ID   LIGB_CHRSD              Reviewed;         629 AA.
AC   Q1QXD7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA ligase B {ECO:0000255|HAMAP-Rule:MF_01587};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01587};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000255|HAMAP-Rule:MF_01587};
GN   Name=ligB {ECO:0000255|HAMAP-Rule:MF_01587}; OrderedLocusNames=Csal_1518;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
CC   -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC       5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC       as a coenzyme and as the energy source for the reaction.
CC       {ECO:0000255|HAMAP-Rule:MF_01587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01587};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01587}.
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DR   EMBL; CP000285; ABE58871.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1QXD7; -.
DR   SMR; Q1QXD7; -.
DR   STRING; 290398.Csal_1518; -.
DR   EnsemblBacteria; ABE58871; ABE58871; Csal_1518.
DR   KEGG; csa:Csal_1518; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   Proteomes; UP000000239; Chromosome.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_01587; DNA_ligase_B; 1.
DR   InterPro; IPR020923; DNA_ligase_B.
DR   InterPro; IPR001679; DNAligase.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Ligase; NAD; Reference proteome.
FT   CHAIN           1..629
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000313533"
FT   REGION          588..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   629 AA;  69898 MW;  661062942FF9B7FD CRC64;
     MSRRPVWIDG SDMRPAPLRT AAWLRACLLV GLSTLAMPGW ASAPPCPQMT PEAMQNDYQA
     LDARIARWDR AYYRQGQRLV DDGTYDSAKR RLAHWAECFP LLAKPSVNTH EPTGAKHHPV
     AQTGIAKLPD RDAVAGWVAR QGDHPLWVQP KVDGVAVTLV YRHGRLAAAI SRGDGVSGQD
     WYTKALHIAA IPSHLPADAP PLVILQGELY ARRTAHRQSR DGTDGARARI AGLMARDTLT
     DREGSTIGLF VWAWPNGPDT MPERLETLAG WGFGDVAEMT HGVATAEDIA AWRQRWYRHA
     LPFATDGVVV KRGDRPPGSD WQASPPDWAM AWKYPAREAL ARVDALEFSV GRTGRIAVVA
     ELEPVLLGDK RVTRVSLGSL AHWRRTDVRP GDQVRLRLAG LTIPQLQEVV VRTRPRPQVD
     APEADQYDRL SCLRFTPACR DQFLARLEWL GSDEGLDFPG IGPATWNQLV DAGLVKGLLD
     WRTLDTAALE ALPGVGKKTA RAWQRHFALA DTRSAVRWLR ALGVPAVPRQ ALTDALERYG
     MAGLGTLAPP DWRDYSGIGE TRAMQLTRFF RDTDIRHWLA SLESTRALQK QHGTNTRNEQ
     KGDVRRVDVK QDNGTTWLPE QDSNLRPND