DNLI_AERPE
ID DNLI_AERPE Reviewed; 602 AA.
AC Q9YD18;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:12935888};
DE EC=6.5.1.7 {ECO:0000305|PubMed:12935888};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP/ADP] {ECO:0000305};
GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=APE_1094.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=12935888; DOI=10.1016/s0014-5793(03)00821-4;
RA Jeon S.J., Ishikawa K.;
RT "A novel ADP-dependent DNA ligase from Aeropyrum pernix K1.";
RL FEBS Lett. 550:69-73(2003).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. Can also use ADP, but
CC not NAD(+). {ECO:0000269|PubMed:12935888}.
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:12935888};
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:12935888};
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:0000250|UniProtKB:A2BJX6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12935888};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12935888};
CC Note=Less active with Ca(2+) or Co(2+). Not active with Cu(2+), Zn(2+),
CC Sr(2+) or Ni(2+). {ECO:0000269|PubMed:12935888};
CC -!- ACTIVITY REGULATION: Inhibited in the presence of 100 mM KCl, NaCl or
CC NH(4)Cl. {ECO:0000269|PubMed:12935888}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12935888};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:12935888};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12935888}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
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DR EMBL; BA000002; BAA80079.2; -; Genomic_DNA.
DR PIR; G72709; G72709.
DR AlphaFoldDB; Q9YD18; -.
DR SMR; Q9YD18; -.
DR STRING; 272557.APE_1094.1; -.
DR PRIDE; Q9YD18; -.
DR EnsemblBacteria; BAA80079; BAA80079; APE_1094.1.
DR KEGG; ape:APE_1094.1; -.
DR PATRIC; fig|272557.25.peg.768; -.
DR eggNOG; arCOG01347; Archaea.
DR OMA; WIKYKRD; -.
DR BRENDA; 6.5.1.1; 171.
DR Proteomes; UP000002518; Chromosome.
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: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; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..602
FT /note="DNA ligase"
FT /id="PRO_0000059600"
FT ACT_SITE 264
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
SQ SEQUENCE 602 AA; 67748 MW; AD1DC7521FAFD814 CRC64;
MPFKPVAEAF ASMERITSRT QLTLLLTRLF KSTPPGAIGI VVYLIQGKLG PDWKGLPELG
VGEKLLVKAI ALAYKATEER VERLYKSVGD LGSVAERLSR EYRSRAARAV TLEAFMAGGG
EALTVRRVYN TLYRIAMAQG EGSRDIKLRL LAGLLADAEP VEAKYIVRFV EGRLRVGVGD
ATVLDALAMA FGGGAHARPV IERAYNLRAD LGYIAEVVAR EGVDALRGVK PQVGVPIRPM
LAERGRDPAE ILRKVGGRAV VEYKYDGERA QIHKKDGEVY IYSRRLENIT RMFPDVVEMA
RKGLKAGEAI VEGEIVAVDP DNYEIQPFQV LMQRKRKHDI HRVMREVPVA VFLFDALYVD
GEDLTSKPLP ERRRRLKEIV VETPLWRLAE SIETSDPEEL WTFFLKAIEE GAEGVMVKAV
HRDSVYTAGV RGWLWVKLKR DYKSEMMDTV DLVVVGAFYG RGKRGGKLSS LLMAAYDPDR
DVFPTVCKVA TGFTDEELDR MNEMLKKHII PRKHPRVESR IEPDVWVEPA LVAEILGAEL
TLSPMHTCCL NTVRPGVGIS IRFPRFIRWR DDKSPEDATT THELLEMYKR QLRRVEEPAE
QV
