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Database: UniProt/SWISS-PROT
Entry: DNLI2_THEPD
LinkDB: DNLI2_THEPD
Original site: 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   05-DEC-2018, entry version 79.
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};
GN   OrderedLocusNames=Tpen_0750;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; 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.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E.,
RA   Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S.,
RA   Detter C., Zhulin I.B., Olsen G.J., Whitman W., Mukhopadhyay B.,
RA   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
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-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-
CC         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}.
DR   EMBL; CP000505; ABL78152.1; -; Genomic_DNA.
DR   RefSeq; WP_011752417.1; NC_008698.1.
DR   ProteinModelPortal; A1RY72; -.
DR   SMR; A1RY72; -.
DR   STRING; 368408.Tpen_0750; -.
DR   EnsemblBacteria; ABL78152; ABL78152; Tpen_0750.
DR   GeneID; 4600401; -.
DR   KEGG; tpe:Tpen_0750; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    601       DNA ligase 2.
FT                                /FTId=PRO_0000365266.
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     314    314       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     354    354       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   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
//
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