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Database: UniProt/SWISS-PROT
Entry: DNLI_STRGG
LinkDB: DNLI_STRGG
Original site: DNLI_STRGG 
ID   DNLI_STRGG              Reviewed;         511 AA.
AC   B1W5J2;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   18-JUL-2018, entry version 71.
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=SGR_6320;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(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; AP009493; BAG23149.1; -; Genomic_DNA.
DR   RefSeq; WP_012381855.1; NC_010572.1.
DR   ProteinModelPortal; B1W5J2; -.
DR   SMR; B1W5J2; -.
DR   STRING; 455632.SGR_6320; -.
DR   EnsemblBacteria; BAG23149; BAG23149; SGR_6320.
DR   GeneID; 6211366; -.
DR   KEGG; sgr:SGR_6320; -.
DR   PATRIC; fig|455632.4.peg.6478; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   BioCyc; SGRI455632:G1G2X-6424-MONOMER; -.
DR   Proteomes; UP000001685; 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; 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.
FT   CHAIN         1    511       Probable DNA ligase.
FT                                /FTId=PRO_0000365241.
FT   ACT_SITE    210    210       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     208    208       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     230    230       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     377    377       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     383    383       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   511 AA;  54767 MW;  715B6B5D62E79FDB CRC64;
     MLLAELAQVS LEVAATSARS RKTALLAGLF RNAGPEDVPV VIPYLAGRLP QGRIGVGWRS
     LGEPVEPACD PTLTVTGVDA ELTALAATSG PGSQARRRER LRTLFAAATA DEQRFLRALL
     TGEVRQGALD AVAADALAHA AGAPPADVRR AVMLAGSLQD VATVLLADGP GALADFRLTV
     GRPVQPMLAR SAASVGEALD KLGPCAVEEK LDGIRVQVHR DGERIRAYTR TLDDITDRLP
     ELVSAVAALH ARRFVLDGEL IALGEDGRPR PFQETASRVG SRRDVAGAAA HVPVVPVFFD
     ALRVDGEDLL DRPFADRHAA LARLLPDDLR VRRTVVADPD APEARAAADA FLAATLERGH
     EGVVVKDLAA AYSAGRRGAS WLKVKPVHTL DLVVLAVERG SGRRTGKLSN LHLGARRPDG
     TFAMLGKTFK GLTDALLDWQ TARLRELATD DDGHVVTVRP ELVVEIAYDG LQRSTRYPAG
     VTLRFARVLR YREDKTAREA DTVETVLSRQ R
//
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