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-NOV-2008, entry version 53.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=lig; OrderedLocusNames=APE_1094.1;
OS   Aeropyrum pernix.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=56636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1;
RX   MEDLINE=99310339; 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).
CC   -!- FUNCTION: This protein seals, during DNA replication, DNA
CC       recombination and DNA repair, nicks in double-stranded DNA (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
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DR   EMBL; BA000002; BAA80079.2; -; Genomic_DNA.
DR   PIR; G72709; G72709.
DR   RefSeq; NP_147713.2; -.
DR   GeneID; 1445787; -.
DR   GenomeReviews; BA000002_GR; APE_1094.1.
DR   KEGG; ape:APE_1094.1; -.
DR   NMPDR; fig|272557.1.peg.821; -.
DR   HOGENOM; Q9YD18; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR   HAMAP; MF_00407; -; 1.
DR   InterPro; IPR000977; DNA_ligase.
DR   InterPro; IPR012309; DNA_ligase_A_C.
DR   InterPro; IPR012310; DNA_ligase_A_M.
DR   InterPro; IPR012308; DNA_ligase_A_N.
DR   InterPro; IPR016059; DNA_ligase_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
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   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; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    602       DNA ligase.
FT                                /FTId=PRO_0000059600.
FT   ACT_SITE    264    264       N6-AMP-lysine intermediate (By
FT                                similarity).
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
//