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Database: UniProt
Entry: Q5YNY7
LinkDB: Q5YNY7
Original site: Q5YNY7 
ID   DNLI_NOCFA              Reviewed;         523 AA.
AC   Q5YNY7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   07-JUN-2017, entry version 98.
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};
GN   OrderedLocusNames=NFA_52520;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD60104.1; -; Genomic_DNA.
DR   RefSeq; WP_011211786.1; NC_006361.1.
DR   ProteinModelPortal; Q5YNY7; -.
DR   SMR; Q5YNY7; -.
DR   STRING; 247156.nfa52520; -.
DR   PRIDE; Q5YNY7; -.
DR   EnsemblBacteria; BAD60104; BAD60104; NFA_52520.
DR   KEGG; nfa:NFA_52520; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000006820; 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; -; 2.
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; 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    523       Probable DNA ligase.
FT                                /FTId=PRO_0000365235.
FT   ACT_SITE    212    212       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     210    210       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     217    217       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     232    232       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     261    261       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     317    317       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     388    388       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     394    394       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   523 AA;  56457 MW;  398B9736FF4F94BA CRC64;
     MLFADVVRTS EAVRATRSRK TKVAALAELL RAAESAELAP VVAWLSGELR QGRIGTGWRT
     LTGVRVPPAL DAALEVATVD AIFDELAAVS GAGSGNRRKE LLTRLWSAAT EPEQEFLLRL
     LTGELRQGAL TALVAEAVAA AADVPVEQVR RAYMLSGQLP VTAEAALRGG AAALAEFRLE
     VGRPIQPMLA APGASLEEAM TEFGGEVSVE HKLDGARIQV HRDGDRIAVF TRTLRDITAG
     VPELVELVAR LDCTSVVLDG ETLALTDAGR PRPFQETMSR FATADPARAA EVDLPPGTPV
     VPPVSSTREL LLHPYFFDCL HLDGRDLLDA PLSERRAALL AVVGEHAIPA LIRPEPEAAA
     EYFDGALAAG HEGLMVKSLS APYAAGRRGR SWQKIKPTHT LDLLVLGAEW GYGRRTGYLS
     NLHLGARDPR TGEPVMVGKT FKGLTDALLA WQTAEFPRHE RARDEHTVYL WPELVVEIAL
     DGVQVSPRYP GGVALRFARV VRYRPDKTPD QADTIDTVRG LLP
//
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