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Database: UniProt/TrEMBL
Entry: C9RD93_AMMDK
LinkDB: C9RD93_AMMDK
Original site: C9RD93_AMMDK 
ID   C9RD93_AMMDK            Unreviewed;       672 AA.
AC   C9RD93;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   19-FEB-2014, entry version 35.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.2;
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN   Name=ligA; OrderedLocusNames=Adeg_1094;
OS   Ammonifex degensii (strain DSM 10501 / KC4).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Ammonifex.
OX   NCBI_TaxID=429009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10501 / KC4;
RG   US DOE Joint Genome Institute;
RA   Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA   Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL   Submitted (OCT-2009) 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; CP001785; ACX52220.1; -; Genomic_DNA.
DR   RefSeq; YP_003239070.1; NC_013385.1.
DR   ProteinModelPortal; C9RD93; -.
DR   STRING; 429009.Adeg_1094; -.
DR   EnsemblBacteria; ACX52220; ACX52220; Adeg_1094.
DR   GeneID; 8491082; -.
DR   KEGG; adg:Adeg_1094; -.
DR   PATRIC; 20881754; VBIAmmDeg104956_1099.
DR   eggNOG; COG0272; -.
DR   HOGENOM; HOG000218459; -.
DR   KO; K01972; -.
DR   OrthoDB; EOG6TTVM9; -.
DR   BioCyc; ADEG429009:GHG1-1125-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:0006266; P:DNA ligation; IEA:GOC.
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   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; 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   NP_BIND      38     42       NAD (By similarity).
FT   NP_BIND      87     88       NAD (By similarity).
FT   ACT_SITE    120    120       N6-AMP-lysine intermediate (By
FT                                similarity).
FT   METAL       411    411       Zinc (By similarity).
FT   METAL       414    414       Zinc (By similarity).
FT   METAL       429    429       Zinc (By similarity).
FT   METAL       434    434       Zinc (By similarity).
FT   BINDING     118    118       NAD (By similarity).
FT   BINDING     141    141       NAD (By similarity).
FT   BINDING     177    177       NAD (By similarity).
FT   BINDING     293    293       NAD (By similarity).
FT   BINDING     317    317       NAD (By similarity).
SQ   SEQUENCE   672 AA;  75991 MW;  5E587E454A6728ED CRC64;
     MARRLSKEEA KRRIEELRRE IAYHDYRYYV LDSPVISDAE YDRLVLELMA LEEAFPEFIT
     PNSPTQRVGG APREGFPTVR HLVPMLSLAN AFEPEDLRDF DRRVREALPG EKVEYVVEPK
     IDGLAVSLLY RDGEFVQGAT RGDGEVGEDV TPNLRTIRSI PLRFLKDAPP LIEVRGEAFM
     PKEAFVKLNE RREEAGEPPF ANPRNAAAGS IRQLDPRVTA GRKLDFFAYG IGHYEGISFS
     THWEVLDWLA EQGFRVNEHR RLFSSIDEVI DYVLSWQSKR FDLPYVIDGM VVKVNSLESQ
     ARLGATMKSP RWAVAFKFPP EEAVTKLRRI EISVGRTGVL TPVAVFDPVQ IAGTTVSRAT
     LHNEDLIREK DIRVGDYIVV HKAGDVIPEV VRSLPERRTG NEQIFRMPDH CPACGAKTIR
     EEGEVAVRCP NISCPARLKE SIFHFASRNA MDIRGLGKVL VEQLVDRGLV KNVADIYFLR
     REDLLRLERM GPKSTANLLR EIEESKSRGL NRLIFGLGIR HVGERAAKLL AEHFGSIDRL
     AQATEEELTE IPEIGPKIAA SVRAFFAEPR NLEVIERLRE AGVRLETTKE VREEGPLKGK
     VFVFTGALKS FTREEAKALI ERLGGRVASS VSRRTDYVVV GENPGSKYDR ARELGIKMLN
     EEEFKRLLGL ES
//
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