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Database: UniProt/TrEMBL
Entry: D6ESF4_STRLI
LinkDB: D6ESF4_STRLI
Original site: D6ESF4_STRLI 
ID   D6ESF4_STRLI            Unreviewed;       512 AA.
AC   D6ESF4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407,
GN   ECO:0000313|EMBL:AIJ17245.1};
GN   ORFNames=SLIV_31785 {ECO:0000313|EMBL:AIJ17245.1};
OS   Streptomyces lividans TK24.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=457428 {ECO:0000313|EMBL:AIJ17245.1, ECO:0000313|Proteomes:UP000028682};
RN   [1] {ECO:0000313|EMBL:AIJ17245.1, ECO:0000313|Proteomes:UP000028682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK24 {ECO:0000313|EMBL:AIJ17245.1,
RC   ECO:0000313|Proteomes:UP000028682};
RG   StrepSynth;
RA   Ruckert C., Fridjonson O.H., Lambert C., van Wezel G.P., Bernaerts K.,
RA   Anne J., Economou A., Kalinowski J.;
RT   "Complete genome sequence of Streptomyces lividans TK24.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP009124; AIJ17245.1; -; Genomic_DNA.
DR   RefSeq; WP_003977629.1; NZ_GG657756.1.
DR   EnsemblBacteria; AIJ17245; AIJ17245; SLIV_31785.
DR   GeneID; 29657820; -.
DR   KEGG; slv:SLIV_31785; -.
DR   PATRIC; fig|457428.16.peg.6512; -.
DR   KO; K10747; -.
DR   Proteomes; UP000028682; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028682};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AIJ17245.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      287    414       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    210    210       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     208    208       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     230    230       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     374    374       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   512 AA;  54712 MW;  29D318C26ECEACCA CRC64;
     MLLARLAQVS REVAATSARS RKTVLLAELF REAEAADVPV VIPYLAGRLP QGRIGVGWKV
     LSRRVPPADA PTLTVRDVDA RLTRVGAVSG AGSQAERTRL VGELMGAATE DEQRFLIGLL
     TGEVRQGALD AAAVEGLAAA TDAPPADVRR AVMLAGSLQT VAEALLADGP SALDRFRLTV
     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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