DNLI2_THEPD
ID DNLI2_THEPD Reviewed; 601 AA.
AC A1RY72;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=DNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00407};
DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 2 {ECO:0000255|HAMAP-Rule:MF_00407};
GN Name=lig2 {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=Tpen_0750;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. {ECO:0000255|HAMAP-
CC Rule:MF_00407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407}.
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DR EMBL; CP000505; ABL78152.1; -; Genomic_DNA.
DR RefSeq; WP_011752417.1; NC_008698.1.
DR AlphaFoldDB; A1RY72; -.
DR SMR; A1RY72; -.
DR STRING; 368408.Tpen_0750; -.
DR PRIDE; A1RY72; -.
DR EnsemblBacteria; ABL78152; ABL78152; Tpen_0750.
DR GeneID; 4600401; -.
DR KEGG; tpe:Tpen_0750; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OMA; WIKYKRD; -.
DR OrthoDB; 52275at2157; -.
DR Proteomes; UP000000641; 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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..601
FT /note="DNA ligase 2"
FT /id="PRO_0000365266"
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 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 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 601 AA; 66943 MW; 8AA565878E7AF78B CRC64;
MGAAGDLPYS VLADFYERIE STSSRLAMTD YLVALFKKTP PEVIDKVVYL TQGQLRPDYE
GVELGVAEKL ALRALAKASG RHLKDVEDLY KKTGDIGAVA EKLLTAPGGG LLEFFGTPVQ
KKELTVSQVY SALMKIAQAS GEGAQETKVN TLVALLQDAK PKEARYILRT VLGRLRLGIA
DMTILDALAA AFAGSKAARD VIERAYTKHP DLGYIAKLLA TKGLDAVASL KIEVGIPVLP
MLAERLSDPA EILEKLGGKC LAEYKYDGER VQAHKSGDKV LLFSRRLENI THHYPDVVEY
VKRLKVREAI VEGEIVAYNP DTGEMLPFQE LMHRRRKYDV EKAMKEYPVR VYLFDVIYMD
GEELIEKPLD QRRLILEKIV PEGDEDILLS TAKVVGDAKD LLHFFEQAIS EGCEGVMCKS
IGPGSIYQMG ARGWLWIKFK RDYRMEMTDT VDLVVVGGFH GRGKRAGTYG ALLMAAYDPE
TDTFKTVCKV GTGFTDEDLA KLPELLDPYK IPHRHPRVFS KIEADVWFVP AVVLEIIGAE
ITLSPLHTCA LNKLEEGAGL AIRFPRFTGR YRFDKKPEQA TTESELIEMY KSQKKTALQQ
S
