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Database: UniProt/SWISS-PROT
Entry: DNLI_STRCO
LinkDB: DNLI_STRCO
Original site: DNLI_STRCO 
ID   DNLI_STRCO              Reviewed;         512 AA.
AC   Q9FCB1;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   07-JUN-2017, entry version 111.
DE   RecName: Full=Probable DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=SCO1202;
GN   ORFNames=2SCG58.02;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; AL939108; CAC01484.1; -; Genomic_DNA.
DR   RefSeq; NP_625491.1; NC_003888.3.
DR   RefSeq; WP_011027650.1; NC_003888.3.
DR   ProteinModelPortal; Q9FCB1; -.
DR   SMR; Q9FCB1; -.
DR   STRING; 100226.SCO1202; -.
DR   EnsemblBacteria; CAC01484; CAC01484; CAC01484.
DR   GeneID; 1096625; -.
DR   KEGG; sco:SCO1202; -.
DR   PATRIC; fig|100226.15.peg.1201; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   InParanoid; Q9FCB1; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   PhylomeDB; Q9FCB1; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 2.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
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; 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; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    512       Probable DNA ligase.
FT                                /FTId=PRO_0000059624.
FT   ACT_SITE    210    210       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     208    208       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     230    230       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     374    374       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   512 AA;  54696 MW;  7A85CA68DC760FF9 CRC64;
     MLLARLAQVS REVAATSARS RKTVLLAELF REAEAADVPV VIPYLAGRLP QGRIGVGWKV
     LSRRVPPADA PTLTVRDVDA RLTRLGAVSG AGSQAERTRL VGELMGAATE DEQRFLIGLL
     TGEVRQGALD AAAVEGLAAA TDAPPADVRR AVMLAGSLQT VAEALLADGP GALDRFRLTV
     GQPVLPMLAH SASSVAEAVG KLGAAAVEEK LDGIRVQVHR DGGTVRIYTR TLDDITDRLP
     EVTEAALALP GERFILDGEA ISLDADGRPR SFQETAGRVG SRTDVATAAR AVPVSAVFFD
     VLSVDGRDLL DLPLTERHAE LARLVPEPLR VRRTLVHGPE DTGAAEEFLA RTLARGHEGV
     VVKGLDAAYS AGRRGASWLK VKPVHTLDLV VLAAEWGHGR RTGKLSNLHL GARTADGSFA
     MLGKTFKGMT DALLTWQTER LKELAVEEHG WGVTVRPELV VEIAYDGLQR STRYPAGVTL
     RFARVVRYRE DKRPEDADTV DTLLAAHPGV AP
//
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