ID   DNLI_ANAD2              Reviewed;         513 AA.
AC   B8JBM1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=Probable 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=A2cp1_4312;
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001359; ACL67629.1; -; Genomic_DNA.
DR   RefSeq; WP_015935329.1; NC_011891.1.
DR   SMR; B8JBM1; -.
DR   PRIDE; B8JBM1; -.
DR   EnsemblBacteria; ACL67629; ACL67629; A2cp1_4312.
DR   KEGG; acp:A2cp1_4312; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   BioCyc; ADEH455488:G1GUO-4359-MONOMER; -.
DR   Proteomes; UP000007089; 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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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; PS00333; DNA_LIGASE_A2; 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.
FT   CHAIN           1..513
FT                   /note="Probable DNA ligase"
FT                   /id="PRO_1000134725"
FT   ACT_SITE        215
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         213
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         220
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         235
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         264
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         304
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         376
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT   BINDING         382
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
SQ   SEQUENCE   513 AA;  54060 MW;  A4CCC38389CAB126 CRC64;
     MLLAELAEVS RAVAATPARL EKIARLAEAL RRLAPDERAV GASWLAGDLP GGRIGIGGAT
     VRAALDAAPA EGGGPGLTVA EVDAALGRIA TASGAGSAGA RRRELDALLA RAGAPERWFL
     AALLLGELRQ GALEGVLADA VARAAGLPAA EVRRAAMLAG ALPPVAVAAL SEGAAGLARF
     RLRVGEPVSP MLAQTAADVE EALRALGGEA ALEWKLDGAR IQAHRDGGEV RVFSRSLRDV
     TAAVPEVVAL LRAAPEPRLV LDGEAIALRA DGTPEPFQVT MRRFGRRLDV ERLAPDLPLT
     AFFFDALVAG GAELLASPER VRWAALERAV PAEQRVPRLV TRDPAEAGAF LEDALARGQE
     GVVAKALDAP YEAGRRGAAW LKVKRAHTLD LVVLAAEWGS GRRRGWLSNL HLGARDPSTG
     GFVMLGKTFK GMTDAMLAWQ TERLKALATG PLDAWQVPVR PELVVEVAFD GIQSSPRYPG
     GLALRFARVK RYREDKRPED ADTIETVRGL YGG
//