GenomeNet

Database: UniProt
Entry: Q9YD18
LinkDB: Q9YD18
Original site: Q9YD18 
ID   DNLI_AERPE              Reviewed;         602 AA.
AC   Q9YD18;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   25-OCT-2017, entry version 107.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:12935888};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:12935888};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP/ADP] {ECO:0000305};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=APE_1094.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC
OS   100138 / K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y.,
RA   Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H.,
RA   Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H.,
RA   Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y.,
RA   Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y.,
RA   Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic
RT   crenarchaeon, Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=12935888; DOI=10.1016/S0014-5793(03)00821-4;
RA   Jeon S.J., Ishikawa K.;
RT   "A novel ADP-dependent DNA ligase from Aeropyrum pernix K1.";
RL   FEBS Lett. 550:69-73(2003).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. Can also
CC       use ADP, but not NAD(+). {ECO:0000269|PubMed:12935888}.
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       ECO:0000269|PubMed:12935888}.
CC   -!- CATALYTIC ACTIVITY: ADP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + phosphate. {ECO:0000269|PubMed:12935888}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12935888};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:12935888};
CC       Note=Less active with Ca(2+) or Co(2+). Not active with Cu(2+),
CC       Zn(2+), Sr(2+) or Ni(2+). {ECO:0000269|PubMed:12935888};
CC   -!- ENZYME REGULATION: Inhibited in the presence of 100 mM KCl, NaCl
CC       or NH(4)Cl. {ECO:0000269|PubMed:12935888}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:12935888};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:12935888};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12935888}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
DR   EMBL; BA000002; BAA80079.2; -; Genomic_DNA.
DR   PIR; G72709; G72709.
DR   ProteinModelPortal; Q9YD18; -.
DR   SMR; Q9YD18; -.
DR   STRING; 272557.APE_1094.1; -.
DR   EnsemblBacteria; BAA80079; BAA80079; APE_1094.1.
DR   KEGG; ape:APE_1094.1; -.
DR   PATRIC; fig|272557.25.peg.768; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BRENDA; 6.5.1.1; 171.
DR   Proteomes; UP000002518; 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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    602       DNA ligase.
FT                                /FTId=PRO_0000059600.
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     284    284       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     314    314       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     354    354       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     431    431       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     437    437       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   602 AA;  67748 MW;  AD1DC7521FAFD814 CRC64;
     MPFKPVAEAF ASMERITSRT QLTLLLTRLF KSTPPGAIGI VVYLIQGKLG PDWKGLPELG
     VGEKLLVKAI ALAYKATEER VERLYKSVGD LGSVAERLSR EYRSRAARAV TLEAFMAGGG
     EALTVRRVYN TLYRIAMAQG EGSRDIKLRL LAGLLADAEP VEAKYIVRFV EGRLRVGVGD
     ATVLDALAMA FGGGAHARPV IERAYNLRAD LGYIAEVVAR EGVDALRGVK PQVGVPIRPM
     LAERGRDPAE ILRKVGGRAV VEYKYDGERA QIHKKDGEVY IYSRRLENIT RMFPDVVEMA
     RKGLKAGEAI VEGEIVAVDP DNYEIQPFQV LMQRKRKHDI HRVMREVPVA VFLFDALYVD
     GEDLTSKPLP ERRRRLKEIV VETPLWRLAE SIETSDPEEL WTFFLKAIEE GAEGVMVKAV
     HRDSVYTAGV RGWLWVKLKR DYKSEMMDTV DLVVVGAFYG RGKRGGKLSS LLMAAYDPDR
     DVFPTVCKVA TGFTDEELDR MNEMLKKHII PRKHPRVESR IEPDVWVEPA LVAEILGAEL
     TLSPMHTCCL NTVRPGVGIS IRFPRFIRWR DDKSPEDATT THELLEMYKR QLRRVEEPAE
     QV
//
DBGET integrated database retrieval system