ID S2L7H6_HALAF Unreviewed; 575 AA.
AC S2L7H6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA ligase B {ECO:0000256|HAMAP-Rule:MF_01587};
DE EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01587};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000256|HAMAP-Rule:MF_01587};
GN Name=ligB {ECO:0000256|HAMAP-Rule:MF_01587};
GN ORFNames=L861_00245 {ECO:0000313|EMBL:EPC03759.1};
OS Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1121939 {ECO:0000313|EMBL:EPC03759.1, ECO:0000313|Proteomes:UP000014463};
RN [1] {ECO:0000313|EMBL:EPC03759.1, ECO:0000313|Proteomes:UP000014463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35
RC {ECO:0000313|Proteomes:UP000014463};
RX PubMed=23868129; DOI=10.1128/genomeA.00497-13;
RA Tahrioui A., Quesada E., Llamas I.;
RT "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT Halomonas anticariensis FP35.";
RL Genome Announc. 1:31-31(2013).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00034005, ECO:0000256|HAMAP-
CC Rule:MF_01587};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01587}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPC03759.1}.
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DR EMBL; ASTJ01000011; EPC03759.1; -; Genomic_DNA.
DR AlphaFoldDB; S2L7H6; -.
DR STRING; 1121939.L861_00245; -.
DR PATRIC; fig|1121939.11.peg.34; -.
DR eggNOG; COG0272; Bacteria.
DR Proteomes; UP000014463; Unassembled WGS sequence.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01587; DNA_ligase_B; 1.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR020923; DNA_ligase_B.
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 PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF14520; HHH_5; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01587};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01587};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01587};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01587};
KW Reference proteome {ECO:0000313|Proteomes:UP000014463};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..575
FT /note="DNA ligase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004510381"
FT DOMAIN 40..441
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT ACT_SITE 137
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01587"
SQ SEQUENCE 575 AA; 64837 MW; AFC113B82108FC92 CRC64;
MYRHSFGARR AIHGLWAPLL VCMSLSPVQA DECPDWTPTQ ADQALEALQT QVSEWDDAYY
RRGERLVEDS VYDQARSRLT AWQTCFDVPA TPLARSSSEE TIVHPVAQTG LAKLDEPQAL
ANWVERRLQD GLWVQPKVDG VAVTLVYEDG RLTAAISRGD GHRGQDWLSH AERIVTIPQQ
LPADSPPRVI LQGELYHRRP GHIQAEHGSD GARSAIIGLM ARHELDAVSA NDIGLFVWDW
PSGPKPMQAR LTALESWGFA DSARLTRPVT GMDDVTRWRQ HWYRGQLPFA TDGVVIRQNT
RPEPVDWQPE PPYWAVAWKH PAQRSLAMVR DIDFRIGRTG TITPVLQLHP TRLDDRTIRR
VSLGSLDQWQ EWDVRPGDQI MIRLAGLTIP QLAEVLIRAE PRPELDAPDS DRYHPLSCLR
LTTGCEAQFL ARLAWLSDNE GLDMAGIGEG TWQRLIDAGL IEGLLDWQAL TPTQLEALPG
VGEARATQWH ASFQASRHRS LTRWLKALGM PPVDERILIN ADGYLDLSEL RSRNRHDWRQ
HPGIGTTTAE RLVAFFAEPE IVSLLSRLVR PTTLQ
//
