ID   H6RLM3_BLASD            Unreviewed;       515 AA.
AC   H6RLM3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   04-NOV-2026, entry version 68.
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=ligB2 {ECO:0000313|EMBL:CCG03749.1};
GN   Synonyms=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=BLASA_2878 {ECO:0000313|EMBL:CCG03749.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03749.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG03749.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG03749.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC       replication, DNA recombination and DNA repair.
CC       {ECO:0000256|ARBA:ARBA00054532, ECO:0000256|HAMAP-Rule:MF_00407}.
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:0000256|ARBA:ARBA00034003,
CC         ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|PROSITE-
CC         ProRule:PRU10135, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO117623; CCG03749.1; -; Genomic_DNA.
DR   RefSeq; WP_014376632.1; NC_016943.1.
DR   AlphaFoldDB; H6RLM3; -.
DR   STRING; 1146883.BLASA_2878; -.
DR   KEGG; bsd:BLASA_2878; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_1_11; -.
DR   OMA; AAGHNNP; -.
DR   OrthoDB; 3733803at2; -.
DR   Proteomes; UP000007517; 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:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1.
DR   FunFam; 2.40.50.140:FF:000163; Probable DNA ligase; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR050191; ATP-dep_DNA_ligase.
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   NCBIfam; TIGR00574; dnl1; 1.
DR   NCBIfam; NF002868; PRK03180.1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
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; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00407};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00407}; Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT   DOMAIN          300..418
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   ACT_SITE        212
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407,
FT                   ECO:0000256|PROSITE-ProRule:PRU10135"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
SQ   SEQUENCE   515 AA;  54233 MW;  1FBED4B2B38F3F32 CRC64;
     MLLAEVVAAS TAVAAARGRK AKAGLIAGAL RLADGDEVPA VTAWLSGEPL QRRLGIGWRS
     LAALTGGAAA ESTLTVADVD AAFAELATTS GPGSAARREE LLRGVLSRAT SEEQRFLVRL
     ITGELRQGAL EGVVLEAVAT ASGVPAADVR RAFMLSGSLP DTATAALRGG AEALSAISLQ
     VGRPVRPMLA GPGSSLDAAL ADLGPDVTVE FKLDGARVQV HRDGNQVRVW TRTLREVTDG
     VPELVERVRA LPCRTAVLDG ETLALDDDGR PRAFQDTMSR FGSAGAGGEM PDAGVLLSPF
     FFDLLHLDGR DLLDEPLDIR LDALAGLLAD DASAPLRMPG VRRPRPGQAA QVLEHALDAG
     HEGVVVKDLA APYAAGRRGK AWQKVKPVHT LDLVVLGAEW GYGRRTGTLS NIHLGARDPD
     GGEPVMVGKT FKGMTDELLA WQTRTFPEHT REETPWGVLL EPALVVEIAV DGAQRSPRYP
     GGVALRFARV LRYRPDKTPA EADTLEAVRA LLAGG
//