ID A0A270PLD6_9PSED Unreviewed; 559 AA.
AC A0A270PLD6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=CES87_02635 {ECO:0000313|EMBL:PAM85393.1};
OS Pseudomonas sp. ERMR1:02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1805930 {ECO:0000313|EMBL:PAM85393.1, ECO:0000313|Proteomes:UP000215719};
RN [1] {ECO:0000313|EMBL:PAM85393.1, ECO:0000313|Proteomes:UP000215719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:02 {ECO:0000313|EMBL:PAM85393.1,
RC ECO:0000313|Proteomes:UP000215719};
RA Kumar R., Acharya V., Singh D., Kumar S.;
RT "Pseudomonas sp. ERMR1:02, Genome sequencing and assembly.";
RL Submitted (JUN-2017) 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}.
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:PAM85393.1}.
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DR EMBL; NKJI01000001; PAM85393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A270PLD6; -.
DR OrthoDB; 9759736at2; -.
DR Proteomes; UP000215719; 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; 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 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.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..559
FT /note="DNA ligase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013261425"
FT DOMAIN 32..429
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT ACT_SITE 127
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01587"
SQ SEQUENCE 559 AA; 62231 MW; 770928874DC1844C CRC64;
MPLTLRLFVT CLLALSYLNA NATQCPDWPP ERASNEVTAL QKQIDTWDDS YHRTGTSLVT
DELYDQSRAR LSQWRQCFNP GIPTDPLRTA RGTMAHPIAH TGLEKLHDKQ AVEHWLRNRT
DVWVQPKVDG VAVTLIYRNG LLNQAISRGD GSHGQDWTAS ARQIAAIPQQ LSQPLDLLVQ
GELYWRLTEH VQAQAGSLNA RAVVAGLMAR KTLNAEQASG IGLFAWDWPQ GPASLPERVA
TLDELGFPVT APYSQPISAL ADAQRWRDHW YRSPLPFASD GIVLRQAQRP LAERWQTKPS
YWSVAWKYPF AQALAQVRKV HFKIGRTGRI TPVLELTPVM LDDRQIKRVS VSSLQRWQAL
DIRPGDQVAI SLAGLTIPRL DGVLLRSTER PELNVPLAAD FHPLSCWQPT PECEGQFLAR
LTWLSGKQGL ALPHVGPGTW EKLLQAGHLN SLLDWLTLDA QELANIDGLG ERSAARLLTS
FDSARQRPFA RWLKALGMPP TGQANLADSW QALAQRDTEQ WQAEAGIGPG RAAQLSAFFR
DPHVLALSET LRDAGIDGF
//
