ID DNLJ_WOLPM Reviewed; 662 AA.
AC Q73H01;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 29-MAY-2013, entry version 72.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=WD_0776;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T.,
RA Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N.,
RA Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA Durkin A.S., Kolonay J.F., Nelson W.C., Mohamoud Y., Lee P.,
RA Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C.,
RA Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel:
RT a streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
CC -!- FUNCTION: DNA ligase that catalyzes the formation of
CC phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl
CC groups in double-stranded DNA using NAD as a coenzyme and as the
CC energy source for the reaction. It is essential for DNA
CC replication and repair of damaged DNA (By similarity).
CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
CC (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-
CC ribonucleotide + (deoxyribonucleotide)(n+m).
CC -!- COFACTOR: Magnesium or manganese (By similarity).
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily.
CC -!- SIMILARITY: Contains 1 BRCT domain.
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DR EMBL; AE017196; AAS14465.1; -; Genomic_DNA.
DR RefSeq; NP_966531.1; NC_002978.6.
DR ProteinModelPortal; Q73H01; -.
DR STRING; 163164.WD0776; -.
DR EnsemblBacteria; AAS14465; AAS14465; WD_0776.
DR GeneID; 2737976; -.
DR KEGG; wol:WD0776; -.
DR PATRIC; 24030145; VBIWolEnd21207_0774.
DR eggNOG; COG0272; -.
DR HOGENOM; HOG000218458; -.
DR KO; K01972; -.
DR OMA; YITKENF; -.
DR ProtClustDB; CLSK739957; -.
DR BioCyc; WEND163164:GJ8W-761-MONOMER; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:EC.
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 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; IPR018239; DNA_ligase_AS.
DR InterPro; IPR004150; DNA_ligase_OB.
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; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR PANTHER; PTHR11107:SF5; PTHR11107:SF5; 1.
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 PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00278; HhH1; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF52113; BRCT; 1.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF47781; RuvA_2_like; 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 Complete proteome; DNA damage; DNA repair; DNA replication; Ligase;
KW Magnesium; Manganese; Metal-binding; NAD; Zinc.
FT CHAIN 1 662 DNA ligase.
FT /FTId=PRO_0000313511.
FT DOMAIN 580 662 BRCT.
FT NP_BIND 32 36 NAD (By similarity).
FT NP_BIND 75 76 NAD (By similarity).
FT ACT_SITE 108 108 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 389 389 Zinc (By similarity).
FT METAL 392 392 Zinc (By similarity).
FT METAL 407 407 Zinc (By similarity).
FT METAL 413 413 Zinc (By similarity).
FT BINDING 106 106 NAD (By similarity).
FT BINDING 129 129 NAD (By similarity).
FT BINDING 164 164 NAD (By similarity).
FT BINDING 271 271 NAD (By similarity).
FT BINDING 295 295 NAD (By similarity).
SQ SEQUENCE 662 AA; 74348 MW; EFBFF7CEB82D9F5C CRC64;
MTNLEKMREK LQDQINYHNV LYHQKNKPEI SDAEYDELKK KLAEIEPEIY ATQDSVGAPP
DERFSKVEHQ EPMLSLENAY DEQGVEKFLS KIKRFLIEDK IEILCEPKID GLSFSAIYED
GRFVKAATRG DGFVGEDVTH NVATIKGFPK FLQGVQGRLE VRGEIYISNS DFLKLNENDE
FANPRNAAAG SLKQLDANIT ASRPLRYFAY SLIGGAEKSQ SEVLNKLEAL GFCVNEHQSL
TSSLDGMLKF YNEVYNCRYN LDYDIDGIVY KVNDLVLQNR LGNTHKAPRS ALAYKFSAVY
AKTKLNKIFI QVGRTGVLTP VADLVPVNVG GVLVSRASLH NQDEIKRKDI REGDIVTIKR
AGDVIPQIVE VSRDSRLPNT PEFVFPEVCP ECGSKVRQVE GEAAVRCPEE FACKAQMIEK
LKHFVSKDAF DIVGLGDKQI EFFYDLGLIK QIHDIFTLEE RLDEFNLEEQ SGWGEKSIAN
LLNSIQSRRV ITLDRFIFSL GIRFIGQVAA ELLADYYVSY NNWYNSMIEL SLDNTELVGI
DGIGKKGAES LESFFSKEHN IKMLNDLTAC LQILPVSSNS SNSVLNNKII VFTGKLLAMS
RGEAKVRAKT LGAKVSSHLS AKTDYLIAGE KPGSKYKKAV ELGVEILDED QWHKVISLGV
FK
//
