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Database: UniProt/SWISS-PROT
Entry: DNLI_ANADF
LinkDB: DNLI_ANADF
Original site: DNLI_ANADF 
ID   DNLI_ANADF              Reviewed;         519 AA.
AC   A7HID3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-OCT-2017, entry version 75.
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};
GN   OrderedLocusNames=Anae109_4301;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Fields M., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter sp. Fw109-5.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000769; ABS28479.1; -; Genomic_DNA.
DR   RefSeq; WP_012099123.1; NC_009675.1.
DR   ProteinModelPortal; A7HID3; -.
DR   SMR; A7HID3; -.
DR   STRING; 404589.Anae109_4301; -.
DR   PRIDE; A7HID3; -.
DR   EnsemblBacteria; ABS28479; ABS28479; Anae109_4301.
DR   KEGG; afw:Anae109_4301; -.
DR   eggNOG; ENOG4107QIM; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000006382; 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; -; 2.
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; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    519       Probable DNA ligase.
FT                                /FTId=PRO_0000365217.
FT   ACT_SITE    213    213       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     211    211       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     218    218       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     233    233       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     262    262       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     302    302       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     374    374       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   519 AA;  54767 MW;  B7FAE8869DBF7AE2 CRC64;
     MQLAELVQTS DVVARTAGRL EKIARLADAL RGLAPEERLA GASWLAGELR QGRIGLGPAA
     VRAALEATAP ADAPALAVRE VDASLDRLAA ARGAGSGRER AALLAALLAR ASADERDFLA
     RLVLGELRQG ALEGVLVEAV ARAAAVPAGE VRRAVMMAGA LPPVAEAALA EGAAGLSRFR
     LRLLEPVQPM LAQPAAGVDE ALAALGEAAL EWKLDGARVQ VHKDGGEVRV FSRALRDVTP
     AVPEVVEAVR RLPASSLVLD GEAIALRGDG APEPFQVTMR RFGRKLDVAG LREGVPLSVL
     FFDALHTAGE DLIARPASER HLALAAAVPD ALRVPRLVTS DGAAAAAFLE GALARGHEGL
     LAKSLTAPYE AGRRGASWLK VKRAHTLDLV VLAAEWGSGR REGFLSNLHL GARDPEGGGF
     VMLGKTFKGM TDAMLAWQTE RFRALALGST DGYVVHLRPE LVVEVAFDGL QESSRYPGGL
     ALRFARVKRY REDKRPEEAD TIATVRALHA RQVAAERGT
//
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