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Database: UniProt/SWISS-PROT
Entry: DNLI_METHJ
LinkDB: DNLI_METHJ
Original site: DNLI_METHJ 
ID   DNLI_METHJ              Reviewed;         547 AA.
AC   Q2FTH4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-OCT-2017, entry version 78.
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=Mhun_2882;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC
OS   100397 / JF-1).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D.,
RA   Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J.,
RA   Stams A.J.M., Boone D.R., Richardson P.;
RT   "Complete sequence of Methanospirillum hungatei JF-1.";
RL   Submitted (JAN-2006) 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; CP000254; ABD42574.1; -; Genomic_DNA.
DR   RefSeq; WP_011449827.1; NC_007796.1.
DR   ProteinModelPortal; Q2FTH4; -.
DR   SMR; Q2FTH4; -.
DR   STRING; 323259.Mhun_2882; -.
DR   EnsemblBacteria; ABD42574; ABD42574; Mhun_2882.
DR   GeneID; 3924177; -.
DR   KEGG; mhu:Mhun_2882; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001941; 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    547       DNA ligase.
FT                                /FTId=PRO_0000365261.
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   547 AA;  61698 MW;  EEB45E15FAC1AA3F CRC64;
     MIFLEFAELC SRLEKISGRL ETISILAETI SSLSDDDLPH FCRLILGKPF PEWSGKKLGV
     GPNLLYEAVA YVTGRKREEV IDRLSRVGDA GAAVEELLSQ KSQTSFFTVE LTLADIMAAL
     IEISGMEGGR SQKEKVRVIQ RILSSASPLE GHYITAILLE DFRIGVGEGN LRDAIAQAFS
     VDPNLVEYAN QVRNDMGEVA VLARKGEEAL RSVRLVPFHP VRMMLARQGT ISGVLKEGDP
     VAVEFKYDGA RFQFHKQNKT CRMYSRRLEE VTNAMPDVVA LLDEALPDDI IVDGEVIAVQ
     GGHPMPFQTV LRRFRRKHNV AEAADAITMI PNLFDILYYN QEMLIDLPFR ERRNILTQVA
     SRYVTPQLVS DDETEIEAYY HTALDAGHEG VMLKLQGSRY TPGVRGKDWV KIKPEADTLD
     LVVTGAEWGE GKRAHVFGSF LLSVRDDDRL VPISRVATGF SDEQLIWLFD TLQDDIIRKD
     GKMVYFEPRL VFEIGYSEIQ KSPNYEGGYA LRFPRFIEVR EDKDLKEANT AEDVEERYIQ
     THSSLNT
//
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