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Protein data for DNLI_SCHPO:

Description:
DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]).

Molecular weight: 86581

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
07-FEB-2006, entry version 51.

Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein DNLI_SCHPO:

DatabasePointerAdd. info#1Add. info#2
EMBLX05107CAA28754.1-
EMBLZ94864CAB08176.1-
EMBLZ95334CAB08595.1-
PIRA29066A29066.
GeneDB_SpombeSPAC20G8.01-.1
BioCycSPOM-XXX-01:SPOM-XXX-01-001954-MONOMER-.1
GOGO:0005739C:mitochondrionIDA.
GOGO:0005634C:nucleusIDA.
GOGO:0003910F:DNA ligase (ATP) activityIGI.
GOGO:0005515F:protein bindingIPI.
GOGO:0043137P:DNA replication, removal of RNA primerTAS.
GOGO:0000723P:telomere maintenanceIMP.
InterProIPR000977DNA_ligase.
InterProIPR012309DNA_ligase_A_C.
InterProIPR012310DNA_ligase_A_M.
InterProIPR012308DNA_ligase_A_N.
PANTHERPTHR10459DNA_ligase.11.
PfamPF04679DNA_ligase_A_C1.
PfamPF01068DNA_ligase_A_M1.
PfamPF04675DNA_ligase_A_N1.
TIGRFAMsTIGR00574dnl11.
PROSITEPS00697DNA_LIGASE_A11.
PROSITEPS00333DNA_LIGASE_A21.
PROSITEPS50160DNA_LIGASE_A31.

General information about the databases mentioned above

Keywords:
ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nuclear protein; Nucleotide-binding.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=87161837; PubMed=3549293;
RA Barker D.G., White J.H.M., Johnston L.H.;
RT "Molecular characterisation of the DNA ligase gene, CDC17, from the
RT fission yeast Schizosaccharomyces pombe.";
RL Eur. J. Biochem. 162:659-667(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).

Feature:
CHAIN 1 768 DNA ligase.
/FTId=PRO_0000059585.
ACT_SITE 416 416 N6-AMP-lysine intermediate (By
similarity).

Comments:
-!- FUNCTION: This protein seals, during DNA replication, DNA
recombination and DNA repair, nicks in double-stranded DNA.
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
(deoxyribonucleotide)(m) = AMP + diphosphate +
(deoxyribonucleotide)(n+m).
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
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Sequence length: 768

     MRTVFSQIPR FKQVNQYIRM STRQSDISNF FISSASHKSE HVEVSQSSSD SKNVDGRSTS
     EKRKVESVKL VDESKHNNHD DTGTQNVERE NNIVSEAKKQ KTLGSSSSSS DAVSSNNDSG
     ASTPIPLPIK EPPLESNARN DKLKGHATFA EMVKAFTKIE NTSKRLEIID IMGTYFFGIL
     RDHPSDLLAC VYLSINKLGP DYSGLELGIG ESIIMKAIGE STGQTLQQIK LSFHKVGDLG
     LVAQTSRQNQ PTMFKPAALT IPFLFDSLKK IAQMSGNQSQ NRKIGVIKRL LSSCEGAEPK
     YLIRALEGKL RLQLAEKTIL VALANATAQY HADKNGEKLS QQDRIEGEQI LRDVYCQLPS
     YDLIVPHLIE HGLGTLRETC KLTPGIPTKP MLAKPTKQIS EVLNTFDQAA FTCEYKYDGE
     RAQVHFTEDG KFYVFSRNSE NMSVRYPDIS VSVSKWKKPD ARSFILDCEA VGWDRDENKI
     LPFQKLATRK RKDVKIGDIK VRACLFAFDI LYLNGQPLLE TPLNERRKLL YSMFQPSTGD
     FTFAKHSDQK SIESIEEFLE ESVKDSCEGL MVKMLEGPDS HYEPSKRSRH WLKVKKDYLS
     GVGDSLDLIV IGAYYGKGKR TSVYGAFLLG CYDPDTETVQ SICKLGTGFS EEHLETFYNQ
     LKDIVISKKK DFYAHSDVPA HQPDVWFEPK YLWEVLAADL SLSPVYKAAI GYVQEDKGIS
     LRFPRFIRIR EDKSWEDATT SEQVSEFYRS QVAYSQKEKE GSPAAEDY

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