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Q980T8

- DNLI_SULSO

UniProt

Q980T8 - DNLI_SULSO

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Protein

DNA ligase

Gene

lig

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Interaction with PCNA enhances ligase activity. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.1 Publication

Catalytic activityi

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

Cofactori

a divalent metal cation1 Publication

Enzyme regulationi

Ligase activity stimulated by PCNA heterotrimer.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei258 – 2581ATP
Active sitei260 – 2601N6-AMP-lysine intermediate
Binding sitei265 – 2651ATP
Binding sitei280 – 2801ATP
Binding sitei310 – 3101ATPBy similarity
Binding sitei350 – 3501ATPBy similarity
Binding sitei427 – 4271ATP
Binding sitei433 – 4331ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. DNA binding Source: InterPro
  3. DNA ligase (ATP) activity Source: RefGenome
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. DNA biosynthetic process Source: InterPro
  4. DNA ligation Source: RefGenome
  5. DNA ligation involved in DNA repair Source: InterPro
  6. DNA recombination Source: UniProtKB-HAMAP
  7. lagging strand elongation Source: RefGenome
  8. nucleotide-excision repair Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-178-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase (EC:6.5.1.1)
Alternative name(s):
Polydeoxyribonucleotide synthase [ATP]
Gene namesi
Name:lig
Ordered Locus Names:SSO0189
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 3030Missing: No interaction with PCNA3, no stimulation by PCNA heterotrimer. 1 PublicationAdd
BLAST
Mutagenesisi110 – 1112FL → AA: Impairs interaction with PCNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 601601DNA ligasePRO_0000059618Add
BLAST

Proteomic databases

PRIDEiQ980T8.

Interactioni

Subunit structurei

Interacts with the PCNA heterotrimer, probably via subunit PCNA3.2 Publications

Protein-protein interaction databases

STRINGi273057.SSO0189.

Structurei

Secondary structure

1
601
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512Combined sources
Helixi19 – 3113Combined sources
Helixi35 – 373Combined sources
Helixi38 – 447Combined sources
Turni45 – 473Combined sources
Helixi52 – 543Combined sources
Helixi63 – 7412Combined sources
Helixi78 – 8811Combined sources
Helixi91 – 10010Combined sources
Helixi121 – 13313Combined sources
Helixi139 – 15315Combined sources
Helixi156 – 16611Combined sources
Helixi176 – 18712Combined sources
Beta strandi188 – 1903Combined sources
Helixi191 – 1933Combined sources
Helixi194 – 20310Combined sources
Helixi207 – 21711Combined sources
Helixi219 – 2224Combined sources
Beta strandi237 – 2404Combined sources
Helixi244 – 2507Combined sources
Turni251 – 2533Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi262 – 27110Combined sources
Beta strandi274 – 2785Combined sources
Helixi286 – 2883Combined sources
Helixi290 – 29910Combined sources
Beta strandi303 – 31412Combined sources
Turni316 – 3183Combined sources
Helixi325 – 3328Combined sources
Helixi336 – 3427Combined sources
Beta strandi345 – 35511Combined sources
Helixi365 – 37511Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi387 – 3926Combined sources
Helixi393 – 40513Combined sources
Beta strandi410 – 4145Combined sources
Beta strandi427 – 4359Combined sources
Helixi436 – 4394Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi444 – 45512Combined sources
Helixi458 – 4603Combined sources
Beta strandi463 – 47311Combined sources
Turni474 – 4774Combined sources
Beta strandi478 – 4858Combined sources
Helixi491 – 50212Combined sources
Beta strandi505 – 5084Combined sources
Beta strandi520 – 5234Combined sources
Beta strandi528 – 53912Combined sources
Turni544 – 5485Combined sources
Beta strandi554 – 5596Combined sources
Beta strandi561 – 5655Combined sources
Helixi571 – 5733Combined sources
Helixi577 – 58610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HIVX-ray2.05A1-601[»]
2HIXX-ray2.87A1-601[»]
ProteinModelPortaliQ980T8.
SMRiQ980T8. Positions 1-590.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ980T8.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

