ID DNLJ_STRP8 Reviewed; 652 AA.
AC Q8P1L1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 29-MAY-2013, entry version 77.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=spyM18_0810;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18
RT group A Streptococcus strains associated with acute rheumatic fever
RT outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL97474.1; -; Genomic_DNA.
DR RefSeq; NP_606975.1; NC_003485.1.
DR ProteinModelPortal; Q8P1L1; -.
DR SMR; Q8P1L1; 1-304.
DR STRING; 186103.spyM18_0810; -.
DR EnsemblBacteria; AAL97474; AAL97474; spyM18_0810.
DR GeneID; 995118; -.
DR KEGG; spm:spyM18_0810; -.
DR PATRIC; 19748242; VBIStrPyo4396_0711.
DR eggNOG; COG0272; -.
DR HOGENOM; HOG000218458; -.
DR KO; K01972; -.
DR OMA; ENVRTIR; -.
DR ProtClustDB; PRK07956; -.
DR BioCyc; SPYO186103:GHJG-694-MONOMER; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:HAMAP.
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; 3.
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 1 652 DNA ligase.
FT /FTId=PRO_0000313460.
FT DOMAIN 577 652 BRCT.
FT NP_BIND 29 33 NAD (By similarity).
FT NP_BIND 78 79 NAD (By similarity).
FT ACT_SITE 109 109 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 395 395 Zinc (By similarity).
FT METAL 398 398 Zinc (By similarity).
FT METAL 413 413 Zinc (By similarity).
FT METAL 418 418 Zinc (By similarity).
FT BINDING 107 107 NAD (By similarity).
FT BINDING 130 130 NAD (By similarity).
FT BINDING 164 164 NAD (By similarity).
FT BINDING 278 278 NAD (By similarity).
FT BINDING 302 302 NAD (By similarity).
SQ SEQUENCE 652 AA; 72394 MW; E89873C9FD66444E CRC64;
MKKRIKELTD LLNRYRYDYY TKDAPSVSDS DYDKLYRELV TLEQSYPEYV LQDSPTQQVG
GTILKGFEKY RHQYPLFSLQ DAFSREELDA FDKRVKAEFP NATYLAELKI DGLSISLSYE
NGFLQVGATR GDGNIGENIT ENIKKIKDIP HQLSEPLTIT VRGEAYMSRQ SFKAINEARQ
ENGETEFANP RNAAAGTLRQ LDTSVVAKRQ LATFLYQEAS PTARNQQNEV LAELADLGFS
VNPYYQLTSS MDEIWDFIKT IEAKRDQLAY DIDGVVIKVN SLAMQEELGF TVKAPRWAIA
YKFPAEEKEA EILSVDWTVG RTGVVTPTAN LTPVQLAGTT VSRATLHNVD YIAEKDIRIG
DTVIVYKAGD IIPAVLNVVM SKRNQQEVML IPKLCPSCGS ELVHFEDEVA LRCINPLCPS
LIQRSLEHFA SRDAMNITGL GPAIVEKLFL AGFVHDVADI YQLTKEDFMQ LDGIKEKSAD
KLLAAIEASK SNSAEKLLFG LGIRHIGSKV SRLILEVYGD ISALLTAKEE EIARIDGLGS
TIAQSLTQYF EQKTAAILVD ELKTAGVNMH YSGQKVNSDA ALFGLTVVLT GKLNQLNRNE
AKDKLEALGA KVTGSVSKKT DLVIAGSDAG SKLEKAKSLG IRIEDEDWLR KL
//
