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Q9Z585 (DNLJ1_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. 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 1

EC=6.5.1.2
Alternative name(s):
Polydeoxyribonucleotide synthase [NAD+] 1
Gene names
Name:ligA1
Ordered Locus Names:SCO5494
ORF Names:SC8D9.06
OrganismStreptomyces coelicolor
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length735 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
Reference 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 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 – 735735DNA ligase 1 HAMAP MF_01588
PRO_0000161767

Regions

Domain643 – 73290BRCT
Nucleotide binding48 – 525NAD By similarity
Nucleotide binding97 – 982NAD By similarity

Sites

Active site1301N6-AMP-lysine intermediate By similarity
Metal binding4231Zinc By similarity
Metal binding4261Zinc By similarity
Metal binding4421Zinc By similarity
Metal binding4481Zinc By similarity
Binding site1281NAD By similarity
Binding site1511NAD By similarity
Binding site1881NAD By similarity
Binding site3051NAD By similarity
Binding site3291NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z585 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 39C4DE1C7CC55930

FASTA73580,572
        10         20         30         40         50         60 
MAGDKQGDKQ AETTSVPAEA RERHAQLAEQ IEEHRFRYYV NDAPVVSDAE FDRLLRTLEE 

        70         80         90        100        110        120 
LEERHPELRT PESPTQKVAG AYATEFTAVQ HPTRMLSLDN TFNDDELAAW FERIARELGE 

       130        140        150        160        170        180 
QEYHFLCELK VDGLAVNLTY ERGRLVRAAT RGDGRTGEDI TPNVRTIAEI PDRLAGDKVP 

       190        200        210        220        230        240 
DLVEIRGEVY FPMEKFQELN ARLNEAGDKP FANARNAAAG SLRQKDPRVT ASRPLHMVVH 

       250        260        270        280        290        300 
GIGTLEGYSG LTRLSQAYDL LKAWGLPTSP HNRVVDGLDG VREFIAYYGE NRHSVAHEID 

       310        320        330        340        350        360 
GVVVKVDEIR LQGRLGSTAR APRWAIAYKY APEEVNTKLV DIKVGVGRTG RVTPYAQVEP 

       370        380        390        400        410        420 
VTVAGSEVEF ATLHNQEVVK AKGVLIGDTV VLRKAGDVIP EILGPVADLR DGSEREFVMP 

       430        440        450        460        470        480 
AECPECGTPL KAMKEGDIDL RCPNARACPA QLRERVAYLA GRECLDIEHF GGVVAAALTG 

       490        500        510        520        530        540 
PLEPSEPPLV DEGDLFDLTV EKLLPIKAYV LDPDSGLPKR DPKTGEEKIA TVFANKEGEP 

       550        560        570        580        590        600 
KKNTLALLQH IEEAKTRPLA RFINGLSIRY VGPVAAQALA REFRSIDRIE QATEEELAST 

       610        620        630        640        650        660 
DGVGGAIATA VKEWFAVDWH REIVRKWKAA GVPLEDRSTG EDEGPRPLEG LTVVVTGTLE 

       670        680        690        700        710        720 
NFTRDGAKEA LQSRGAKVTG SVSKKTSFVV VGDNPGSKYD KAMQLKVPVL NEDGFAVLLE 

       730 
QGPEAAADVA LSAEE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939123 Genomic DNA. Translation: CAB37570.1.
PIRT35810.
RefSeqNP_629629.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9Z585.
SMRQ9Z585. Positions 15-333.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1100934.
GenomeReviewsGene locus SCO5494 in contig AL645882_GR.
KEGGsco:SCO5494.
NMPDRfig|100226.1.peg.5446.
PATRIC23740844. VBIStrCoe124346_5578.

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ9Z585.
ProtClustDBPRK07956.

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.
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.
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 nameDNLJ1_STRCO
AccessionPrimary (citable) accession number: Q9Z585
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 79 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