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Database: UniProt/SWISS-PROT
Entry: DNLI2_KORCO
LinkDB: DNLI2_KORCO
Original site: DNLI2_KORCO 
ID   DNLI2_KORCO             Reviewed;         594 AA.
AC   B1L3V2;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   28-MAR-2018, entry version 68.
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=Kcr_0375;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N.,
RA   Wanner G., Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(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: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {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}.
DR   EMBL; CP000968; ACB07131.1; -; Genomic_DNA.
DR   RefSeq; WP_012309028.1; NC_010482.1.
DR   ProteinModelPortal; B1L3V2; -.
DR   SMR; B1L3V2; -.
DR   STRING; 374847.Kcr_0375; -.
DR   EnsemblBacteria; ACB07131; ACB07131; Kcr_0375.
DR   GeneID; 6093662; -.
DR   KEGG; kcr:Kcr_0375; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   InParanoid; B1L3V2; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; CKOR374847:G1GBF-387-MONOMER; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
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   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    594       DNA ligase 2.
FT                                /FTId=PRO_0000365250.
FT   ACT_SITE    252    252       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     250    250       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     257    257       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     273    273       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     303    303       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     343    343       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     419    419       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     425    425       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   594 AA;  67657 MW;  662A34BCFC2A573E CRC64;
     MNFIDVAKIY EKIEATTGRL EMIDYLKNLF LSTPPEILDK IVYLTLGNIA ASFEGIELGV
     GEKLFLRALS LATGIPQERL EEEYPKLGDI GKLAEWAVSK KAAQSFFTED LTVERVFDTL
     SKVARATGEG AQDLKVRLIA GILSDAKPLE ARYIARIVTE KLRLGVRDMT VLDALSEAFL
     KGRAYRDKLE RKYNIYPDIG KIAKVVAEKG IKGLDEITIT LGIPVRPMLA QRLRSAEEIM
     EKIGPRIFAE FKYDGERMQI HVWKDGKVKI FSRRLEDITE PYPDVREYVS KAVEGHEVVL
     DCETVAINPD TGEILPFQEL MHRRRKYGVE EAMKTYPTVT YAFDLLYLDG RELLDEQLDD
     RRKILKEILK ENEKARLVQY EEIDGNVEEL ERFFEHAVEM GTEGLVVKDP KSIYQAGVRG
     WSWIKLKRSY ISKMIEPVDL VVVGAFWGKG KRAGTYGALL MAAYSPEEDV FKTVCKMGSG
     FTDEELARMP KLLEDYKIDH KHPSVISNIE ADVYFVPVKV AQVLGDEITL SPTHTCGWNK
     VRKNAGLAIR FPRFMGWRDD KGPQDATTEE EIIEMYKEQL KVVEVEETKS EEEA
//
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