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Database: UniProt
Entry: A7IAA9
LinkDB: A7IAA9
Original site: A7IAA9 
ID   DNLI_METB6              Reviewed;         550 AA.
AC   A7IAA9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-OCT-2017, entry version 65.
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};
GN   OrderedLocusNames=Mboo_2156;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
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., Meincke L., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Zinder S., Richardson P.;
RT   "Complete sequence of Candidatus Methanoregula boonei 6A8.";
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; CP000780; ABS56670.1; -; Genomic_DNA.
DR   RefSeq; WP_012107728.1; NC_009712.1.
DR   ProteinModelPortal; A7IAA9; -.
DR   SMR; A7IAA9; -.
DR   STRING; 456442.Mboo_2156; -.
DR   EnsemblBacteria; ABS56670; ABS56670; Mboo_2156.
DR   GeneID; 5410132; -.
DR   KEGG; mbn:Mboo_2156; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000002408; 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; -; 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; 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    550       DNA ligase.
FT                                /FTId=PRO_0000365256.
FT   ACT_SITE    246    246       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     244    244       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     251    251       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     266    266       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     295    295       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     334    334       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     405    405       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     411    411       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   550 AA;  61583 MW;  9029C3918A446474 CRC64;
     MLFSEFAQVC EELEHLSGRL DMIEVISRAL PDLAPDELPV FVRFVMGRIF PDWSAQKLGI
     GPNLLYEAVR QAAGVKLETV ITRINQQGDV GRAVEDILAK KTQVSWSHQD LELVYVYNKL
     TGISSRGGVT SQKEKIRIAM LLLGDASPLE GRYLARIMLE ELRIGVGEGT VREAIAKAFM
     VDSALVEHAM QAINDLGEVA RLAKKGPTAL SDVHITPFHP VKMMLAQQGT IAGMIEDHGE
     IAAEYKYDGS RFQFHKEGAK ARMYSRRLED VSEALPDVID LLSKATSHDV ILDGEVIAIK
     DDRPMPFQSV LRRFRRRHDI AEAQEAIRMV PNVFDILYLD GETLIDLPFF ERRKKLETVV
     GKFVAPQVVS TDPQTIEQTY HDALAAGHEG IMLKVPASPY TPGQRGKNWI KIKPEVDTLD
     LAVIGAEWGE GKRAHVFGSF LVACQDQGKL IPLSRVATGF SDEQLTEVYD LLKDAVISRT
     GKEVRFEPEL VFEVGYAELQ VSPTYDAGFA LRFPRFIRIR DDKDTTEIET LESIRGRYQR
     QAKSAQAYTK
//
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