ID G2ZBE2_LISIP Unreviewed; 671 AA.
AC G2ZBE2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 29-MAY-2013, entry version 15.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=LIV_1735;
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55;
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M.,
RA Lampidis R., Karst U., Chakraborty T., Cossart P., Kreft J.,
RA Vazquez-Boland J.A., Goebel W., Glaser P.;
RT "Complete Genome Sequence of the Animal Pathogen Listeria ivanovii,
RT Which Provides Insights into Host Specificities and Evolution of the
RT Genus Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
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; FR687253; CBW86222.1; -; Genomic_DNA.
DR RefSeq; YP_004855485.1; NC_016011.1.
DR EnsemblBacteria; CBW86222; CBW86222; LIV_1735.
DR GeneID; 11162382; -.
DR KEGG; liv:LIV_1735; -.
DR KO; K01972; -.
DR BioCyc; LIVA881621:GJTC-2607-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; 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 DOMAIN 587 671 BRCT (By similarity).
FT NP_BIND 31 35 NAD (By similarity).
FT NP_BIND 80 81 NAD (By similarity).
FT ACT_SITE 112 112 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 401 401 Zinc (By similarity).
FT METAL 404 404 Zinc (By similarity).
FT METAL 419 419 Zinc (By similarity).
FT METAL 424 424 Zinc (By similarity).
FT BINDING 110 110 NAD (By similarity).
FT BINDING 133 133 NAD (By similarity).
FT BINDING 167 167 NAD (By similarity).
FT BINDING 283 283 NAD (By similarity).
FT BINDING 307 307 NAD (By similarity).
SQ SEQUENCE 671 AA; 74952 MW; 23C98CA514F30D5F CRC64;
MADKKRYEEL INILDQYSYD YYVIDNPTVE DAEYDQKMQE LLQIEEAHPE WVTPESPSNR
VGGEVLEGFQ KVAHDTPMLS LANAFNKEDL ADFDRRIRDK VGEDIAYMCE LKIDGLAVSL
QYDNGKYKQG ATRGDGTIGE DITANLRTIR SIPMKLQKDY SIEVRGEAFM PKRSFQKLNE
IREEEGQMLF ANPRNAAAGS LRQLDTKIAA SRNLDIFLYA VADFGEMGVT THSDGLDMLE
TLGLKVNKER RLCANLEEVY AYIDEWTEKR AGLAYDIDGI VLKLNDLEQQ RQMGTTAKSP
RWSIAYKFPA EEVPTKLLDI ELNIGRTGVV TPTAVLEPVR VAGTTVSRAS LHNEDLITEK
DIRIGDTVLI KKAGDIIPEV IKSITEERTG DEEPFHMPKN CPTCESELVR LEEEVALRCI
NPKCPAQIKE GLIHFVSRNA MNIDGLGEKV IIQLFTHHLI KDVADLFFLS KEKLLELERM
GEKSVTNLLA SIEQSKQNSL EKLLFGLGIR HVGAKAAKSL AIHFETMDNL KIADKETLTS
INDIGEKMAD SIVTYFANEE VHDLLDELKR ANVNMTYTGP KLEDMSEEEL VFAGKTVVLT
GKLEQLTRND AKALIESLGG NVSGSVSKKT DVVVAGSDAG SKLAKAEELA IPIWSENDLI
EYLPDEGGLD K
//
