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Database: UniProt/TrEMBL
Entry: A0A0N6ZSZ6_9ACTN
LinkDB: A0A0N6ZSZ6_9ACTN
Original site: A0A0N6ZSZ6_9ACTN 
ID   A0A0N6ZSZ6_9ACTN        Unreviewed;       512 AA.
AC   A0A0N6ZSZ6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
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=ligB {ECO:0000313|EMBL:AIV37782.1};
GN   Synonyms=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=NI25_33240 {ECO:0000313|EMBL:AIV37782.1};
OS   Streptomyces sp. CCM_MD2014.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1561022 {ECO:0000313|EMBL:AIV37782.1};
RN   [1] {ECO:0000313|Proteomes:UP000069932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM_MD2014 {ECO:0000313|Proteomes:UP000069932};
RA   Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA   Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA   Newman D.K.;
RT   "Isolation and characterization of species affiliated with family
RT   Actinomycetaceae.";
RL   Submitted (OCT-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; CP009754; AIV37782.1; -; Genomic_DNA.
DR   RefSeq; WP_061446026.1; NZ_CP009754.1.
DR   EnsemblBacteria; AIV37782; AIV37782; NI25_33240.
DR   KEGG; strd:NI25_33240; -.
DR   PATRIC; fig|1561022.5.peg.6919; -.
DR   KO; K10747; -.
DR   Proteomes; UP000069932; 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:UP000069932};
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:AIV37782.1};
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;  54441 MW;  50892DA575060BF3 CRC64;
     MLLARLAQVS REVAATSARS RKTALLAELF REAEAADVPV VIPYLAGRLP QGRIGVGWKV
     LSRRVPPADA PTLTVRDVDA RLTRLGAVSG AGSQAERARL VGELMGSATE EEQRFLIGLL
     TGEVRQGALD AAAVEGLAAA TGAPPADVRR AVMLAGSLQT VAEALLADGP GALEGFRLTV
     GRPVLPMLAH SASSVGEAVA KLGTAAVEEK LDGIRVQVHR DGGTVRIYTR TLDDITDRLP
     EVTEAALALP AGRFVLDGEA ISLDASGRPR SFQETAGRVG SRTDVATAAR AVPVSAVFFD
     VLSVDGRDLL DLPLTERHAE LARLVPEPLR VRRTLVRGPE ETGAAEEFLA EALTRGHEGV
     VVKGLDAAYS AGRRGASWLK VKPVHTLDLV VLAAEWGHGR RTGKLSNLHL GARAPDGSFA
     MLGKTFKGMT DALLAWQTER LQELAVEEHG WGVTVRPELV VEIAYDGLQR STRYPAGVTL
     RFARVVRYRE DKRPEDADTV ETLLAAHPGA AP
//
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