eggNOGiCOG1793.
HOGENOMiHOG000036008.
InParanoidiQ980T8.
KOiK10747.
OMAiCTDIGEL.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
HAMAPiMF_00407. DNA_ligase.
InterProiIPR022865. 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]
PfamiPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00574. dnl1. 1 hit.
PROSITEiPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q980T8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEFKVIAEYF DKLEKISSRL QLTALLADLL SKSDKTIIDK VVYIIQGKLW
60 70 80 90 100
PDFLGYPELG IGEKFLIKAI SIATNTDENS VENLYKTIGD LGEVARRLKS
110 120 130 140 150
KQQSTGILGF LGTTSKESLT VDEVYSTLSK VALTTGEGSR DLKIRLLAGL
160 170 180 190 200
LKKADPLEAK FLVRFVEGRL RVGIGDATVL DAMAIAFGGG QSASEIIERA
210 220 230 240 250
YNLRADLGNI AKIIVEKGIE ALKTLKPQVG IPIRPMLAER LSNPEEILKK
260 270 280 290 300
MGGNAIVDYK YDGERAQIHK KEDKIFIFSR RLENITSQYP DVVDYVSKYI
310 320 330 340 350
EGKEFIIEGE IVAIDPESGE MRPFQELMHR KRKSDIYEAI KEYPVNVFLF
360 370 380 390 400
DLMYYEDVDY TTKPLEARRK LLESIVKPND YVKIAHHIQA NNVEDLKSFF
410 420 430 440 450
YRAISEGGEG VMVKAIGKDA IYQAGARGWL WIKLKRDYQS EMADTVDLVV
460 470 480 490 500
VGGFYGKGKR GGKISSLLMA AYNPKTDSFE SVCKVASGFS DEQLDELQKK
510 520 530 540 550
LMEIKRDVKH PRVNSKMEPD IWVEPVYVAE IIGSEITISP LHTCCQDVVE
560 570 580 590 600
KDAGLSIRFP RFIRWRDDKS PEDATTTDEI LEMYNKQPKK KIESPAVDES

V
Length:601
Mass (Da):67,733
Last modified:October 1, 2001 - v1
Checksum:iDA6814F4A6F0546E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40535.1.
PIRiH90159.
RefSeqiNP_341745.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40535; AAK40535; SSO0189.
GeneIDi1455345.
KEGGisso:SSO0189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40535.1 .
PIRi H90159.
RefSeqi NP_341745.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HIV X-ray 2.05 A 1-601 [» ]
2HIX X-ray 2.87 A 1-601 [» ]
ProteinModelPortali Q980T8.
SMRi Q980T8. Positions 1-590.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273057.SSO0189.

Proteomic databases

PRIDEi Q980T8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK40535 ; AAK40535 ; SSO0189 .
GeneIDi 1455345.
KEGGi sso:SSO0189.

Phylogenomic databases

eggNOGi COG1793.
HOGENOMi HOG000036008.
InParanoidi Q980T8.
KOi K10747.
OMAi CTDIGEL.

Enzyme and pathway databases

BioCyci SSOL273057:GCH2-178-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q980T8.

Family and domain databases

Gene3Di 1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
HAMAPi MF_00407. DNA_ligase.
InterProi IPR022865. 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 ]
Pfami PF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00574. dnl1. 1 hit.
PROSITEi PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus."
    Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.
    Mol. Cell 11:275-282(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH PCNA3, SUBUNIT, MUTAGENESIS OF 1-MET--LEU-30.
  3. "A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA."
    Pascal J.M., Tsodikov O.V., Hura G.L., Song W., Cotner E.A., Classen S., Tomkinson A.E., Tainer J.A., Ellenberger T.
    Mol. Cell 24:279-291(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEXES WITH ATP AND PCNA, PARTIAL PROTEIN SEQUENCE, SUBUNIT, MUTAGENESIS OF 110-PHE-LEU-111, COFACTOR.

Entry informationi

Entry nameiDNLI_SULSO
AccessioniPrimary (citable) accession number: Q980T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: October 1, 2001
Last modified: November 26, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3