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Database: UniProt/SWISS-PROT
Entry: DNLI_METLZ
LinkDB: DNLI_METLZ
Original site: DNLI_METLZ 
ID   DNLI_METLZ              Reviewed;         546 AA.
AC   A2SR38;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   28-MAR-2018, entry version 74.
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=Mlab_0620;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A.,
RA   Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K.,
RA   Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain
RT   Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06794.1; -; Genomic_DNA.
DR   RefSeq; WP_011832995.1; NC_008942.1.
DR   ProteinModelPortal; A2SR38; -.
DR   SMR; A2SR38; -.
DR   STRING; 410358.Mlab_0620; -.
DR   EnsemblBacteria; ABN06794; ABN06794; Mlab_0620.
DR   GeneID; 4795702; -.
DR   KEGG; mla:Mlab_0620; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; MLAB410358:G1G83-656-MONOMER; -.
DR   Proteomes; UP000000365; 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; 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; 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; 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    546       DNA ligase.
FT                                /FTId=PRO_0000365254.
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   546 AA;  61358 MW;  E830A47BEE2DAF24 CRC64;
     MQFVEFAEIC NTIEGTSSRL ATADILAEKF PLLTEEELPV FVRFMRGRLF PDWSSEKLGF
     GPNLLYDALA YVIGKKRSYV VSAINNAGDI GKVVESLIEK REQTMFFSEE LDLLDVNARF
     LQMAKSSGRR SQQERLRSAQ YLLSNATPLE GRYLARLMLE EMRIGVGEGV VKDAVSKAFG
     VPSDIVEHAH QALNDLGEVA FLAKTDPSRL SNVHITAFRP VKMMLAQQGS ITSMVETHGT
     LAAENKYDGS RFQFHKSGGK CAIYSRRLEE MTASLPDVVK MLDKATDHDV IIDGEVIAIM
     NGKPMPFQTI LRRIRRKHDV GDAQEAITLL PWVFDILAAD GETLIDLPFR ERRKILESVM
     NAYVAPQLVS DSAEEIEAYY HSSLDNGNEG IMLKVLDSPY LPGNRGKLWI KIKPEVDTID
     LVVTAAEWGE GKRAKMFGSF LLACQDENGD LLEISRVATG IDDSMLSTLY DLFKDKIIAE
     KGKTVTFEPD VVFEVGYAEL QKSTNYEAGY ALRFPRFVRL RDDKDVSEIE TLESLTRRYS
     LQNKEE
//
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