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Database: UniProt/SWISS-PROT
Entry: DNLI_ANASK
LinkDB: DNLI_ANASK
Original site: DNLI_ANASK 
ID   DNLI_ANASK              Reviewed;         513 AA.
AC   B4UIS1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-OCT-2017, 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};
GN   OrderedLocusNames=AnaeK_4290;
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=447217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikiva G., Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) 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; CP001131; ACG75493.1; -; Genomic_DNA.
DR   RefSeq; WP_012528245.1; NC_011145.1.
DR   ProteinModelPortal; B4UIS1; -.
DR   SMR; B4UIS1; -.
DR   PRIDE; B4UIS1; -.
DR   EnsemblBacteria; ACG75493; ACG75493; AnaeK_4290.
DR   KEGG; ank:AnaeK_4290; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000001871; 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.
FT   CHAIN         1    513       Probable DNA ligase.
FT                                /FTId=PRO_0000365218.
FT   ACT_SITE    215    215       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     213    213       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     220    220       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     304    304       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     376    376       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     382    382       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   513 AA;  54097 MW;  53187E6F37F04B77 CRC64;
     MLLAELAEVS RAVAATPARL EKVALLSEAL RRLAPDERAV GASWLAGDLA GGRVGIGAAT
     LRAALEAAPP GAAGPGLTVG EVDAALRRIA AAAGPGSGAA RRRELDALLA RAGDPERRFL
     AALVLGELRQ GALEGVLSDA VARVAGLPGA EVRRAAMLAG ALPPVAEAAL AEGAAGLARF
     RLRVGEPVSP MLAQTAAGVD EALRALGGEA ALEWKLDGAR IQAHRDGDEV RVFSRSLREV
     TAAVPEVVAL LRAAPEPLLV LDGEAIALRA DGTPEPFQVT MRRFGRKLDV ERLAPDLPLT
     AFFFDALVAG GGELLGAPER ERWAALERAI PAERRVPRLV TGDAAEARAF LEEALARGQE
     GVVAKALDAP YEAGRRGAAW LKVKRAHTLD LVVLAAEWGS GRRRGWLSNL HLGARDPATG
     EFVMLGKTFK GMTDAMLAWQ TERLKALATG PLDAWQVPVR PELVVEVAFD GIQASPRYPG
     GLALRFARVK RYREDKRPED ADTIETVRGL YGG
//
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