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Q980T8

- DNLI_SULSO

UniProt

Q980T8 - DNLI_SULSO

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Protein
DNA ligase
Gene
lig, SSO0189
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).UniRule annotation

Cofactori

Divalent metal cations.1 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 – 3101ATP By similarity
Binding sitei350 – 3501ATP By 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. DNA ligation Source: RefGenome
  2. DNA ligation involved in DNA repair Source: InterPro
  3. DNA recombination Source: UniProtKB-HAMAP
  4. cell cycle Source: UniProtKB-KW
  5. cell division Source: UniProtKB-KW
  6. lagging strand elongation Source: RefGenome
  7. 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. 2 Publications
Add
BLAST
Mutagenesisi110 – 1112FL → AA: Impairs interaction with PCNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 601601DNA ligaseUniRule annotation
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HIVX-ray2.05A1-601[»]
2HIXX-ray2.87A1-601[»]
ProteinModelPortaliQ980T8.
SMRiQ980T8. Positions 1-590.

Miscellaneous databases

EvolutionaryTraceiQ980T8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1793.
HOGENOMiHOG000036008.
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

MEFKVIAEYF DKLEKISSRL QLTALLADLL SKSDKTIIDK VVYIIQGKLW    50
PDFLGYPELG IGEKFLIKAI SIATNTDENS VENLYKTIGD LGEVARRLKS 100
KQQSTGILGF LGTTSKESLT VDEVYSTLSK VALTTGEGSR DLKIRLLAGL 150
LKKADPLEAK FLVRFVEGRL RVGIGDATVL DAMAIAFGGG QSASEIIERA 200
YNLRADLGNI AKIIVEKGIE ALKTLKPQVG IPIRPMLAER LSNPEEILKK 250
MGGNAIVDYK YDGERAQIHK KEDKIFIFSR RLENITSQYP DVVDYVSKYI 300
EGKEFIIEGE IVAIDPESGE MRPFQELMHR KRKSDIYEAI KEYPVNVFLF 350
DLMYYEDVDY TTKPLEARRK LLESIVKPND YVKIAHHIQA NNVEDLKSFF 400
YRAISEGGEG VMVKAIGKDA IYQAGARGWL WIKLKRDYQS EMADTVDLVV 450
VGGFYGKGKR GGKISSLLMA AYNPKTDSFE SVCKVASGFS DEQLDELQKK 500
LMEIKRDVKH PRVNSKMEPD IWVEPVYVAE IIGSEITISP LHTCCQDVVE 550
KDAGLSIRFP RFIRWRDDKS PEDATTTDEI LEMYNKQPKK KIESPAVDES 600
V 601
Length:601
Mass (Da):67,733
Last modified:October 1, 2001 - v1
Checksum:iDA6814F4A6F0546E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK40535.1.
PIRiH90159.
RefSeqiNP_341745.1. NC_002754.1.
WP_009990427.1. NC_002754.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK40535.1 .
PIRi H90159.
RefSeqi NP_341745.1. NC_002754.1.
WP_009990427.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
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: September 3, 2014
This is version 88 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

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