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Database: UniProt
Entry: Q6L195
LinkDB: Q6L195
Original site: Q6L195 
ID   DNLI_PICTO              Reviewed;         585 AA.
AC   Q6L195;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   25-OCT-2017, entry version 85.
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}; OrderedLocusNames=PTO0672;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT43257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE017261; AAT43257.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048059460.1; NC_005877.1.
DR   ProteinModelPortal; Q6L195; -.
DR   SMR; Q6L195; -.
DR   STRING; 263820.PTO0672; -.
DR   EnsemblBacteria; AAT43257; AAT43257; PTO0672.
DR   GeneID; 2845337; -.
DR   KEGG; pto:PTO0672; -.
DR   PATRIC; fig|263820.9.peg.707; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000000438; 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    585       DNA ligase.
FT                                /FTId=PRO_0000059610.
FT   ACT_SITE    250    250       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     248    248       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     255    255       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     341    341       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     418    418       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     424    424       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   585 AA;  66334 MW;  9AED5BCA48C11F94 CRC64;
     MDFSDVASYF SRMEETTKRL ELTSILAELF KRSGDDLKKL VYLVQGKLMP DYLGIELGLS
     DKLIIKSLSK ASGRSEEDIN RIFSRLGDLG STAEEISSSG IQRPLLKESL TVDYVYNQLI
     KISGYTGHGS IKTKMDAYID LLINSGPMEI KYITRIITGK LRLGVADSTI LDGLIEAFSE
     KKYADDIETA YNFHPDLGYI AENLMMGNIN ELLNAGPVPL IPFKVMLAER LQSISDIRNK
     MGHNASYEYK YDGLRTQLHF LKGGIKIFSR GLEETTSSFP DIVQNFKSYY SFDSCIIDGE
     SVPYNPETGE LYPFQMVSKR RGRKYELTEK TREVPIVMFI FDILYLNGKS LVNLPYPERR
     SILEKNFKEN EYFKLAKRIV SDDEHDIMKF FERSIEEGCE GIVAKSNGID SIYRAGARGW
     LWIKFKRDYQ SELSDSLDLV VVGAFDGHGR RKGTFGALLL ACYNSKDDTF ETVCKLGSGF
     TDEMLSEMPR LLGDKIVEKK PARVNSSMEP DHWIYPSLVL EIRGAEITVS PVHTCAMNII
     EKGSGLALRF PRLIKPRDDK KPEDATTTNE IIEMYKAQKK VIEKS
//
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