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Database: UniProt
Entry: Q02093
LinkDB: Q02093
Original site: Q02093 
ID   DNLI_ACIAM              Reviewed;         600 AA.
AC   Q02093;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   15-MAR-2017, entry version 87.
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};
OS   Acidianus ambivalens (Desulfurolobus ambivalens).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Acidianus.
OX   NCBI_TaxID=2283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Lei 10 / DSM 3772 / JCM 9191;
RX   PubMed=1437556; DOI=10.1093/nar/20.20.5389;
RA   Kletzin A.;
RT   "Molecular characterisation of a DNA ligase gene of the extremely
RT   thermophilic archaeon Desulfurolobus ambivalens shows close
RT   phylogenetic relationship to eukaryotic ligases.";
RL   Nucleic Acids Res. 20:5389-5396(1992).
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; X63438; CAA45034.1; -; Genomic_DNA.
DR   PIR; S26383; S26383.
DR   ProteinModelPortal; Q02093; -.
DR   SMR; Q02093; -.
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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN         1    600       DNA ligase.
FT                                /FTId=PRO_0000059599.
FT   ACT_SITE    261    261       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     266    266       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     281    281       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     311    311       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     351    351       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     428    428       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     434    434       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   600 AA;  67618 MW;  8FCBFF36F2475DD8 CRC64;
     MEFKIIAEYF DRLEKISSRL QLTSLLADLF KKTDKNVIDK VVYIIQGKLW PDFLGMPELG
     IGEKFLIRAL SIATSVSDDE IEKMYKSVGD LGQVAFDIKQ KQQSASILAF LGAQKASKPL
     TVEKVYDDLA KVATSTGEGS RDIKIRLLAG LLKDASPLEA KYLVRFVDGR LRVGIGDATI
     LDALAITFGG GQNFRPIVER AYNLRADLGN IAKILANGGI EQLKNIKPQP GIPIRPMLAE
     RLSDPAEMLS KVGNIALVDY KYDGERGQIH KAGDKIFIFS RRLENITNQY PDVAEYISKY
     VKGNEFIVEG EIIPVDPETG EMRPFQELMH RKRKSDIHEA IKEYPVNVFL FDLMYYEGED
     YTVKPLSERR KKLESIVEDN DYVHIATHII TDNVEKLKEF FYQAISEGAE GVMVKSLAPD
     AIYQAGSRGW LWIKFKRDYQ SEMADTVDLV MVGAFHGKGR KGGKYSSFLM AAYNPDKDVF
     ETVCKVASGF TDAELDDLQK KIAELKRDTP HPRVVSTMVP DVWLTPALVA EIIGAEITIS
     PLHTCCKDQY AEGGLSIRFP RFIRWRPDKS PEDATTNREI LEMYKSQLKK IEEKPSDQSV
//
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