(data stored in ACNUC7421 zone)

SWISSPROT: DNLJ_METNO

ID   DNLJ_METNO              Reviewed;         829 AA.
AC   B8ICE5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   30-AUG-2017, entry version 62.
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=Mnod_0491;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-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. {ECO:0000255|HAMAP-
CC       Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl
CC       + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m)
CC       + AMP + beta-nicotinamide D-nucleotide. {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}.
DR   EMBL; CP001349; ACL55533.1; -; Genomic_DNA.
DR   RefSeq; WP_015927243.1; NC_011894.1.
DR   ProteinModelPortal; B8ICE5; -.
DR   SMR; B8ICE5; -.
DR   STRING; 460265.Mnod_0491; -.
DR   PRIDE; B8ICE5; -.
DR   EnsemblBacteria; ACL55533; ACL55533; Mnod_0491.
DR   KEGG; mno:Mnod_0491; -.
DR   eggNOG; ENOG4105C77; Bacteria.
DR   eggNOG; COG0272; LUCA.
DR   HOGENOM; HOG000218459; -.
DR   KO; K01972; -.
DR   OMA; QPADLFR; -.
DR   OrthoDB; POG091H024G; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-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   CDD; cd00027; BRCT; 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; IPR033136; DNA_ligase_CS.
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; 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; SM00278; HhH1; 3.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 2.
DR   SUPFAM; SSF50249; SSF50249; 2.
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;
DR   PRODOM; B8ICE5.
DR   SWISS-2DPAGE; B8ICE5.
KW   Complete proteome; DNA damage; DNA repair; DNA replication; Ligase;
KW   Magnesium; Manganese; Metal-binding; NAD; Reference proteome; Zinc.
FT   CHAIN         1    829       DNA ligase.
FT                                /FTId=PRO_0000380417.
FT   DOMAIN      750    829       BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   NP_BIND      47     51       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   NP_BIND      96     97       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   ACT_SITE    132    132       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       453    453       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       456    456       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       477    477       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   METAL       483    483       Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     130    130       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     153    153       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     190    190       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     306    306       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
FT   BINDING     330    330       NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
SQ   SEQUENCE   829 AA;  89489 MW;  FC65B9407AD4623E CRC64;
     MPAQTSRARP VEEMTAAQAR EAHESLSAEI AEHDRRYHGE DAPIISDAEY DALRRRLEAI
     EERFPELAGT GAASVSVGAK ASDKFAKVRH AVPMLSLGNA FAEEEITEFV ERVRRFLGLP
     ASEPLAFTAE PKIDGLSLSL RYEGGRLVTA ATRGDGEVGE DVTANVRTIR EIPHELAGDD
     VPEICEVRGE VYLSHADFAA INARQEEAGR PLFANPRNAA AGSLRQLDPG ITASRPLRFF
     AYAAGEMSSW PAETQSGLIG AFRRFGLPVN PRTKRCTSVA EMLAHYRAIE TERAELGYDI
     DGVVYKVDEF ALQRRLGFVA RAPRWALAHK FPAQRAVTVI EAIEINVGRT GSLNPLARLK
     PVTVGGVVVS NATLHNEDYI RGIDADGNTI RSGINIWDGF RLREDVDLRQ GSDVRVGDTV
     VVLRAGDVIP KVADVVLERR PADAVPYAFP ETCPACGSHA VRAYNPRTGK LDSVRRCTGG
     LICPAQGQER LRHFVSRNAF DIEGFGETYI ATLFEAGLVR QPADLFRLDF EPLKAAIVAR
     RQALSAERAL AAGKTPEAKK AKPKANEEDK AIHNLLAAVE ARRTIPLNRF IFALGIEQVG
     EATAKALAKH FPDMPALMEG VRAAAACRPG PDWIELASLP RVGPTTRERL LAAAEAGETD
     LLADGAVTRL TSAQKEALLA AYGDRDGLRN AVERALRQKP GDAYRHLADD SEIGAVTTAS
     LIEFFSEAHN VEAVEALLRE VRTERAGTPA AAAVFSGQTV VFTGSLERMT RSEAKATAER
     LGAKVSGSVS AKTDLVVAGP GAGSKLKDAE KHGVRVISEA EWLAMVEAA
//

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