ID D9TQN3_THETC Unreviewed; 659 AA.
AC D9TQN3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 23.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=Tthe_2090;
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM
OS 571 / NCIB 9385 / NCA 3814) (Clostridium thermosaccharolyticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis;
OC Thermoanaerobacterium.
OX NCBI_TaxID=580327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-2010) 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; CP002171; ADL69569.1; -; Genomic_DNA.
DR RefSeq; YP_003852653.1; NC_014410.1.
DR ProteinModelPortal; D9TQN3; -.
DR EnsemblBacteria; ADL69569; ADL69569; Tthe_2090.
DR GeneID; 9707673; -.
DR KEGG; ttm:Tthe_2090; -.
DR PATRIC; 42453590; VBITheThe89703_2120.
DR HOGENOM; HOG000218458; -.
DR KO; K01972; -.
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: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; 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 DOMAIN 581 659 BRCT (By similarity).
FT NP_BIND 31 35 NAD (By similarity).
FT NP_BIND 80 81 NAD (By similarity).
FT ACT_SITE 111 111 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 400 400 Zinc (By similarity).
FT METAL 403 403 Zinc (By similarity).
FT METAL 418 418 Zinc (By similarity).
FT METAL 423 423 Zinc (By similarity).
FT BINDING 109 109 NAD (By similarity).
FT BINDING 132 132 NAD (By similarity).
FT BINDING 166 166 NAD (By similarity).
FT BINDING 282 282 NAD (By similarity).
FT BINDING 306 306 NAD (By similarity).
SQ SEQUENCE 659 AA; 74112 MW; F088E28CFCD73342 CRC64;
MTIEERIKEL KDKLNHHNYM YYVLDRPEIS DYEYDMMMRE LIKLEEEHPE FKTPDSPTQR
VGGEPVKEFE PFTHVVVMQS LANAFSEGEL RDFDRRVRSS VGDVEYVVEL KIDGLSVELI
YENGIFTIGS TRGDGFVGEN VTNNLKTIKS IPLRLKDNLN LIVRGEVFMP RASFEKLNEE
RELNGESLFA NPRNAAAGSL RQLNPKITAK RDLDIFVFNL QRIEGVELKT HVEALEFLKE
QGFKVSPHLK KCKNIDEVIE DINYIRTIRD SLPYDTDGAV VKVNDLEKRE ILGSTVKDPR
WAIAFKYPAE RQKTKVKDII VQVGRTGALT PTAILEPVKI AGSIVSRATL HNEDYIKEKD
IRIGDTVIIQ KAGEIIPEVV SVVVEDRKGH EKNFFMPDTC PECGATTVRL PGEAVTRCTG
LNCPAKLKRG IIHFASKDAM DIDGLGPAVI GQLLDNHLIH NIADLYYLKY DDLIKLDRMG
DKSVKNLLNA IEESKGRDLD RVIFGLGIDL IGSKAASILA NHFKTMDSLE EASFDELTNI
EEVGPKMADS IIAFFKEKQN KEILDKLKEA GVNMVKKKSE NTSNIFDGLT FVLTGTLSNY
TRDEAKKLIE ERGGKVTGSV SKKTNYVVAG TDPGSKLSKA QQLGVKVIDE EEFENMLKQ
//
