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UniProtKB/Swiss-Prot entry P12000


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DNLI1_SCHPO
Primary accession number P12000
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    October 14, 2008 (Entry version 68)
Name and origin of the protein
Protein name DNA ligase 1
Synonyms EC 6.5.1.1
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene name
Name: cdc17
ORFNames: SPAC20G8.01, SPAC57A10.13c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3549293 [NCBI, ExPASy, EBI, Israel, Japan]
Barker D.G., White J.H.M., Johnston L.H.;
"Molecular characterisation of the DNA ligase gene, CDC17, from the fission yeast Schizosaccharomyces pombe.";
Eur. J. Biochem. 162:659-667(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05107; CAA28754.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAB08176.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29066; A29066.
RefSeq NP_593318.2; -.
3D structure databases
ModBase P12000.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001954-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC20G8.01; -.
Gene expression databases
ArrayExpress P12000; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from direct assay from GeneDB_SPombe).
GO:0005657; Cellular component: replication fork (inferred by curator from GeneDB_SPombe).
GO:0003910; Molecular function: DNA ligase (ATP) activity (inferred from genetic interaction from GeneDB_SPombe).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from GeneDB_SPombe).
GO:0043137; Biological process: DNA replication, removal of RNA primer (traceable author statement from GeneDB_SPombe).
GO:0000723; Biological process: telomere maintenance (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
IPR012308; DNA_ligase_A_N.
IPR016059; DNA_ligase_CS.
IPR012340; NA-bd_OB-fold.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
Pfam PF04679; DNA_ligase_A_C; 1.
PF01068; DNA_ligase_A_M; 1.
PF04675; DNA_ligase_A_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00574; dnl1; 1.
PROSITE PS00697; DNA_LIGASE_A1; 1.
PS00333; DNA_LIGASE_A2; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P12000.
ProtoNet P12000.
Genome annotation databases
GeneID 2541849; -.
KEGG spo:SPAC20G8.01; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nucleotide-binding; Nucleus.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   768  768     DNA ligase 1. PRO_0000059585
ACT_SITE   416   416        N6-AMP-lysine intermediate (By similarity). 
Sequence information
Length: 768 AA [This is the length of the unprocessed precursor] Molecular weight: 86581 Da [This is the MW of the unprocessed precursor] CRC64: 6783FF3DDC675F31 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRTVFSQIPR FKQVNQYIRM STRQSDISNF FISSASHKSE HVEVSQSSSD SKNVDGRSTS 

        70         80         90        100        110        120 
EKRKVESVKL VDESKHNNHD DTGTQNVERE NNIVSEAKKQ KTLGSSSSSS DAVSSNNDSG 

       130        140        150        160        170        180 
ASTPIPLPIK EPPLESNARN DKLKGHATFA EMVKAFTKIE NTSKRLEIID IMGTYFFGIL 

       190        200        210        220        230        240 
RDHPSDLLAC VYLSINKLGP DYSGLELGIG ESIIMKAIGE STGQTLQQIK LSFHKVGDLG 

       250        260        270        280        290        300 
LVAQTSRQNQ PTMFKPAALT IPFLFDSLKK IAQMSGNQSQ NRKIGVIKRL LSSCEGAEPK 

       310        320        330        340        350        360 
YLIRALEGKL RLQLAEKTIL VALANATAQY HADKNGEKLS QQDRIEGEQI LRDVYCQLPS 

       370        380        390        400        410        420 
YDLIVPHLIE HGLGTLRETC KLTPGIPTKP MLAKPTKQIS EVLNTFDQAA FTCEYKYDGE 

       430        440        450        460        470        480 
RAQVHFTEDG KFYVFSRNSE NMSVRYPDIS VSVSKWKKPD ARSFILDCEA VGWDRDENKI 

       490        500        510        520        530        540 
LPFQKLATRK RKDVKIGDIK VRACLFAFDI LYLNGQPLLE TPLNERRKLL YSMFQPSTGD 

       550        560        570        580        590        600 
FTFAKHSDQK SIESIEEFLE ESVKDSCEGL MVKMLEGPDS HYEPSKRSRH WLKVKKDYLS 

       610        620        630        640        650        660 
GVGDSLDLIV IGAYYGKGKR TSVYGAFLLG CYDPDTETVQ SICKLGTGFS EEHLETFYNQ 

       670        680        690        700        710        720 
LKDIVISKKK DFYAHSDVPA HQPDVWFEPK YLWEVLAADL SLSPVYKAAI GYVQEDKGIS 

       730        740        750        760 
LRFPRFIRIR EDKSWEDATT SEQVSEFYRS QVAYSQKEKE GSPAAEDY 

P12000 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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