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Database: UniProt/TrEMBL
Entry: A0A1V0AHY8_9ACTN
LinkDB: A0A1V0AHY8_9ACTN
Original site: A0A1V0AHY8_9ACTN 
ID   A0A1V0AHY8_9ACTN        Unreviewed;       507 AA.
AC   A0A1V0AHY8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
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=BKM31_57825 {ECO:0000313|EMBL:AQZ69844.1};
OS   Nonomuraea sp. ATCC 55076.
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Nonomuraea.
OX   NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ69844.1, ECO:0000313|Proteomes:UP000190797};
RN   [1] {ECO:0000313|EMBL:AQZ69844.1, ECO:0000313|Proteomes:UP000190797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55076 {ECO:0000313|EMBL:AQZ69844.1,
RC   ECO:0000313|Proteomes:UP000190797};
RA   Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA   Setedsayamdost M.R.;
RT   "Nonomuraea sp. ATCC 55076 harbors the largest actinomycete chromosome
RT   to date and the kistamicin biosynthetic gene cluster.";
RL   Med. Chem. Commun. 0:0-0(2017).
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; CP017717; AQZ69844.1; -; Genomic_DNA.
DR   KEGG; noa:BKM31_57825; -.
DR   KO; K10747; -.
DR   Proteomes; UP000190797; 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; -; 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; 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:UP000190797};
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:AQZ69844.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190797}.
FT   DOMAIN      288    412       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    211    211       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     209    209       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     216    216       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     231    231       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     260    260       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     372    372       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   507 AA;  54632 MW;  BDC2A46DD1C611FA CRC64;
     MLLIDVVRVS EAVTRTSARL GKVGHLAELL GRVGPDEAEI AISYLSGELP QRQVGVGWRT
     LEDVPQPKLA ATATLTDVDR LLSKIKAVSG PGSQAARKAL VAELFAGLTS QEQQFMRRLL
     HGELRQGALD GVMIEAIAKA SGAPSADVRR ALTLRGWLPA VGAAALSGGV AALHAFRLEV
     GRAVAPMLAG SAPNVAAALE KAGTPAALEW KLDGVRVQAH RSGAEVRVFT RTLDDITPQV
     PELVEAVLEM PSTDLVLDGE VLALRPDGRP HPFQVTASRV SSKTNVAALR AQTPLSVFFF
     DALRVDGADL LDLPYAERQE ALARTVPQGL LTPRLVTGEP AEAEQFFTDV VKAGHEGLVV
     KSLASPYAAG RRGAGWIKVK PRHTLDLVVL AAEWGHGRRE GKLSNLHLGA RDPEGGFVML
     GKTFKGLTDE LLAWQTERFL QLAEGPTDEW TVRLRPELVV EIAFDGVQRS PRYPGGMALR
     FARVLRYRPD KRVEDADTVE TVRSLML
//
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