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Protein data for DNLI_ARATH:

Description:
DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]).

Molecular weight: 87740

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:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
10-JAN-2003, sequence version 2.
07-FEB-2006, entry version 38.

Phylogenetic order:
Eukaryota Viridiplantae Streptophyta Embryophyta Tracheophyta Spermatophyta Magnoliophyta eudicotyledons core eudicotyledons rosids eurosids II Brassicales Brassicaceae Arabidopsis.

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 DNLI_ARATH:

DatabasePointerAdd. info#1Add. info#2
EMBLX97924CAA66599.1-
EMBLAC026875AAF79833.1ALT_SEQ
EMBLAC011438AAF18258.1ALT_SEQ
EMBLBT005964AAO64899.1-
PIRS71278S71278.
TAIRAt1g08130-.1
InterProIPR000977DNA_ligase.
InterProIPR012309DNA_ligase_A_C.
InterProIPR012310DNA_ligase_A_M.
InterProIPR012308DNA_ligase_A_N.
PANTHERPTHR10459DNA_ligase.11.
PfamPF04679DNA_ligase_A_C1.
PfamPF01068DNA_ligase_A_M1.
PfamPF04675DNA_ligase_A_N1.
TIGRFAMsTIGR00574dnl11.
PROSITEPS00697DNA_LIGASE_A11.
PROSITEPS00333DNA_LIGASE_A21.
PROSITEPS50160DNA_LIGASE_A31.

General information about the databases mentioned above

Keywords:
ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nuclear protein; Nucleotide-binding.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Landsberg erecta;
RX MEDLINE=98346005; PubMed=9681027;
RA Taylor R.M., Hamer M.J., Rosamond J., Bray C.M.;
RT "Molecular cloning and functional analysis of the Arabidopsis thaliana
RT DNA ligase I homologue.";
RL Plant J. 14:75-81(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).

Feature:
CHAIN 1 790 DNA ligase.
/FTId=PRO_0000059586.
ACT_SITE 444 444 N6-AMP-lysine intermediate (By
similarity).
CONFLICT 639 639 A -> P (in Ref. 1).

Comments:
-!- FUNCTION: This protein seals, during DNA replication, DNA
recombination and DNA repair, nicks in double-stranded DNA.
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
(deoxyribonucleotide)(m) = AMP + diphosphate +
(deoxyribonucleotide)(n+m).
-!- SUBCELLULAR LOCATION: Nucleus (By similarity).
-!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
-!- CAUTION: Ref.2 sequences differ from that shown due to erroneous
gene model prediction.
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Sequence length: 790

     MLAIRSSNYL RCIPSLCTKT QISQFSSVLI SFSRQISHLR LSSCHRAMSS SRPSAFDALM
     SNARAAAKKK TPQTTNLSRS PNKRKIGETQ DANLGKTIVS EGTLPKTEDL LEPVSDSANP
     RSDTSSIAED SKTGAKKAKT LSKTDEMKSK IGLLKKKPND FDPEKMSCWE KGERVPFLFV
     ALAFDLISNE SGRIVITDIL CNMLRTVIAT TPEDLVATVY LSANEIAPAH EGVELGIGES
     TIIKAISEAF GRTEDHVKKQ NTELGDLGLV AKGSRSTQTM MFKPEPLTVV KVFDTFRQIA
     KESGKDSNEK KKNRMKALLV ATTDCEPLYL TRLLQAKLRL GFSGQTVLAA LGQAAVYNEE
     HSKPPPNTKS PLEEAAKIVK QVFTVLPVYD IIVPALLSGG VWNLPKTCNF TLGVPIGPML
     AKPTKGVAEI LNKFQDIVFT CEYKYDGERA QIHFMEDGTF EIYSRNAERN TGKYPDVALA
     LSRLKKPSVK SFILDCEVVA FDREKKKILP FQILSTRARK NVNVNDIKVG VCIFAFDMLY
     LNGQQLIQEN LKIRREKLYE SFEEDPGYFQ FATAVTSNDI DEIQKFLDAS VDVGCEGLII
     KTLDSDATYE PAKRSNNWLK LKKDYMDSIG DSVDLVPIAA FHGRGKRTGV YGAFLLACYD
     VDKEEFQSIC KIGTGFSDAM LDERSSSLRS QVIATPKQYY RVGDSLNPDV WFEPTEVWEV
     KAADLTISPV HRAATGIVDP DKGISLRFPR LLRVREDKKP EEATSSEQIA DLYQAQKHNH
     PSNEVKGDDD

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