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Entry: G2ZBE2_LISIP
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ID   G2ZBE2_LISIP            Unreviewed;       671 AA.
AC   G2ZBE2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   11-JUN-2014, entry version 22.
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: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; 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   NP_BIND      31     35       NAD (By similarity){EA3}.
FT   NP_BIND      80     81       NAD (By similarity){EA3}.
FT   ACT_SITE    112    112       N6-AMP-lysine intermediate (By
FT                                similarity){EA3}.
FT   METAL       401    401       Zinc (By similarity){EA3}.
FT   METAL       404    404       Zinc (By similarity){EA3}.
FT   METAL       419    419       Zinc (By similarity){EA3}.
FT   METAL       424    424       Zinc (By similarity){EA3}.
FT   BINDING     110    110       NAD (By similarity){EA3}.
FT   BINDING     133    133       NAD (By similarity){EA3}.
FT   BINDING     167    167       NAD (By similarity){EA3}.
FT   BINDING     283    283       NAD (By similarity){EA3}.
FT   BINDING     307    307       NAD (By similarity){EA3}.
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
//
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