ID DNLJ_EHRCJ Reviewed; 677 AA.
AC Q3YRC1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 29-MAY-2013, entry version 62.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=Ecaj_0702;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake;
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
RA Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
RA Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
RA Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000107; AAZ68734.1; -; Genomic_DNA.
DR RefSeq; YP_303332.1; NC_007354.1.
DR ProteinModelPortal; Q3YRC1; -.
DR STRING; 269484.Ecaj_0702; -.
DR EnsemblBacteria; AAZ68734; AAZ68734; Ecaj_0702.
DR GeneID; 3617902; -.
DR KEGG; ecn:Ecaj_0702; -.
DR PATRIC; 20575016; VBIEhrCan118076_0755.
DR eggNOG; COG0272; -.
DR HOGENOM; HOG000218458; -.
DR KO; K01972; -.
DR OMA; NPKNSDM; -.
DR ProtClustDB; CLSK2558359; -.
DR BioCyc; ECAN269484:GI02-737-MONOMER; -.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:EC.
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; 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; FALSE_NEG.
DR PROSITE; PS01056; DNA_LIGASE_N2; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; DNA damage; DNA repair; DNA replication; Ligase;
KW Magnesium; Manganese; Metal-binding; NAD; Zinc.
FT CHAIN 1 677 DNA ligase.
FT /FTId=PRO_0000313223.
FT DOMAIN 594 677 BRCT.
FT NP_BIND 34 38 NAD (By similarity).
FT NP_BIND 83 84 NAD (By similarity).
FT ACT_SITE 119 119 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 401 401 Zinc (By similarity).
FT METAL 404 404 Zinc (By similarity).
FT METAL 419 419 Zinc (By similarity).
FT METAL 425 425 Zinc (By similarity).
FT BINDING 117 117 NAD (By similarity).
FT BINDING 140 140 NAD (By similarity).
FT BINDING 175 175 NAD (By similarity).
FT BINDING 283 283 NAD (By similarity).
FT BINDING 307 307 NAD (By similarity).
SQ SEQUENCE 677 AA; 76854 MW; A54363B8D5F86757 CRC64;
MKQEEAKLEL DKLNSQIQHH DFLYYTQDNP QITDAEYDVL CHKRNLILES FPELASNNNY
QDNVGSTPDA KFAKVKHAEK MLSLDNAFNQ QDIEKFITRT KKLLDMDNSQ SIAISCELKI
DGLSFSVIYK KGEISQASTR GNGYFGENIT NNVKTIKNLP HTIQNAPDSL EVRGEIYIDR
SDFIQLNKDG NNFANPRNAA AGSVRQLDIN ITAQRKLKYF MYTIVNTKCL TQEETLNQLK
TLGFCVNEHT ITTNNIEDAL NFYNQFYNNR SNISYDIDGI IYKVNDIKSQ HILGATNKSP
RWAIAYKFPA AEAKTLVNKI SIQIGRTGVL TPIAELSPIN IGGVIVTRAS LHNKSEIERK
DIREGDYVIV KRAGDVIPQV VDVDKNLRAQ ELTKFIFPTT CPSCGSNLFQ AEQEVSIYCT
GELFCKNQIL EKIKHFVSKD AFNIIGFGKK QLLFFYEQGL ITNIVDIFTL EEKISNSDLK
LESLHGWGEK SIHNLFSAIN NSKTISLENF IFALGIRFVG KYIAKILAKH FLSYEKWYHE
MLRLAQDENY LLNIQQIGHK TIHSLKMFFT EQHNLDTINN LVRHLTITDA KTTSHLSLLH
GKTIVFTGEL SNMSRHEAKT KSETAGAKVS SSLSKNTDFL IVGNNPGSKY KKAQSLNIQI
LTEDLWLQYI SPNTNEN
//
