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 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=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; YITKENF; -.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR010994; RuvA_2-like.
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 PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 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; FALSE_NEG.
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
//
