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Database: UniProt
Entry: Q1BAU4
LinkDB: Q1BAU4
Original site: Q1BAU4 
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   16-APR-2014, entry version 61.
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; FTAKSPR; -.
DR   OrthoDB; EOG6TTVM9; -.
DR   ProtClustDB; PRK07956; -.
DR   BioCyc; MSP164756:GHQ8-1893-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; 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; 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.
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
//
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