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Database: UniProt
Entry: A4YD25
LinkDB: A4YD25
Original site: A4YD25 
ID   DNLI_METS5              Reviewed;         598 AA.
AC   A4YD25;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   28-MAR-2018, entry version 70.
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=Msed_0150;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC
OS   15509 / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely
RT   thermoacidophilic archaeon Metallosphaera sedula provides insights
RT   into bioleaching-associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94327.1; -; Genomic_DNA.
DR   RefSeq; WP_011921295.1; NC_009440.1.
DR   ProteinModelPortal; A4YD25; -.
DR   SMR; A4YD25; -.
DR   STRING; 399549.Msed_0150; -.
DR   EnsemblBacteria; ABP94327; ABP94327; Msed_0150.
DR   GeneID; 5105003; -.
DR   KEGG; mse:Msed_0150; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000000242; 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   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    598       DNA ligase.
FT                                /FTId=PRO_1000072271.
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   598 AA;  67922 MW;  A9C70DF05DA44BB0 CRC64;
     MKFKLIAEYF DRLEKISSRI QLTSLLSDLF KNTEREVIDK VVYLIQGRLW PDFTGMPEIG
     MGEKFLIKAI AMAYGNKEEE VEKLYKNIGD LGEVAYSLRS KVKGVSILSF VGGNQEAGEL
     DVMEVYNELV KIATSTGEGS RDIKIRIFAG LIKKATPIEA KYLVRFVEGR LRLGIGDATV
     LDALAITFGG SADYRPIVER AYNLRADLGD IARVIATEGI EKLKNISPTP GIPIRPMLAE
     RLPDPEEIME KMNGKALVDY KYDGERAQIH RKGDKVTIFS RRMENITDQY IDVTEYVKQF
     VKGDNFIVEG EIVPVDPESG EMRPFQELMH RRRKNNIAEA IKEYPVNLFL FDLMFFEGED
     YTTKPLPERR AKLEEILASN DKVHIASHII ADRVDKLREY FYQAISEGAE GVMVKSIGPD
     SIYQAGSRGW LWIKLKRDYQ SEMADTVDLV VVGAFYGKGK RGGKFSSLLM AAYNPEKDVF
     ETVCKVASGF SDQELDEMQK KINELKREQK HPRVVSDMIP DVWVSPTLVA EVIGAEITIS
     PLHTCCRGEK GGLSIRFPRF IRWRDDKSPE DATTNQEIME MYSKQLKKIE EKPVDENI
//
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