DNLJ_CYTH3
ID DNLJ_CYTH3 Reviewed; 670 AA.
AC Q11VI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=CHU_1313;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG58585.1; -; Genomic_DNA.
DR RefSeq; WP_011584700.1; NZ_FPJX01000009.1.
DR AlphaFoldDB; Q11VI1; -.
DR SMR; Q11VI1; -.
DR STRING; 269798.CHU_1313; -.
DR PRIDE; Q11VI1; -.
DR EnsemblBacteria; ABG58585; ABG58585; CHU_1313.
DR KEGG; chu:CHU_1313; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_10; -.
DR OMA; HDVEHEI; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000001822; 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; 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; 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..670
FT /note="DNA ligase"
FT /id="PRO_0000313210"
FT DOMAIN 591..670
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT ACT_SITE 115
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 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ SEQUENCE 670 AA; 74931 MW; BF28A362B0ADB894 CRC64;
MNDAQALARI EELNKVLHYH NNLYYQKDTT EISDFEFDTL LQELIELEKQ FPLYLKADSP
SQRVGGTVTK EFASISHKYP MLSLSNTYSE EEIREFDERV QKAVGHAVEY VCEMKFDGVA
ISITYKNGMI AQAVTRGDGV RGDDVTNNIK TIKSIPLKIQ SATFPEEFEV RGEVYLPYEM
FERINQERED IGEAALANPR NAASGTVKMQ DSGIVAKRAL DCFIYSLLQD SNKQPTHAAA
LAQLKEWGFR VSDSYKVCKN VDEIIQYINH WSEERFKLPL ATDGIVIKVN DLRLQSELGM
TAKSPRWAIA YKFKAEEAST PILSVEYQVG RTGAVTPVAN LAPVHLAGTT VKRATLHNAN
EMERLNLHIG DTVFVEKGGE IIPKITRVDV SKRIAGSQMI PFIQNCPVCD TKLIRIEGEA
AWYCPNDKGC APQITGKIEH FIQRKAMNID GIGSETIELL YQKKLIRNVA DLYTLTYDQL
IQLDRFGEKS VTNVLNGIEA SKQTPFKSVL FAIGIRYVGS TVAEKLALHF KSINALEKAS
IEELLQAPEI GIKIAQSIIE WFSVDTNVQL IEDLKKAGVK LELSEHEILK PESDKFAGKS
FVISGVFENY ERDELKDLIL KNGGKISSGI TGKLNYLVAG ENMGPAKLEK AQKLNITILS
EAEFISLLNS
