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Database: UniProt
Entry: Q8P1L1
LinkDB: Q8P1L1
Original site: Q8P1L1 
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   01-OCT-2014, entry version 83.
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};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-
CC       ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
CC   -!- COFACTOR: Magnesium or manganese. {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC   -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
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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; FPAQEQL; -.
DR   OrthoDB; EOG6TTVM9; -.
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:UniProtKB-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; 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   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00278; HhH1; 3.
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   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. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   NP_BIND      29     33       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   NP_BIND      78     79       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   ACT_SITE    109    109       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       395    395       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       398    398       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       413    413       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       418    418       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     107    107       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     130    130       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     164    164       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     278    278       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     302    302       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
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
//
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