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 28-MAR-2018, entry version 103.
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; WLFEESY; -.
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
//
