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Database: UniProt/SWISS-PROT
Entry: DNLI_ANAD2
LinkDB: DNLI_ANAD2
Original site: DNLI_ANAD2 
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   07-JUN-2017, entry version 61.
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=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.,
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   Ovchinnikova G., 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
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; CP001359; ACL67629.1; -; Genomic_DNA.
DR   RefSeq; WP_015935329.1; NC_011891.1.
DR   ProteinModelPortal; B8JBM1; -.
DR   SMR; B8JBM1; -.
DR   EnsemblBacteria; ACL67629; ACL67629; A2cp1_4312.
DR   KEGG; acp:A2cp1_4312; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000007089; 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; 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_1000134725.
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;  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
//
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