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 03-AUG-2022, entry version 126.
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; Schizosaccharomycetaceae;
OC 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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 fission
RT 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}.
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DR EMBL; CU329671; CAC22607.1; -; Genomic_DNA.
DR RefSeq; NP_595345.1; NM_001021253.2.
DR AlphaFoldDB; 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 PomBase; SPBC713.06; adl1.
DR VEuPathDB; FungiDB:SPBC713.06; -.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_1_1_1; -.
DR InParanoid; Q9C1W9; -.
DR OMA; RDFSCEY; -.
DR PhylomeDB; Q9C1W9; -.
DR PRO; PR:Q9C1W9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070421; C:DNA ligase III-XRCC1 complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
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:0006288; P:base-excision repair, DNA ligation; IBA:GO_Central.
DR GO; GO:0071897; P:DNA biosynthetic process; IC:PomBase.
DR GO; GO:0006266; P:DNA ligation; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0043504; P:mitochondrial DNA repair; IBA:GO_Central.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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; DNA replication; Ligase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..774
FT /note="DNA ligase 3"
FT /id="PRO_0000372334"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /note="N6-AMP-lysine intermediate"
FT /evidence="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
