DNLI_METPE
ID DNLI_METPE Reviewed; 556 AA.
AC B8GGB8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=Mpal_2781;
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. {ECO:0000255|HAMAP-
CC Rule:MF_00407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={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}.
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DR EMBL; CP001338; ACL18036.1; -; Genomic_DNA.
DR RefSeq; WP_012619355.1; NC_011832.1.
DR AlphaFoldDB; B8GGB8; -.
DR SMR; B8GGB8; -.
DR STRING; 521011.Mpal_2781; -.
DR EnsemblBacteria; ACL18036; ACL18036; Mpal_2781.
DR GeneID; 7272662; -.
DR KEGG; mpl:Mpal_2781; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OMA; WLFEESY; -.
DR OrthoDB; 52275at2157; -.
DR Proteomes; UP000002457; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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; 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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..556
FT /note="DNA ligase"
FT /id="PRO_1000134728"
FT ACT_SITE 247
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
SQ SEQUENCE 556 AA; 61297 MW; 6665DC65DB81AE57 CRC64;
MQFSIFAQTC AALEAQNGRL EMKHAISVIL PSLSGEDLPI FIRFLMGKIF PDWSPQKLGI
GPNLLYEAVA YVAGTKKTAL VDLINRTGDA GLAIEQFLAT KEQTAFFTED PSLAEVYAAC
TRIAASAGGR SQRERLLVLR QLFGNVSPFE ARYLARLILG ELRIGIGEGT VRDAIAEAYT
VEPAQVEHAM QALNDLGEVA LRAREGEEGL IHLSIAPFRP VKMMLAQAGT TIPEMLAAHG
EVAVEFKYDG TRFQFHKEGK TCRIYSRKLE EVTDAVPEVG EALLGATDHD VILDGEVIAI
GADGRPLPFQ TVLRRFRRKH GIAAAREAIT LVPRVFDILY RDGETLIDLP FQSRRAILSA
TIGPEYLAPQ QVLSSAEAVD LLYLEAMAEG HEGVMLKDLL SLYSPGVRGK HWVKIKPEVE
TLDLVVIGAE WGEGRRARTF GSFLLACLDQ GVFRAVSKVA TGISDEQLQE LYTLFKDQVI
AESGNTVTFE PTVIFEVGYA EIQKSPSYES GYALRFPRFV QVRDDKAVEE IETLESLTTR
YLAQKTQANG QPEFTL
