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Database: UniProt/TrEMBL
Entry: A0A0A0NHK3_9ACTN
LinkDB: A0A0A0NHK3_9ACTN
Original site: A0A0A0NHK3_9ACTN 
ID   A0A0A0NHK3_9ACTN        Unreviewed;       512 AA.
AC   A0A0A0NHK3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
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=M271_24675 {ECO:0000313|EMBL:AGP56429.1};
OS   Streptomyces rapamycinicus NRRL 5491.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1343740 {ECO:0000313|EMBL:AGP56429.1, ECO:0000313|Proteomes:UP000030183};
RN   [1] {ECO:0000313|EMBL:AGP56429.1, ECO:0000313|Proteomes:UP000030183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 5491 {ECO:0000313|EMBL:AGP56429.1};
RX   PubMed=23929477;
RA   Baranasic D., Gacesa R., Starcevic A., Zucko J., Blazic M., Horvat M.,
RA   Gjuracic K., Fujs S., Hranueli D., Kosec G., Cullum J., Petkovic H.;
RT   "Draft Genome Sequence of Streptomyces rapamycinicus Strain NRRL 5491,
RT   the Producer of the Immunosuppressant Rapamycin.";
RL   Genome Announc. 1:0-0(2013).
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; CP006567; AGP56429.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGP56429; AGP56429; M271_24675.
DR   KEGG; src:M271_24675; -.
DR   PATRIC; fig|1343740.8.peg.2857; -.
DR   KO; K10747; -.
DR   Proteomes; UP000030183; 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; 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 {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:UP000030183};
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:AGP56429.1};
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      299    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   512 AA;  54891 MW;  2A0DD9A4150CA194 CRC64;
     MLLADVALTS RQVAATAART EKIAALARLF RRTEPAEAAV VITYLAGKLP QRRTGVGWST
     LRHRREPAAE PTLAVLDVDE ALSRVAAVAG TGATAARKRL VGELLSAATK EEQGFLLGLI
     GGELRQGALE GLAVEGLAEA VGAPAAEVRR AVMLGGSLGA VAEALLARGP EALADFRLEV
     GRPVLPMLAQ SAKDLDEAMD RLGACAVEEK LDGIRVQVHR DGEEVRIYTR TLDEITERLP
     EVVTAARELA VDRAILDGEV ILLDAEGRPR PFQETSGRVG SRLDVAGASA ALPLSPVFFD
     LLMVDDRDLL DLPAHERHAE LARIAPGPRR VRRLVADDPA DPETRRAAGE FAADVLARGH
     EGVLVKGLEA PYGAGRRGAS WLKVKPVHTL DLVVLAAEWG HGRRTGKLSN LHLGARAPDG
     TYVMLGKTFK GLTDVMLEWQ TEALLGIAVS DDGWVVRVRP ELVVEVAFDG LQRSSRYPAG
     VTLRFARVLR YREDKPADQA DTVETVLALR GG
//
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