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Database: UniProt
Entry: Q8PVR7
LinkDB: Q8PVR7
Original site: Q8PVR7 
ID   DNLI1_METMA             Reviewed;         579 AA.
AC   Q8PVR7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   07-JUN-2017, entry version 101.
DE   RecName: Full=DNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1 {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig1 {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=MM_1895;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31591.1; -; Genomic_DNA.
DR   RefSeq; WP_011033828.1; NC_003901.1.
DR   ProteinModelPortal; Q8PVR7; -.
DR   SMR; Q8PVR7; -.
DR   STRING; 192952.MM_1895; -.
DR   EnsemblBacteria; AAM31591; AAM31591; MM_1895.
DR   GeneID; 24878633; -.
DR   KEGG; mma:MM_1895; -.
DR   PATRIC; fig|192952.21.peg.2183; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000000595; 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; 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; 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    579       DNA ligase 1.
FT                                /FTId=PRO_0000365259.
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     296    296       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     342    342       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     419    419       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     425    425       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   579 AA;  65867 MW;  9E11E66075B8DEEC CRC64;
     MRFKELAELF EELEKTTSHR EIVRKISEFF KNLRGDEVKD SAYLFLGSTG PAFENTTLGI
     KDMLAIRAIA GAYGVTREDV RKRYARTGDL GDVAFELSKK RESSLTIEDV FQRLLQIRET
     SGKGSQEEKT ALFSDILQKA TPEEGKYIVR LVLGRLRLGF GDQFLLEAFA IAFTGDKKHA
     AKIKESYSVC TDIGELAKIL AENGARATGF ISIKPGRPVK SMLSQRVESF EELEKRVKGK
     KAAEEKYDGE RVQVHKTGEG IKAFSRRLED ITSQYPEIIE DVRKTVPANE IVLDGEIVAY
     AELERNGNRI EEFYPFQNLM QRRRKYEIEN YRKKCPVAVF FFDILYLNGE PLLKRPYPER
     RALLEMNVVE SGIIRLSKRI VTESVEEIED FFNETIEKGL EGIVVKSMSS NSYYEAGKRS
     WFWFKWKQEY SEGMRETFDL VVVGSYYGRG RRKGSFGALL CAVLNKEGQR FETLTKVGTG
     FTEADAEEIN RLLSDHIVSE IPKGVSIKKG MLPDIFIEPA VVIEVLGSEI TNSPGHTAGE
     GEEETGLALR FPRFLRIRHD KTPYDAMTVK EVRDLKDGT
//
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