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Database: UniProt/TrEMBL
Entry: N0CJ65_9ACTN
LinkDB: N0CJ65_9ACTN
Original site: N0CJ65_9ACTN 
ID   N0CJ65_9ACTN            Unreviewed;       511 AA.
AC   N0CJ65;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-SEP-2017, entry version 29.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=SFUL_761 {ECO:0000313|EMBL:AGK75745.1};
OS   Streptomyces fulvissimus DSM 40593.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1303692 {ECO:0000313|EMBL:AGK75745.1, ECO:0000313|Proteomes:UP000013304};
RN   [1] {ECO:0000313|EMBL:AGK75745.1, ECO:0000313|Proteomes:UP000013304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40593 {ECO:0000313|EMBL:AGK75745.1,
RC   ECO:0000313|Proteomes:UP000013304};
RA   Myronovskyi M., Tokovenko B., Manderscheid N., Petzke L.,
RA   Luzhetskyy A.;
RT   "Complete genome sequence of Streptomyces fulvissimus.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP005080; AGK75745.1; -; Genomic_DNA.
DR   RefSeq; WP_015607131.1; NC_021177.1.
DR   EnsemblBacteria; AGK75745; AGK75745; SFUL_761.
DR   KEGG; sfi:SFUL_761; -.
DR   PATRIC; fig|1303692.3.peg.778; -.
DR   KO; K10747; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000013304; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013304};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AGK75745.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      287    417       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    210    210       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     208    208       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     230    230       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     377    377       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     383    383       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   511 AA;  54632 MW;  0F52184B683C4F4C CRC64;
     MLLAELAQVS LEVAATSARS KKVALLAALF RDAGPDDVPV VIPYLAGRLP QGRIGVGWRS
     LGDPVEPASE PTLTVTGVDA ELTALAAVSG SGSQALRRER LRALFAAATA DEQHFLRALL
     TGEVRQGALD AVAADALARA AEAPPADVRR AVMLAGSLQE VARTLLAEGP GALAAFRLTV
     GRPVQPMLAH TAASVTEAVD KLGPCAVEEK LDGIRVQVHR DGDRVRAFTR TLDDITDRLP
     ELVTAVAALE TGRFILDGEV IALGDDGRPR PFQETAARVG SRRDVAAAAA GVPIVPVFFD
     ALSADGEDLL DLPYTERHTA LARLVPEHLR VRRALVPEAG DADARRAAEA FLAETLERGH
     EGVVVKDLAA AYSAGRRGAS WLKVKPVHTL DLVVLAAEWG SGRRTGKLSN LHLGARRPDG
     TFAMLGKTFK GLTDALLEWQ TEKLRELATG EDGHVVTVRP ELVVEIAYDG LQRSTRYPAG
     VTLRFARVLR YREDKTAQEA DTVETVLSRQ R
//
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