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Database: UniProt
Entry: Q98QH2
LinkDB: Q98QH2
Original site: Q98QH2 
ID   DNLJ_MYCPU              Reviewed;         679 AA.
AC   Q98QH2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   14-MAY-2014, entry version 82.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.2;
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN   Name=ligA; OrderedLocusNames=MYPU_3890;
OS   Mycoplasma pulmonis (strain UAB CTIP).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C.,
RA   Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen
RT   Mycoplasma pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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; AL445564; CAC13562.1; -; Genomic_DNA.
DR   PIR; E90560; E90560.
DR   RefSeq; NP_326220.1; NC_002771.1.
DR   ProteinModelPortal; Q98QH2; -.
DR   STRING; 272635.MYPU_3890; -.
DR   EnsemblBacteria; CAC13562; CAC13562; CAC13562.
DR   GeneID; 911331; -.
DR   KEGG; mpu:MYPU_3890; -.
DR   PATRIC; 20023688; VBIMycPul29704_0391.
DR   GenoList; MYPU_3890; -.
DR   eggNOG; COG0272; -.
DR   HOGENOM; HOG000218458; -.
DR   KO; K01972; -.
DR   OMA; KEYYVDS; -.
DR   OrthoDB; EOG6TTVM9; -.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
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.
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    679       DNA ligase.
FT                                /FTId=PRO_0000313327.
FT   DOMAIN      603    679       BRCT.
FT   NP_BIND      36     40       NAD (By similarity).
FT   NP_BIND      94     95       NAD (By similarity).
FT   ACT_SITE    126    126       N6-AMP-lysine intermediate (By
FT                                similarity).
FT   METAL       415    415       Zinc (By similarity).
FT   METAL       418    418       Zinc (By similarity).
FT   METAL       433    433       Zinc (By similarity).
FT   METAL       438    438       Zinc (By similarity).
FT   BINDING     147    147       NAD (By similarity).
FT   BINDING     181    181       NAD (By similarity).
FT   BINDING     299    299       NAD (By similarity).
FT   BINDING     323    323       NAD (By similarity).
SQ   SEQUENCE   679 AA;  79499 MW;  8A5B8CA964476DAC CRC64;
     MSLSKSKVKS KIKELNEKLK LYNHHYYNKN ESLVSDEYYD AKLLELENIR DNFPEEYNQV
     FQKDFSKSVL EKVNHLDEQD VKLKKEKHQK LMLSLNKAYS FEDLERYTNR INTFVGNNHQ
     YILQEKIDGV SISLYYENGI LTKALTRGDG IYGENVTHNA LNIKDIPKTI NIKENIELRG
     EIFFSLKLFE SLKNEFLDKQ DGTKNKKWNT PRNKASGILK SLKTTDESSW LSCFIYEVVS
     PENFNLKTQK QLFDFLKIQG FNLPKFEFIE NENLIENFIT NFKFEDDQRD YEIDGLVIKL
     NDLSLYDLLG KTSKFFHHSI AYKFRKKFVM TKIEDIFVTV GRTGLITYNA KLQEVVLNGS
     KIKAATLHNY EYIKNIKINI GDKVYIEKAG EIIPRVVKLV SPKNDQNYFS PIEFCPSCKN
     KLSWSENMLN QFCLNPDCIE KKIQKLKYFV SKDGMEIQEL GGKKIELFFA KGWVKKIEDI
     YNLKNNYDDL LKLENFQEHS VNVLLHKIEE SKDVYTWKLI AALGIKNIGK KLAKSLVKII
     FENDQKNLLS LLEFNYDELE KYDEFGSVKI ESLKEFFAND ENRNLIQFLD QNGFELKMEK
     EIIQSTKLEN KTFLITGTLE KPRDFYKNLI IQNGGIISSS ISKKLDYLIV GQNPGSKEKK
     AMELNIKIID EEFLKKMLE
//
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