(data stored in ACNUC30630 zone)

SWISSPROT: DNLJ_THERP

ID   DNLJ_THERP              Reviewed;         695 AA.
AC   B9KXM2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 64.
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}; OrderedLocusNames=trd_0210;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC       linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC       stranded DNA using NAD as a coenzyme and as the energy source for the
CC       reaction. It is essential for DNA replication and repair of damaged
CC       DNA. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={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; CP001275; ACM05038.1; -; Genomic_DNA.
DR   RefSeq; WP_012641622.1; NC_011959.1.
DR   SMR; B9KXM2; -.
DR   STRING; 309801.trd_0210; -.
DR   EnsemblBacteria; ACM05038; ACM05038; trd_0210.
DR   KEGG; tro:trd_0210; -.
DR   eggNOG; ENOG4105C77; Bacteria.
DR   eggNOG; COG0272; LUCA.
DR   HOGENOM; HOG000218459; -.
DR   KO; K01972; -.
DR   OMA; HDVEHEI; -.
DR   OrthoDB; 241401at2; -.
DR   BioCyc; TROS309801:G1GU8-204-MONOMER; -.
DR   Proteomes; UP000000447; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
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; cd00114; LIGANc; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   HAMAP; MF_01588; DNA_ligase_A; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR041663; DisA/LigA_HHH.
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   Pfam; PF12826; HHH_2; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00278; HhH1; 4.
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;
DR   PRODOM; B9KXM2.
DR   SWISS-2DPAGE; B9KXM2.
KW   DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW   Metal-binding; NAD; Zinc.
FT   CHAIN           1..695
FT                   /note="DNA ligase"
FT                   /id="PRO_0000380496"
FT   DOMAIN          606..695
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   NP_BIND         44..48
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   NP_BIND         93..94
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   ACT_SITE        126
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           422
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           425
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           440
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   METAL           445
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         124
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         147
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         187
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         304
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         328
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ   SEQUENCE   695 AA;  77976 MW;  A2DF222A37D4A940 CRC64;
     MAEQPALQAD RVPPEVRARV EELRRLIQRY NYEYYVLNAP TVSDAEYDAL MLELRRWEEQ
     YPELVTPDSP TQRVGAPPAE GFATVQHEIP MLSLGNVFSD GEIRAWAERV YRLSGRQDVE
     FVTEPKVDGL AVSLLYRDGV LVRGATRGDG YTGEDVTNNV RTIRMIPLRL YPPEGVIVPP
     VLEVRGEVYM NVRDFERLNR ERGEQGLPLF ANPRNAAAGS LRQLDPSVTA SRPLRFAAWD
     IGLWEGTEPP ATHLATLEFL RQLQIPVVPD YRLCRSVDEV IAECHRWQER RDALEFEADG
     VVIKVNDRAL YQALGVVGRE PRGATAYKFP AHEKTTIVRD VIWSVGRTGK LTPVAVLEPV
     EIGGVIVERA TLHNEEEIRR LGLLIGDAVV VQRRGDVIPK VVATIPQRRD GDERPVDIPR
     QCPVCGAHTI RLEGEVDRYC PNPNCPARLK ASVRHFASRN AMDIEGLGEK ISDLFVDLGI
     IRSLPDLYEI DWARVLQLEG FGPKKVENLR KAIEASKNRP FARFLFALGI RHVGERNAQL
     LADHFRSIDR LMEATIDELL QIPGFGPAVA QSVFEFFREP KNREMIERFR RLGVRMAEEE
     AAAVATVQGP LAGKTVVLTG RLETLTRSQA EELLRRAGAH VTDSVSRKTD YVFAGADPGS
     KYVRAQQLGV PILGEEDLLR MLRESGIEVE AAARS
//

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