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Database: UniProt
Entry: Q3YRC1
LinkDB: Q3YRC1
Original site: Q3YRC1 
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   26-NOV-2014, entry version 70.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN   Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-
CC       ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC   -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
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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; DSKITAN; -.
DR   OrthoDB; EOG6TTVM9; -.
DR   BioCyc; ECAN269484:GI02-737-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; IPR001679; DNAligase.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
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.
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. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   NP_BIND      34     38       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   NP_BIND      83     84       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   ACT_SITE    119    119       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       401    401       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       404    404       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       419    419       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       425    425       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     117    117       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     140    140       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     175    175       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     283    283       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     307    307       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
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
//
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