ID   DNLI_METMA              Reviewed;         568 AA.
AC   Q8PTK1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 44.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=lig; OrderedLocusNames=MM_2714;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; 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: This protein seals, during DNA replication, DNA
CC       recombination and DNA repair, nicks in double-stranded DNA (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
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DR   EMBL; AE008384; AAM32410.1; -; Genomic_DNA.
DR   RefSeq; NP_634738.1; -.
DR   GeneID; 1481056; -.
DR   GenomeReviews; AE008384_GR; MM_2714.
DR   KEGG; mma:MM_2714; -.
DR   NMPDR; fig|192952.1.peg.2714; -.
DR   HOGENOM; Q8PTK1; -.
DR   BioCyc; MMAZ192952:MM2714-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR   HAMAP; MF_00407; -; 1.
DR   InterPro; IPR000977; DNA_ligase.
DR   InterPro; IPR012309; DNA_ligase_A_C.
DR   InterPro; IPR012310; DNA_ligase_A_M.
DR   InterPro; IPR012308; DNA_ligase_A_N.
DR   InterPro; IPR016059; DNA_ligase_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
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   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; FALSE_NEG.
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;
KW   Nucleotide-binding.
FT   CHAIN         1    568       DNA ligase.
FT                                /FTId=PRO_0000059606.
FT   ACT_SITE    256    256       N6-AMP-lysine intermediate (By
FT                                similarity).
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
//