GenomeNet

Database: UniProt
Entry: D2CJS7
LinkDB: D2CJS7
Original site: D2CJS7 
ID   DNLI_SULZI              Reviewed;         606 AA.
AC   D2CJS7;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-OCT-2017, entry version 30.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:18647334};
DE            EC=6.5.1.7 {ECO:0000269|PubMed:18647334};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP/ADP/GTP] {ECO:0000305};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
OS   Sulfophobococcus zilligii.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Sulfophobococcus.
OX   NCBI_TaxID=53426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18647334; DOI=10.1111/j.1462-2920.2008.01710.x;
RA   Sun Y., Seo M.S., Kim J.H., Kim Y.J., Kim G.A., Lee J.I., Lee J.H.,
RA   Kwon S.T.;
RT   "Novel DNA ligase with broad nucleotide cofactor specificity from the
RT   hyperthermophilic crenarchaeon Sulfophobococcus zilligii: influence of
RT   ancestral DNA ligase on cofactor utilization.";
RL   Environ. Microbiol. 10:3212-3224(2008).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. Can use
CC       ATP, ADP and GTP, but not CTP, TTP or NAD(+).
CC       {ECO:0000269|PubMed:18647334}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407,
CC       ECO:0000269|PubMed:18647334}.
CC   -!- CATALYTIC ACTIVITY: ADP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + phosphate. {ECO:0000269|PubMed:18647334}.
CC   -!- CATALYTIC ACTIVITY: GTP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       GMP + diphosphate. {ECO:0000269|PubMed:18647334}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:18647334};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:18647334};
CC       Note=Other divalent cations such as Zn(2+), Ni(2+), Ca(2+) and
CC       Co(2+) are not able to activate the enzyme.
CC       {ECO:0000269|PubMed:18647334};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:18647334};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius. Activity declines
CC         drastically at temperatures from 75 to 80 degrees Celsius.
CC         {ECO:0000269|PubMed:18647334};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
DR   EMBL; EF506613; ABS72370.1; -; Genomic_DNA.
DR   ProteinModelPortal; D2CJS7; -.
DR   SMR; D2CJS7; -.
DR   KEGG; ag:ABS72370; -.
DR   KO; K10747; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; GTP-binding; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    606       DNA ligase.
FT                                /FTId=PRO_0000431839.
FT   ACT_SITE    265    265       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     263    263       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     285    285       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     315    315       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     355    355       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     432    432       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     438    438       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   606 AA;  68393 MW;  9B4D6B7AD0A6EB02 CRC64;
     MPDMPLRILV ETIERLELVT ARTQLVAFLV NLFKQTPPEI IDKVVYLVQG ILWPDWKGMP
     ELGVGEKMLI KAISLACNIS EREVEKTAKE IGDIGKATEK LKQTAQSKQT GLTIFAFTQQ
     PTGLTVTNTY NTLVKIAMAQ GEGSKDLKIR LLAGLLKDAS PKEAKFIVKF VEGKLRVGIG
     DATIMDALAV TFGGGVANRP VIERAYNLRS DLGEVAKILA SKGIEELKKI KPEVGVPIRP
     MLAERLSDPR EILVKTGGEA FVEYKYDGER AQIHKKGDKI WIYSRRLENI TSQYPDVVER
     ALEKIKADEA IVEGEIVVYD PDTGELKPFQ ELMHRKRKHD IRQAIKEYPV KVFLFDLLYL
     NGEDYTLKPL PVRREALEKI IDKTEDFTIA EYIKTSNPEE LEKFFLEAIG NGVEGVMAKA
     IHKDSIYQAG VRGWLWIKYK RDYKSEMADT VDLVVVGAFY GKGRRGGKYG ALLMAAYNKE
     KDVFETVCKV GSGFKDEDLD KLPDMLKPYI RDRKHPRVVA EIEPDVWVDP VLVAEIIGAE
     LTLSPIHTCA KGVIKPDAGI SIRFPRFIRW RPDKRPEDAT TSSELVEMYQ RQLKKITTEQ
     ATQEQL
//
DBGET integrated database retrieval system