ID A0A1I7CFR2_9GAMM Unreviewed; 569 AA.
AC A0A1I7CFR2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN04487956_1432 {ECO:0000313|EMBL:SFT98233.1};
OS Halomonas saccharevitans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=416872 {ECO:0000313|EMBL:SFT98233.1, ECO:0000313|Proteomes:UP000199594};
RN [1] {ECO:0000313|EMBL:SFT98233.1, ECO:0000313|Proteomes:UP000199594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6493 {ECO:0000313|EMBL:SFT98233.1,
RC ECO:0000313|Proteomes:UP000199594};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FPAQ01000043; SFT98233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7CFR2; -.
DR OrthoDB; 9759736at2; -.
DR Proteomes; UP000199594; 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; IPR020923; DNA_ligase_B.
DR InterPro; IPR033136; DNA_ligase_CS.
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 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.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..569
FT /note="DNA ligase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011757210"
FT DOMAIN 41..439
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 569 AA; 61797 MW; 2929F95D238D2612 CRC64;
MASRVSAGLL VFSLALSLAL PLLLTSLPAR AATCPGGAEA PSESELNALA RRLAEWDDAY
YRRGESPVSD ALYDQARRQF EAWRRCFPAR APEASMPNHL EGEASHPIYQ TGLAKLEDAA
TVRRWLARRN DVWLQPKVDG VAVTLVYRDG RLVRAISRGD GRHGQDWTAA ARRLPAVPAR
LPEAVDALLQ GELYRRLEDH VQAESGGVGA RSEVAGWLAR EVLSSEAAAR VGLFVWDWPD
GPPAMRERLA GLARLGFAES AALTHPVATL EKVERFRERW YRGPLPFATD GVVLRQGRRP
AGEGWQAEPP DWAAAWKHPP REALAEVRGV EFRIGRTGRI TPLLHLMPVA LDGRVIRRVS
AGSLDRWREL DIRPGDRVAI VLAGLTIPRL DGVVWRAATR PALSPPAAAD YHALSCLRLT
PGCEAQFLER LAWLGGPEGL DLPGVGPGTW AALVDAGLIG DLLDWRALGA PALRRAHGIG
EKRAAALVAA FTGTHASPFS RWLEALGAPP GVEAALPADW TTLSERSRRD WRALPGVGPD
RAAALVDFFA HPEVRALARR LGEAGTDGF
//
