DNLI_SULZI
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 03-AUG-2022, entry version 39.
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, COFACTOR,
RP 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 during DNA
CC replication, DNA recombination and DNA repair. Can use ATP, ADP and
CC GTP, but not CTP, TTP or NAD(+). {ECO:0000269|PubMed:18647334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00407,
CC ECO:0000269|PubMed:18647334};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.;
CC EC=6.5.1.7; Evidence={ECO:0000269|PubMed:18647334};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP +
CC diphosphate.; EC=6.5.1.7; Evidence={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 Co(2+)
CC are not able to activate the enzyme. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF506613; ABS72370.1; -; Genomic_DNA.
DR AlphaFoldDB; D2CJS7; -.
DR SMR; D2CJS7; -.
DR PRIDE; D2CJS7; -.
DR KEGG; ag:ABS72370; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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; Manganese;
KW Metal-binding; Nucleotide-binding.
FT CHAIN 1..606
FT /note="DNA ligase"
FT /id="PRO_0000431839"
FT ACT_SITE 265
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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
