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Database: UniProt/SWISS-PROT
Entry: DNLI_STRAW
LinkDB: DNLI_STRAW
Original site: DNLI_STRAW 
ID   DNLI_STRAW              Reviewed;         512 AA.
AC   Q826P6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   28-FEB-2018, entry version 103.
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=SAV_7136;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC74847.1; -; Genomic_DNA.
DR   RefSeq; WP_010988531.1; NZ_JZJK01000085.1.
DR   ProteinModelPortal; Q826P6; -.
DR   SMR; Q826P6; -.
DR   STRING; 227882.SAV_7136; -.
DR   PRIDE; Q826P6; -.
DR   EnsemblBacteria; BAC74847; BAC74847; SAVERM_7136.
DR   KEGG; sma:SAVERM_7136; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   BioCyc; SAVE227882:G1G23-7459-MONOMER; -.
DR   Proteomes; UP000000428; 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; 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   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    512       Probable DNA ligase.
FT                                /FTId=PRO_0000365240.
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     374    374       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   512 AA;  54366 MW;  83BCF5CCA086779F CRC64;
     MLLSRLAHVS REVAATSARS RKIALLAELF RDADADDVPI VIPYLAGRLP QGRLGIGWKL
     LGRPVTPASE PSLTVRDVDA RLTAVGAVTG TGSQAGRGRL MGELMAAATD VEQAFLRGLL
     TGEVRQGALD AVAVEGLAEA TGAPPADVRR AVMLAGSLQT VARALLAEGP GALDGFRLTV
     GRPVLPMLAH TAGSVAEAVG KLGACAVEEK LDGIRVQLHR DGDHVRIYTR TLDDITDRLP
     ELTAAALELK GDRFILDGEV IALDGNGRPR SFQEIAGRVG SRVDVAAAAA SVPVSPVFFD
     ALSVDGRDLL DLPFTERHAE LARLVPEPLR VRRALVSGPD DGAAAETFLA DTLARGHEGV
     VVKALDAPYS AGRRGASWLK VKPVHTLDLV VLAAEWGHGR RTGKLSNLHL GARAADGSFA
     MLGKTFKGMT DAMLTWQTER LTELAVEENG SVVTVRPELV VEIAYDGLQK STRYPAGVTL
     RFARVVRYRE DKTPAEADTV ETLLAAHPEV TR
//
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