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Description:
DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD+]).
Molecular weight: 74602
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:
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
07-MAR-2006, entry version 41.
Phylogenetic order:
Bacteria Cyanobacteria Chroococcales Synechocystis.
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_SYNY3:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BA000022 | BAA16588.1 | - |
| PIR | S74436 | S74436. | |
| HSSP | O87703 | 1B04 | |
| GenomeReviews | BA000022_GR | sll1209.1 | |
| BioCyc | SSP1148:SLL1209-MONOMER | -.1 | |
| InterPro | IPR001357 | BRCT. | |
| InterPro | IPR004150 | DNA_ligase_OB. | |
| InterPro | IPR001679 | DNAligase. | |
| InterPro | IPR000445 | HhH. | |
| InterPro | IPR003583 | HHH1_bd. | |
| InterPro | IPR004149 | Znf_DNAligase_C4. | |
| PANTHER | PTHR11107 | DNAligase.1 | 1. |
| Pfam | PF00533 | BRCT | 1. |
| Pfam | PF01653 | DNA_ligase_aden | 1. |
| Pfam | PF03120 | DNA_ligase_OB | 1. |
| Pfam | PF03119 | DNA_ligase_ZBD | 1. |
| Pfam | PF00633 | HHH | 1. |
| ProDom | PD003944 | DNAligase | 1. |
| SMART | SM00292 | BRCT | 1. |
| SMART | SM00278 | HhH1 | 2. |
| SMART | SM00532 | LIGANc | 1. |
| TIGRFAMs | TIGR00575 | dnlj | 1. |
| PROSITE | PS50172 | BRCT | 1. |
| PROSITE | PS01055 | DNA_LIGASE_N1 | 1. |
| PROSITE | PS01056 | DNA_LIGASE_N2 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; DNA replication; Ligase; NAD.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT entire genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
Feature:
CHAIN 1 669 DNA ligase.
/FTId=PRO_0000161768.
DOMAIN 591 669 BRCT.
ACT_SITE 114 114 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 1 BRCT domain.
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Sequence length: 669
MTTPDRLLQL RQQLQKASYA YYVLDAPVME DSVYDQLYRE LQRLEAENPE LITPDSPTQR
VGEQPASQFR SVAHNIPLYS LENAFNVQEL QQWQERWQRI APTIEKAEYV CELKIDGSAI
ALTYENGLLV RGVTRGDGTT GEEISQNIKT IRSIPVKLNL DNPPPTVEVR GEAFLPLEEF
NRINHEREAQ GESLFANPRN AAAGTLRQLD PKIVHQRRLQ FFAYTLHLPG QEDKIQSQWQ
ALEYLKKAGF MVNPHCQLCK GLDEVVAYFE DWEGARQRLP YMTDGVVVKI NQYPLQRELG
FTQKFPRWAI ALKYPAEETP TVVKAIEVNV GRTGAVTPLA VMEPVQLAGT TVQRATLHNQ
DRIQELDIRV GDTVIIRKAG EIIPEVVRVM TELRPENTTP YIFPSHCPAC GSPLVRPLEE
AVIRCVNSSC SAILQGSLIH WASRNALDIQ GLGEKVVITL LENRLVNSVA DLYGLQVEQL
LGLERFAQKS AEKLIAAIEV SKSQPWSRIL FGLGIRHVGQ VNAKLLSQQF PTVEKLSQAS
IPDLEGVYGI GPEIAEAVVN WFRNPGNQQL IQDLEELGLV LANQGIDQTK TDSGKLKGKT
FVLTGTLPNL SRLEAQELIE QSGGKVTSSV STKTDYVLLG DKPGSKAAKA ESLGIKLLSE
AEFLQLLEP