ID   D1Z0H5_METPS            Unreviewed;       295 AA.
AC   D1Z0H5;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=DNA ligase D polymerase domain-containing protein {ECO:0000259|Pfam:PF21686};
GN   OrderedLocusNames=MCP_2125 {ECO:0000313|EMBL:BAI62197.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI62197.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
RN   [2] {ECO:0007829|PDB:5DMU}
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-293.
RX   PubMed=26405198; DOI=10.1093/nar/gkv965;
RA   Bartlett E.J., Brissett N.C., Plocinski P., Carlberg T., Doherty A.J.;
RT   "Molecular basis for DNA strand displacement by NHEJ repair polymerases.";
RL   Nucleic Acids Res. 44:2173-2186(2016).
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DR   EMBL; AP011532; BAI62197.1; -; Genomic_DNA.
DR   PDB; 5DMU; X-ray; 1.95 A; A=1-293.
DR   PDBsum; 5DMU; -.
DR   AlphaFoldDB; D1Z0H5; -.
DR   SMR; D1Z0H5; -.
DR   STRING; 304371.MCP_2125; -.
DR   KEGG; mpd:MCP_2125; -.
DR   PATRIC; fig|304371.9.peg.2166; -.
DR   eggNOG; arCOG04110; Archaea.
DR   InParanoid; D1Z0H5; -.
DR   OrthoDB; 147675at2157; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5DMU};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          28..280
FT                   /note="DNA ligase D polymerase"
FT                   /evidence="ECO:0000259|Pfam:PF21686"
SQ   SEQUENCE   295 AA;  33525 MW;  17A2962696A018F9 CRC64;
     MTEVLHIEGH DIKVTNPDKV LFPEDGITKG ELVDYYRRIS GVMVPLVRGR PMTMQRFPDG
     IGKEGFFQKE ASDYFPDWVH RATLELGKGG IQHQVVCDDA ATLVYLASQA MITPHVFLSR
     IDKVHYPDRL IFDLDPPDNN FETVRSAAKT IREALDAEGY PVYLMTTGSR GLHVVVPLDR
     SADFDTVRAF ARGFGEKLTK KYPDRFTIEL SKEKRRGRLF LDYLRNSYGQ TGVAPYGVRA
     RSGAPVATPI TWDELDDISG SQEYNIRNIM GRMDKRGDAW KYIDKDRTSI KNLDN
//