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Database: UniProt
Entry: Q0AMX9
LinkDB: Q0AMX9
Original site: Q0AMX9 
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   16-APR-2014, entry version 58.
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; FTAKSPR; -.
DR   OrthoDB; EOG6TTVM9; -.
DR   BioCyc; MMAR394221:GHNB-2113-MONOMER; -.
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; IPR012340; NA-bd_OB-fold.
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; 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_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
//
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