ID DNLJ_MARMM Reviewed; 701 AA.
AC Q0AMX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 29-MAY-2013, entry version 54.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=Mmar10_2066;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Hyphomonadaceae; Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-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; CP000449; ABI66358.1; -; Genomic_DNA.
DR RefSeq; YP_757296.1; NC_008347.1.
DR ProteinModelPortal; Q0AMX9; -.
DR STRING; 394221.Mmar10_2066; -.
DR EnsemblBacteria; ABI66358; ABI66358; Mmar10_2066.
DR GeneID; 4284302; -.
DR KEGG; mmr:Mmar10_2066; -.
DR PATRIC; 22452300; VBIMarMar77530_2121.
DR eggNOG; COG0272; -.
DR HOGENOM; HOG000218459; -.
DR KO; K01972; -.
DR OMA; ENVRTIR; -.
DR BioCyc; MMAR394221:GHNB-2113-MONOMER; -.
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; 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; 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_0000313302.
FT DOMAIN 623 701 BRCT.
FT NP_BIND 43 47 NAD (By similarity).
FT NP_BIND 92 93 NAD (By similarity).
FT ACT_SITE 128 128 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 420 420 Zinc (By similarity).
FT METAL 423 423 Zinc (By similarity).
FT METAL 444 444 Zinc (By similarity).
FT METAL 450 450 Zinc (By similarity).
FT BINDING 126 126 NAD (By similarity).
FT BINDING 149 149 NAD (By similarity).
FT BINDING 186 186 NAD (By similarity).
FT BINDING 302 302 NAD (By similarity).
FT BINDING 326 326 NAD (By similarity).
SQ SEQUENCE 701 AA; 76147 MW; 8A8F7849CB101E58 CRC64;
MSALKDVDQL TEAEARAEHA RLAREIAGHD KAYYQSDAPK ISDAAYDALR RKLEAIEVRF
PQFIDLLSPT QRVGAVPSGK FGEIRHAVPM LSLGNAFNDE DVADFVGRIR RFLGLAESDV
VAVTAEPKID GLSASLRYVG GKLVHGATRG DGQTGEDVTQ NLLTLDDIPD TLPPGDWPDV
VEVRGEVYMS HADFAALNER QIEAGKDAYK NPRNAAAGSL RQIDPKMTSQ RPLRFFAYAW
GEVSEPLSDT QMGAVARFGE MGFPVNDLMA RCETVEALLA VYRDIEARRA GLGYDIDGVV
YKADRLDWQE RLGFVARAPR WAIAHKFPAE QATTILEAID IQVGRTGALT PVARLTPVTV
GGVVVTNATL HNQDEIERKD IRVGDTVVIQ RAGDVIPQVV RVVDPDRPGR GEAFDFPTEC
PVCGSQALRE HDAKTGKLDV VRRCTGGLIC GAQLKERLKH FVSRKAFDIE GLGIKQIEAF
QEEGLITEPA HIFTLKARNE AGEIKPPLQE REGFGETSIR NLFTSIEDRR TITLARFLNA
LGIRHVGENT SALFARTYGS WAAFHAAAAN LSDEAVRAEM LGIDGIGNAA VEALEQYFTE
AHNRDLLDRL VAQLTIEDAE AIANDSPVAG KTVVFTGALE RMTRDEAKAK AQALGAKVAG
SVSGKTDYLV AGPGAGSKAK KAAELGVETL TEDEWFDLIG A
//
