ID C9RD93_AMMDK Unreviewed; 672 AA.
AC C9RD93;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 30.
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 BioCyc; ADEG429009:GHG1-1153-MONOMER; -.
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 592 672 BRCT (By similarity).
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
//
