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A4YD25 (DNLI_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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

Names and origin

Protein namesRecommended name:
DNA ligase

EC=6.5.1.1
Alternative name(s):
Polydeoxyribonucleotide synthase [ATP]
Gene names
Name:lig
Ordered Locus Names:Msed_0150
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair By similarity. HAMAP-Rule MF_00407

Catalytic activity

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). HAMAP-Rule MF_00407

Cofactor

Divalent metal cations By similarity. HAMAP-Rule MF_00407

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598DNA ligase HAMAP-Rule MF_00407
PRO_1000072271

Sites

Active site2611N6-AMP-lysine intermediate By similarity
Binding site2591ATP By similarity
Binding site2661ATP By similarity
Binding site2811ATP By similarity
Binding site3111ATP By similarity
Binding site3511ATP By similarity
Binding site4281ATP By similarity
Binding site4341ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YD25 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: A9C70DF05DA44BB0

FASTA59867,922
        10         20         30         40         50         60 
MKFKLIAEYF DRLEKISSRI QLTSLLSDLF KNTEREVIDK VVYLIQGRLW PDFTGMPEIG 

        70         80         90        100        110        120 
MGEKFLIKAI AMAYGNKEEE VEKLYKNIGD LGEVAYSLRS KVKGVSILSF VGGNQEAGEL 

       130        140        150        160        170        180 
DVMEVYNELV KIATSTGEGS RDIKIRIFAG LIKKATPIEA KYLVRFVEGR LRLGIGDATV 

       190        200        210        220        230        240 
LDALAITFGG SADYRPIVER AYNLRADLGD IARVIATEGI EKLKNISPTP GIPIRPMLAE 

       250        260        270        280        290        300 
RLPDPEEIME KMNGKALVDY KYDGERAQIH RKGDKVTIFS RRMENITDQY IDVTEYVKQF 

       310        320        330        340        350        360 
VKGDNFIVEG EIVPVDPESG EMRPFQELMH RRRKNNIAEA IKEYPVNLFL FDLMFFEGED 

       370        380        390        400        410        420 
YTTKPLPERR AKLEEILASN DKVHIASHII ADRVDKLREY FYQAISEGAE GVMVKSIGPD 

       430        440        450        460        470        480 
SIYQAGSRGW LWIKLKRDYQ SEMADTVDLV VVGAFYGKGK RGGKFSSLLM AAYNPEKDVF 

       490        500        510        520        530        540 
ETVCKVASGF SDQELDEMQK KINELKREQK HPRVVSDMIP DVWVSPTLVA EVIGAEITIS 

       550        560        570        580        590 
PLHTCCRGEK GGLSIRFPRF IRWRDDKSPE DATTNQEIME MYSKQLKKIE EKPVDENI 

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP94327.1.
RefSeqYP_001190251.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YD25.
SMRA4YD25. Positions 1-588.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399549.Msed_0150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP94327; ABP94327; Msed_0150.
GeneID5105003.
KEGGmse:Msed_0150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1793.
HOGENOMHOG000036008.
KOK10747.
OMALDPSGYN.

Enzyme and pathway databases

BioCycMSED399549:GH1O-160-MONOMER.

Family and domain databases

Gene3D1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
HAMAPMF_00407. DNA_ligase.
InterProIPR022865. DNA_ligae_ATP-dep_bac/arc.
IPR000977. DNA_ligase_ATP-dep.
IPR012309. DNA_ligase_ATP-dep_C.
IPR012310. DNA_ligase_ATP-dep_cent.
IPR016059. DNA_ligase_ATP-dep_CS.
IPR012308. DNA_ligase_ATP-dep_N.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00574. dnl1. 1 hit.
PROSITEPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLI_METS5
AccessionPrimary (citable) accession number: A4YD25
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 51 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