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Database: UniProt
Entry: Q8PTK1
LinkDB: Q8PTK1
Original site: Q8PTK1 
ID   DNLI2_METMA             Reviewed;         568 AA.
AC   Q8PTK1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-OCT-2017, entry version 102.
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=MM_2714;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32410.1; -; Genomic_DNA.
DR   RefSeq; WP_011034623.1; NC_003901.1.
DR   ProteinModelPortal; Q8PTK1; -.
DR   SMR; Q8PTK1; -.
DR   STRING; 192952.MM_2714; -.
DR   EnsemblBacteria; AAM32410; AAM32410; MM_2714.
DR   GeneID; 24851642; -.
DR   KEGG; mma:MM_2714; -.
DR   PATRIC; fig|192952.21.peg.3124; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000000595; Chromosome.
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; IEA:UniProtKB-EC.
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-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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    568       DNA ligase 2.
FT                                /FTId=PRO_0000059606.
FT   ACT_SITE    256    256       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     261    261       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     276    276       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     306    306       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     346    346       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     425    425       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     431    431       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   568 AA;  63185 MW;  D98B7C62AD2B6751 CRC64;
     MTSFREFAET CQAIEKISST IETTNKVADL LKKVDVEELP VATHFIMSEV FPAWSGEQLG
     IGTSLLYVSL SKASGMSIHS IESLVRTTGD IGDTALLILK EKRKNQVTFS SFFEEKPELS
     ITEVYRRFKI ASEASGKGSQ DIKVKNLQFL FTSSSPREAK YISRLALEEL RIGVGEGVVR
     DAIAKAFSVP AEIVEHSFMV TNDLGIVAAA AKKGGVEALE RLGIEINRPI KMMLSQISPD
     IDADIRAMKE VAIEWKFDGA RVQIHKDGNS VTLFSRKLEN VTSSLPDLVE IVRKHVKAES
     AILDGEAVAV DENGVPRAFQ EILKRFRRKY DVREKALGIP IQLNFFDIMY INGKTLIDLP
     LLERRKALES CVESSVEDSK SISVAEQVIT GDLELVEKIY REALKAGHEG VMVKNPNSVY
     SPGKRGKNWL KKKPLMDTLD LVIVGAEWGF GRRANLIGSY TVACYDPDTT RFLQVGKVGT
     GLTDDQLKEL TEILSGLMEG GEAGGVFAIR PKVVLEIAFE EIQKSPNYDS GFALRFPRFI
     RIRDDKDPEE ADTIQRIGRV YSQQLKRL
//
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