ID DNLJ_MYCSS Reviewed; 701 AA.
AC Q1BAU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 01-MAY-2013, entry version 56.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=Mmcs_1881;
OS Mycobacterium sp. (strain MCS).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=164756;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000384; ABG07990.1; -; Genomic_DNA.
DR RefSeq; YP_639046.1; NC_008146.1.
DR ProteinModelPortal; Q1BAU4; -.
DR SMR; Q1BAU4; 17-337, 619-698.
DR STRING; 164756.Mmcs_1881; -.
DR EnsemblBacteria; ABG07990; ABG07990; Mmcs_1881.
DR GeneID; 4110715; -.
DR KEGG; mmc:Mmcs_1881; -.
DR PATRIC; 18113935; VBIMycSp106721_1923.
DR eggNOG; COG0272; -.
DR HOGENOM; HOG000218459; -.
DR KO; K01972; -.
DR OMA; ENVRTIR; -.
DR ProtClustDB; PRK07956; -.
DR BioCyc; MSP164756:GHQ8-2167-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 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:SF8; PTHR11107:SF8; 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; 2.
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; 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 1 701 DNA ligase.
FT /FTId=PRO_0000313315.
FT DOMAIN 616 701 BRCT.
FT NP_BIND 50 54 NAD (By similarity).
FT NP_BIND 100 101 NAD (By similarity).
FT ACT_SITE 132 132 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 427 427 Zinc (By similarity).
FT METAL 430 430 Zinc (By similarity).
FT METAL 446 446 Zinc (By similarity).
FT METAL 452 452 Zinc (By similarity).
FT BINDING 130 130 NAD (By similarity).
FT BINDING 153 153 NAD (By similarity).
FT BINDING 193 193 NAD (By similarity).
FT BINDING 309 309 NAD (By similarity).
FT BINDING 333 333 NAD (By similarity).
SQ SEQUENCE 701 AA; 75899 MW; FC4714A2EEB824E5 CRC64;
MSAKSTPDAG PQEQATEAEA ELRHRWQALA DEVRDHQFRY YVRDAPVISD ADFDKLFQQL
EALEAEHPEL RAPDSPTQLV GGAGFATDFT PAEHLERMLS LDDVFNVDEL TAWSSRVRAE
VGDDAAYLCE LKVDGLALAL VYRDGRLERA ATRGDGRVGE DVTLNARTLD DVPERLTPSD
EFPHPAVLEV RGEVFFRVAD FEALNAGLVA EGKPPFANPR NSAAGSLRQK NPAVTARRPL
RMVCHGIGYT EGFSPTSLHE AYGALRAWGL PVSDHTTRVQ GMDAVRERIA YWGEHRHDIE
HEIDGVVVKL DQIALQRRLG ATSRAPRWAV AYKYPPEEAQ TKLLDIRVNV GRTGRVTPFA
YMEPVKVAGS TVGLATLHNA SEVKRKGVLI GDTVVIRKAG DVIPEVLGPV VDLRDGTERE
FVMPTHCPEC GTELAPAKEG DADIRCPNSR TCPAQLRERV FHVAGRGAFD IEGLGYEAAI
ALLQAGVITD EGDLFTLTED DLLRTELFTT KGGAVSANGR RLLANLGKAK AQPLWRVLVA
LSIRHVGPTA ARALATEFGS LDAIIEASED QLAAVEGVGP TIAAAVKEWF TVDWHCAIVE
KWRAAGVRMA DERDASIART LEGLSIVVTG SLAGFSRDEA KEAIIARGGK AAGSVSKKTA
YVVAGDSPGS KYDKAIDLGV PVLDEDGFRN LLENGPQAPE G
//
