPGYVTELK 

       130        140        150        160        170        180 
IDGSALALTY ENGLLVRGTT RGDGTKGEEI TQNVRTIRSI PLRLNIEHPP EWLEVRGEAF 

       190        200        210        220        230        240 
LGLQVFDQIN RDRIQAGEAE FANPRNAAAG TLRQLDSKVV AERKLDFFAY TIHISGPTDD 

       250        260        270        280        290        300 
LALPQTQWQA LETLKQLGFR VNPNRRQCES LAEVQTYYDD WSLKRLDLPY LTDGVVIKLD 

       310        320        330        340        350        360 
NLGVQDELGF TQKFPRWAIA WKYPPEEAAT RIEQITVNVG RTGALTPVAE FKPVQLAGTT 

       370        380        390        400        410        420 
VSRATLHNRD RISELDIHIG DTVVVRKAGE IIPEVLRVLP ELRPAGAQPY QMPTACPSCG 

       430        440        450        460        470        480 
QPAVQLETEA VTRCVNASCP AILRGSLIHW VSRGALDIDG LGEKIVGQLT DSQMVQSVAD 

       490        500        510        520        530        540 
LYELNEDKLM DLDRMGTKLA RKIVSAIATS KQQPWHRVLY GLGIRHVGSV NAQLLTENYP 

       550        560        570        580        590        600 
TVDALMAVDG DKIATIHGIG PEIAQSVYEW FQTPTNQTLI QRLQSAGLQF EAIVSESTQP 

       610        620        630        640        650        660 
QTLSGKTFVI TGTLPTLKRD QAKQMIQDAG GKVTGSVSKN TSYVVVGADA GSKLTKAQSL 

       670 
GINQLSEADL LALLQ

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000828 Genomic DNA. Translation: ABW26224.1.
RefSeqYP_001515538.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C308.
SMRB0C308. Positions 6-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0C308.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5680010.
GenomeReviewsGene locus AM1_1187 in contig CP000828_GR.
KEGGamr:AM1_1187.
PATRIC20616812. VBIAcaMar40141_1053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBB0C308.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycAMAR329726:AM1_1187-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. 3 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_ACAM1
AccessionPrimary (citable) accession number: B0C308
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 31 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents