Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA ligase 1

Gene

cdc17

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).PROSITE-ProRule annotation

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei414 – 4141ATPBy similarity
Active sitei416 – 4161N6-AMP-lysine intermediatePROSITE-ProRule annotation
Binding sitei421 – 4211ATPBy similarity
Binding sitei437 – 4371ATPBy similarity
Metal bindingi469 – 4691Magnesium 1By similarity
Metal bindingi568 – 5681Magnesium 2By similarity
Binding sitei573 – 5731ATPBy similarity
Binding sitei587 – 5871ATPBy similarity
Binding sitei593 – 5931ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: InterPro
  • DNA ligase (ATP) activity Source: PomBase
  • DNA ligase activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • base-excision repair Source: PomBase
  • cell division Source: UniProtKB-KW
  • DNA biosynthetic process Source: InterPro
  • DNA recombination Source: PomBase
  • DNA repair Source: PomBase
  • nucleotide-excision repair Source: PomBase
  • Okazaki fragment processing involved in mitotic DNA replication Source: PomBase
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, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-174414. Processive synthesis on the C-strand of the telomere.
R-SPO-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-SPO-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-SPO-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-69183. Processive synthesis on the lagging strand.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase 1 (EC:6.5.1.1)
Alternative name(s):
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene namesi
Name:cdc17
ORF Names:SPAC20G8.01, SPAC57A10.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC20G8.01.
PomBaseiSPAC20G8.01. cdc17.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 768768DNA ligase 1PRO_0000059585Add
BLAST

Proteomic databases

MaxQBiP12000.

Interactioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei165 – 1651Interaction with target DNABy similarity
Sitei438 – 4381Interaction with target DNABy similarity
Sitei619 – 6191Interaction with target DNABy similarity
Sitei644 – 6441Interaction with target DNABy similarity

Protein-protein interaction databases

BioGridi278340. 14 interactions.
MINTiMINT-4687250.

Structurei

3D structure databases

ProteinModelPortaliP12000.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni309 – 31810Interaction with target DNABy similarity
Regioni490 – 4923Interaction with target DNABy similarity

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

HOGENOMiHOG000036006.
InParanoidiP12000.
KOiK10747.
OMAiSQCPNYD.
OrthoDBiEOG7TXKRG.
PhylomeDBiP12000.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR000977. 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.

P12000-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTVFSQIPR FKQVNQYIRM STRQSDISNF FISSASHKSE HVEVSQSSSD
60 70 80 90 100
SKNVDGRSTS EKRKVESVKL VDESKHNNHD DTGTQNVERE NNIVSEAKKQ
110 120 130 140 150
KTLGSSSSSS DAVSSNNDSG ASTPIPLPIK EPPLESNARN DKLKGHATFA
160 170 180 190 200
EMVKAFTKIE NTSKRLEIID IMGTYFFGIL RDHPSDLLAC VYLSINKLGP
210 220 230 240 250
DYSGLELGIG ESIIMKAIGE STGQTLQQIK LSFHKVGDLG LVAQTSRQNQ
260 270 280 290 300
PTMFKPAALT IPFLFDSLKK IAQMSGNQSQ NRKIGVIKRL LSSCEGAEPK
310 320 330 340 350
YLIRALEGKL RLQLAEKTIL VALANATAQY HADKNGEKLS QQDRIEGEQI
360 370 380 390 400
LRDVYCQLPS YDLIVPHLIE HGLGTLRETC KLTPGIPTKP MLAKPTKQIS
410 420 430 440 450
EVLNTFDQAA FTCEYKYDGE RAQVHFTEDG KFYVFSRNSE NMSVRYPDIS
460 470 480 490 500
VSVSKWKKPD ARSFILDCEA VGWDRDENKI LPFQKLATRK RKDVKIGDIK
510 520 530 540 550
VRACLFAFDI LYLNGQPLLE TPLNERRKLL YSMFQPSTGD FTFAKHSDQK
560 570 580 590 600
SIESIEEFLE ESVKDSCEGL MVKMLEGPDS HYEPSKRSRH WLKVKKDYLS
610 620 630 640 650
GVGDSLDLIV IGAYYGKGKR TSVYGAFLLG CYDPDTETVQ SICKLGTGFS
660 670 680 690 700
EEHLETFYNQ LKDIVISKKK DFYAHSDVPA HQPDVWFEPK YLWEVLAADL
710 720 730 740 750
SLSPVYKAAI GYVQEDKGIS LRFPRFIRIR EDKSWEDATT SEQVSEFYRS
760
QVAYSQKEKE GSPAAEDY
Length:768
Mass (Da):86,581
Last modified:October 1, 1989 - v1
Checksum:i6783FF3DDC675F31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05107 Genomic DNA. Translation: CAA28754.1.
CU329670 Genomic DNA. Translation: CAB08176.1.
PIRiA29066.
RefSeqiNP_593318.2. NM_001018749.2.

Genome annotation databases

EnsemblFungiiSPAC20G8.01.1; SPAC20G8.01.1:pep; SPAC20G8.01.
GeneIDi2541849.
KEGGispo:SPAC20G8.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05107 Genomic DNA. Translation: CAA28754.1.
CU329670 Genomic DNA. Translation: CAB08176.1.
PIRiA29066.
RefSeqiNP_593318.2. NM_001018749.2.

3D structure databases

ProteinModelPortaliP12000.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278340. 14 interactions.
MINTiMINT-4687250.

Proteomic databases

MaxQBiP12000.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC20G8.01.1; SPAC20G8.01.1:pep; SPAC20G8.01.
GeneIDi2541849.
KEGGispo:SPAC20G8.01.

Organism-specific databases

EuPathDBiFungiDB:SPAC20G8.01.
PomBaseiSPAC20G8.01. cdc17.

Phylogenomic databases

HOGENOMiHOG000036006.
InParanoidiP12000.
KOiK10747.
OMAiSQCPNYD.
OrthoDBiEOG7TXKRG.
PhylomeDBiP12000.

Enzyme and pathway databases

ReactomeiR-SPO-174414. Processive synthesis on the C-strand of the telomere.
R-SPO-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-SPO-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-SPO-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-69183. Processive synthesis on the lagging strand.

Miscellaneous databases

PROiP12000.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR000977. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterisation of the DNA ligase gene, CDC17, from the fission yeast Schizosaccharomyces pombe."
    Barker D.G., White J.H.M., Johnston L.H.
    Eur. J. Biochem. 162:659-667(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiDNLI1_SCHPO
AccessioniPrimary (citable) accession number: P12000
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.