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Database: UniProt/SWISS-PROT
Entry: DNLI3_SCHPO
LinkDB: DNLI3_SCHPO
Original site: DNLI3_SCHPO 
ID   DNLI3_SCHPO             Reviewed;         774 AA.
AC   Q9C1W9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   05-DEC-2018, entry version 111.
DE   RecName: Full=DNA ligase 3;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase III;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 3;
GN   Name=adl1; Synonyms=lig3; ORFNames=SPBC713.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10135};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; CU329671; CAC22607.1; -; Genomic_DNA.
DR   RefSeq; NP_595345.1; NM_001021253.2.
DR   ProteinModelPortal; Q9C1W9; -.
DR   SMR; Q9C1W9; -.
DR   STRING; 4896.SPBC713.06.1; -.
DR   iPTMnet; Q9C1W9; -.
DR   PaxDb; Q9C1W9; -.
DR   PRIDE; Q9C1W9; -.
DR   EnsemblFungi; SPBC713.06.1; SPBC713.06.1:pep; SPBC713.06.
DR   GeneID; 2541111; -.
DR   KEGG; spo:SPBC713.06; -.
DR   EuPathDB; FungiDB:SPBC713.06; -.
DR   PomBase; SPBC713.06; adl1.
DR   HOGENOM; HOG000036006; -.
DR   InParanoid; Q9C1W9; -.
DR   KO; K10747; -.
DR   OMA; LCQHLRI; -.
DR   OrthoDB; EOG092C0FHN; -.
DR   PhylomeDB; Q9C1W9; -.
DR   PRO; PR:Q9C1W9; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; ISM:PomBase.
DR   GO; GO:0071897; P:DNA biosynthetic process; IC:PomBase.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA replication; Ligase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1    774       DNA ligase 3.
FT                                /FTId=PRO_0000372334.
FT   ACT_SITE    433    433       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
SQ   SEQUENCE   774 AA;  87587 MW;  9D69F9EA510F78FF CRC64;
     MPPKKRMKNG SSLKSTSKKG EKSRNIITIQ DLFSKREAQL TDTPNKLLTD HDQSASDYAY
     ALKLQQLFDS ENQATAPEKL PKDVIIPEEE YHTDTFNVVK ESNDKPKENL VTSEECKASF
     FSTDSVNKDS TIDYDALQKD PLTYVKSCRA RFVSKDTKSF SYSSLANTFS LISSTKSRIR
     IVTLLTNFLL TLLYADPDSL IATVWLCTNS IAPNFYGKNL GVGPAMYSKA LKEVCGITAS
     ALKNLWNKYG DPGDVAFEAK VSVRTLSRPE PLTIKKVYST LLKIADSNGN GAQNRKLELT
     KFLLISSNAE EVRYIGRSIM QNLRIGAVQN TMLASLSKAF FIFDNQNEIF NFNSDSLQQQ
     FRQGEEIVKQ SFFQVPDYNI LVATLLREGI ENLKDNMSIR PGIPVKPMLG SITKNLQHML
     ERLTDHNFSC EFKYDGQRAQ IHCDRLGNIK IFSRHLEEIT GRFPDVIEVA QLALKHSCDF
     IIEGELVAID KSNGQILDFQ KLSTRERKKV TVADITIDVC VFVFDIMFCD GKSCLQMPLI
     ERRRMFFEHF NLIPNRFQFV SSLETNEEQS IQEFFSLAIT NKCEGLMVKV LNGTNSKFPS
     TYEPDKRGEG WIKVKQDYDD EFESLDLVPI GAWYGNGRKA GWFSPILLAV YNPDTGAYEA
     VCKCMSGFSD QFYKELTQKY SLESGNSSLK PIYNFCETGK VTPQIYFAPQ EVWEIKGAQI
     TSSPAYKAAL GLIQDDRGLS IRFPRFIRVR SDKGPEDAST NSILADMYMK QLNT
//
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