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Database: UniProt/SWISS-PROT
Entry: DNLI_AQUAE
LinkDB: DNLI_AQUAE
Original site: DNLI_AQUAE 
ID   DNLI_AQUAE              Reviewed;         584 AA.
AC   O67398;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   23-MAY-2018, entry version 121.
DE   RecName: Full=Probable 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}; OrderedLocusNames=aq_1394;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC07362.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE000657; AAC07362.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70421; D70421.
DR   RefSeq; NP_213963.1; NC_000918.1.
DR   ProteinModelPortal; O67398; -.
DR   SMR; O67398; -.
DR   STRING; 224324.aq_1394; -.
DR   PRIDE; O67398; -.
DR   EnsemblBacteria; AAC07362; AAC07362; aq_1394.
DR   GeneID; 1192929; -.
DR   KEGG; aae:aq_1394; -.
DR   PATRIC; fig|224324.8.peg.1092; -.
DR   eggNOG; ENOG4107TRG; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   InParanoid; O67398; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG091H09SJ; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
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    584       Probable DNA ligase.
FT                                /FTId=PRO_0000059623.
FT   ACT_SITE    250    250       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     248    248       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     255    255       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     339    339       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;  66945 MW;  CB96A7451E9BDC1D CRC64;
     MEYRILAEFY ERIEKTTSRI EMVSSLVELF KQTPKELIDK VVYLSIGKIA PEYTGLDYNF
     GEKLAIRALS RVLKIPALEI EKRVRQEGDL GEAGRKLYEE LGFKPEGTLT VEEVYNGLLN
     IAKAVGIGSQ ERKISIFASL LKKATPLEAK YLLRTITERL RLGIGDNTIL EALSIAFTGS
     SVNREVVERA YNLTSDLGYV AKILAEKGLE GVKQVKIQVG RPVRPMLAER MSSPILILRK
     LGGKCGAEYK YDGERIQAHR KGDEFYLFSR RLENITHQYP DLIEFLKEAI PHDFIVELEA
     VVIDPASGEI RPFQELMHRK VKYVTKYHIT KYPVAGFLFD IIYLDGEDLT LKPYPERREI
     LEKVVKRTDR IGLVPRKIVD NVEDLENFFY QAIEEGCEGL VCKSLAPNSI YQAGKRGFLW
     IKYKRDYKSV LADTLDLVVV GGFYGKGQRK GTFGSLLMAC YDPESDMFKT VTKVGTGFTE
     DDFKKLEEIL MPRKLNHRHP RVNSILEADM WFEPYLVLEI TGAELTLSPV HTCGWGKVSP
     NRGIGLRFPR FTGRYRFDKR PEDATTEQEI IEMYRMQRKI RVRS
//
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