DNLJ_LARHH
ID DNLJ_LARHH Reviewed; 692 AA.
AC C1D4R5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=LHK_02877;
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Laribacter.
OX NCBI_TaxID=557598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9;
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA. {ECO:0000255|HAMAP-Rule:MF_01588}.
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_01588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
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DR EMBL; CP001154; ACO75856.1; -; Genomic_DNA.
DR RefSeq; WP_012698319.1; NC_012559.1.
DR AlphaFoldDB; C1D4R5; -.
DR SMR; C1D4R5; -.
DR STRING; 557598.LHK_02877; -.
DR PRIDE; C1D4R5; -.
DR EnsemblBacteria; ACO75856; ACO75856; LHK_02877.
DR KEGG; lhk:LHK_02877; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_4; -.
DR OMA; HDVEHEI; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR001679; DNAligase.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00278; HhH1; 4.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00575; dnlj; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..692
FT /note="DNA ligase"
FT /id="PRO_0000380406"
FT DOMAIN 612..692
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT ACT_SITE 126
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 34..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 83..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 334
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ SEQUENCE 692 AA; 73986 MW; E741629FBDAD083A CRC64;
MTDLNPTARA AGLRALLHRY NHEYYVLDAP SVPDAEYDRL FRELEALEAA HPELASADSP
TRRVGGAPLA AFASVTHRLP MLSLNNVFSD MQDSDPAGRH AELAAFDQRV RDGLGLDEVE
YAVEPKFDGL AVSLVYEHGV LVQGATRGDG ETGENVTENL RTVRSIPLRL ENAPGDDLFA
PAVVPARLEV RGEVLMLKRD FERLNSEQDA AGLKRFANPR NAAAGSLRQL DSRITASRRL
TFFAYAVAEA DGVSLPATHS ATMDWLAGLG LPVSRQRSVV RGLAGLTGAY EAMLAQRAGL
PFDIDGVVYK VNRLSEQARL GFVSRAPRFA VAHKFPAEEA LTVVEDITVQ VGRTGAITPV
ARLQPVFVGG VTVTNATLHN EDEVRRKDVH VGDTVIVRRA GDVIPEVVSV LAERRPPQAR
AFEMPLVCPV CGSHIVREAD EAVARCSGGL YCSAQHKQAL QHFASRKALD VEGLGEKLVD
QLVDAGLVHT PADLFALDQP ALARLERMGD KSAENLVRAL DACRHTTLAR FVYALGIRNV
GEATARDLAR HFGTLDALMA ADQDMLMTAP DVGPIVARSI VDFFAEAHNR EVVDALLAAG
VSWPVVETVT SAGVAGVSGK TFVLTGTLPT LGRDDAKARI EAAGGKVTGS VSKKTHYVVA
GEAAGSKLDK AHELGITVLD EAALLALLAG NA
