GenomeNet

Database: UniProt
Entry: Q46C04
LinkDB: Q46C04
Original site: Q46C04 
ID   DNLI1_METBF             Reviewed;         549 AA.
AC   Q46C04;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-SEP-2017, entry version 90.
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=Mbar_A1643;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70588.1; -; Genomic_DNA.
DR   RefSeq; WP_011306634.1; NC_007355.1.
DR   ProteinModelPortal; Q46C04; -.
DR   SMR; Q46C04; -.
DR   STRING; 269797.Mbar_A1643; -.
DR   PRIDE; Q46C04; -.
DR   EnsemblBacteria; AAZ70588; AAZ70588; Mbar_A1643.
DR   GeneID; 3625441; -.
DR   KEGG; mba:Mbar_A1643; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000008156; 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    549       DNA ligase 1.
FT                                /FTId=PRO_0000365258.
FT   ACT_SITE    214    214       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     212    212       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     219    219       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     234    234       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     310    310       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     387    387       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     393    393       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   549 AA;  61905 MW;  AFEDB817138AF856 CRC64;
     MERKEIKDSA YLFLGSIGPA FENITLGIGD KLALKAIAGA YRVSEEEVKK RYSRTGDLGD
     VAFELNQGEE KSLAIDEVFG SLKEIKEASG KGSQEEKTGL LSSILQRASP KEGKYIVRIV
     LGKLRLGFGD QFLLEAFSIA FTGDKKYVVK IKESYSVCTD IGELAESLAE QGPKALGHFS
     IKLGRPVRSM LAQRVKTFEE LEERIPGKKA AEEKYDGERV QIHKNGEEIK AFSRRLEDIT
     AQYPDVIEAV RKGILAKKIV LDGEIIAYVE GGKANDSTGE FYSFQRLMKR RRKYEVQKYT
     EICPVAVFFF DILYLEGNSL LKKPYPERRA ILEEHVKESE ILHLARRIVT DNLEEIEDFF
     NEALEKRLEG IIIKSMGRNS AYEAGKRSWF WLKWKEEYAS GMRETFDLAI IGKYYGRGKR
     KGSFGALLCA ILNGEEQRFE TFTKVGTGFT EADAKEIDSL LSEHIISEVP KNVLIKSRML
     PDIFVEPSLV IEVLGSEITE SPSHTAGQGE GDTGLALRFP RFLRIRHDKG PYDITTLTEV
     RNLKEGKSI
//
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