GenomeNet

Database: UniProt
Entry: A8MDU6
LinkDB: A8MDU6
Original site: A8MDU6 
ID   DNLI_CALMQ              Reviewed;         603 AA.
AC   A8MDU6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-OCT-2017, entry version 71.
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=Cmaq_1124;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307
OS   / IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
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., Saunders E., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T.,
RA   Lowe T.M., Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-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; CP000852; ABW01952.1; -; Genomic_DNA.
DR   RefSeq; WP_012186171.1; NC_009954.1.
DR   ProteinModelPortal; A8MDU6; -.
DR   SMR; A8MDU6; -.
DR   STRING; 397948.Cmaq_1124; -.
DR   EnsemblBacteria; ABW01952; ABW01952; Cmaq_1124.
DR   GeneID; 5710004; -.
DR   KEGG; cma:Cmaq_1124; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001137; 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; 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    603       DNA ligase.
FT                                /FTId=PRO_0000365243.
FT   ACT_SITE    264    264       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     262    262       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     269    269       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     285    285       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     315    315       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     355    355       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     432    432       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     438    438       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   603 AA;  67561 MW;  616703AB3A417D84 CRC64;
     MESDLEFSNI VSVLKLVEAT TQRTVMAKAL SSLLAKTPPQ VIDKVIYFLL GSLRPDWEGV
     ELGLAERLTL RAISMATGLP IRQVEELYKK LGDAGEVAKR AAEIKRSKGG GGTIFDFIDT
     GPKRRLTISK VYDTLMAIAK ASGEGAQDTK VKLLSSLLTD AEPDEAKYIT RFVIGRLRLG
     VADMTILDAL SDAFDVNRDL LEKAYHVYPD LGKIAKTLAE GGEEAVKAIK VTPGVPIQPM
     LAERLSSPKE ILNKLGGVAI CEFKYDGERM QIHKLKDGTV KIFSRRMEDI TNQYPDVAEY
     AREAIDAEEF IVEGEGVAID PDTGEFKPFQ ELMHRKRKHN IKEAIEEYPI NLYLFDVMYV
     NGQDLTDLPL PDRKKVLFSI IKPHEHVHHA DWIITDDADS LEKFFLDAIS SGCEGVMCKS
     VKLGSVYEMG ARGWLWIKYK RDYKSELSDT MDLVVVGAFW GRGKRAGTYG ALLLAAYDPD
     SDQFYTVCKV GSGFTDEDLK KLPQMLEPYK IPHRHPRVVS KMEPDIWFTP GLVLEITGAE
     ITMSPLHTCC SVMLKGDVGL AIRFPRFTGR YRTDKRPEDA TTVKEIFEMY SNQKKVKLTD
     QVP
//
DBGET integrated database retrieval system