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Description:
DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD+]).
Molecular weight: 91098
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
07-MAR-2006, entry version 39.
Phylogenetic order:
Bacteria Spirochaetes Spirochaetales Spirochaetaceae Treponema.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DNLJ_TREPA:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE000520 | AAC65609.1 | - |
| PIR | H71300 | H71300. | |
| HSSP | O87703 | 1B04 | |
| GenomeReviews | AE000520_GR | TP0634.1 | |
| TIGR | TP0634 | -. | |
| LinkHub | O83642 | -.1 | |
| InterPro | IPR001357 | BRCT. | |
| InterPro | IPR004150 | DNA_ligase_OB. | |
| InterPro | IPR001679 | DNAligase. | |
| InterPro | IPR003583 | HHH1_bd. | |
| PANTHER | PTHR11107 | DNAligase.1 | 2. |
| Pfam | PF00533 | BRCT | 3. |
| Pfam | PF01653 | DNA_ligase_aden | 1. |
| Pfam | PF03120 | DNA_ligase_OB | 1. |
| ProDom | PD003944 | DNAligase | 1. |
| SMART | SM00292 | BRCT | 3. |
| SMART | SM00278 | HhH1 | 1. |
| SMART | SM00532 | LIGANc | 1. |
| TIGRFAMs | TIGR00575 | dnlj | 1. |
| PROSITE | PS50172 | BRCT | 3. |
| PROSITE | PS01055 | DNA_LIGASE_N1 | 1. |
| PROSITE | PS01056 | DNA_LIGASE_N2 | FALSE_NEG. |
Keywords:
Complete proteome; DNA damage; DNA repair; DNA replication; Ligase; NAD; Repeat.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA Weidman J.F., Smith H.O., Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis
RT spirochete.";
RL Science 281:375-388(1998).
Feature:
CHAIN 1 823 DNA ligase.
/FTId=PRO_0000161774.
DOMAIN 562 653 BRCT 1.
DOMAIN 654 740 BRCT 2.
DOMAIN 741 823 BRCT 3.
ACT_SITE 100 100 N6-AMP-lysine intermediate (By
similarity).
Comments:
-!- FUNCTION: This protein catalyzes the formation of phosphodiester
linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
stranded DNA using NAD as a coenzyme and as the energy source for
the reaction. It is essential for DNA replication and repair of
damaged DNA (By similarity).
-!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
(deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide +
(deoxyribonucleotide)(n+m).
-!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family.
-!- SIMILARITY: Contains 3 BRCT domains.
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Sequence length: 823
MSTAQRRVQE LEKLILHHQD RYYNAESDIS DDAFDALWEE LARLDPGNPL LKAIGSDSQR
DAVKKRHIVP MGSQHKAADE ESFSAWAKKN ALQAFLVQHK LDGVSLELQY ERGHFCCALT
RGNGIVGDDV TANVRGMRGF VPTLTAEWGP CGNLPFTGGV RGEVIMHKDI HRSHYPTHAN
CRNTVNGILK RKDGRGRTHL HIVCYDAVPG TPGKPFTGSL PFADETEKLA WLARQGFVTV
HSHRCANAQE VVALRSEIMR TRELLPYSID GLVVKSTDLD FQDAQLPRPK KQIAFKFSTQ
EAITTLRDVQ WQTSGVTYTP IGITDPVRLA GTTVKRANLC NPNMLTKLCL KIGSHVLISK
RGEIIPKIEA LVSTPAHAQE IHIPTQCTSC NTVLENSGSR LFCPNVNCPL LSHHRITRWI
ECLEIKHVGT ELIQRLFEEK KVRRIPDLYT LTCEDLIEIE HVGNATAKKI LEAIHHKKEI
ALQTFIAGFG IEGIGETMGE KLICAGFDTL EKVLHATTET LESIYQFGTE LAKSVVTGIA
RVKDDMCELL DRGFVRILAK QQAESPLRGK SFCFSGSLRN GDRATIHRIR ALGGVVRTSV
TRDLSYLIFE SLSQPYRTAQ KLKKEQGVAL EIISEDEFCR LLDQASASCT HTGETVHPLQ
GKSFYFSGAS RSMNHKHAQE KVRALGGDVA SSVTAQLDYL VFYSQSTRYR TACALGIQII
SEETLHKLIA TAQSPLHTDA HVHAPLHGMS FCFSGDLDGM TRAQAIALVQ RLGGTVKTAV
STQLTYLVSN DPHGQSRKCQ NAVRCGVRII SEHVFLALCT PGT