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Database: UniProt
Entry: A4WH24
LinkDB: A4WH24
Original site: A4WH24 
ID   DNLI_PYRAR              Reviewed;         584 AA.
AC   A4WH24;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   07-JUN-2017, entry version 65.
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=Pars_0076;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13514 / JCM 11321;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C.,
RA   Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) 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; CP000660; ABP49691.1; -; Genomic_DNA.
DR   ProteinModelPortal; A4WH24; -.
DR   SMR; A4WH24; -.
DR   EnsemblBacteria; ABP49691; ABP49691; Pars_0076.
DR   KEGG; pas:Pars_0076; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001567; 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.
FT   CHAIN         1    584       DNA ligase.
FT                                /FTId=PRO_1000049875.
FT   ACT_SITE    251    251       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     249    249       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     256    256       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     271    271       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     301    301       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     341    341       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     416    416       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     422    422       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   584 AA;  64746 MW;  D65376C5A129E101 CRC64;
     MQFGELVKAL AAVESTTQRS VMVKLLASLF KKALPEEIDK VIYLILGDLR PPWEGLELGV
     GEKLCLRALA KATGTSQAEL ESMYKKTGDI GEAARRALAS SKRPGLLAFG SQKPLEVSEV
     YDALIKVARA TGEGAQDMKI ALLSSLFARS SPEEGKYIAR FVVGKLRLGV ADMTIIEALA
     DAYGVRKEDL ERAYHVYPDL GHLAKLVASG KPLDEVKVTP GVPVLPMLAQ RLSSSSEILA
     KLGGAAICEY KYDGERAQIH ISQSGVRIFS RRLEDITHAY PDVVKAVREA VSAREAILEG
     EIVAVDPDTG EMLPFQELMH RKRKHEVAAA MEMYPTVLYL FDIVYVDGED LTNEPLIYRR
     VKLSEIVHES DKVQIAKWQM FDDPDTVDVF FHEAVSVGTE GLICKSPTSE YEMGARGWNW
     IKYKRDYKSE MIDTVDLVVV GAFYGRGKRA GLYGAFLLAA YDPSSDMFYT VCKVGSGFTD
     ADLKKMYEIL QPLKIPHRHP RVSSKMEADV WFVPQVVIEV IGAEITLSPL HTCCLGAVRP
     GVGLAVRFPR FTGRYRTDKG PEQATTVAEM LELYKRQKKV AQPE
//
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