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Entry: A0A1V0DBS5_9BACT
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ID   A0A1V0DBS5_9BACT        Unreviewed;       860 AA.
AC   A0A1V0DBS5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN   ORFNames=AWN76_004345 {ECO:0000313|EMBL:ARA92472.1};
OS   Rhodothermaceae bacterium RA.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX   NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA92472.1, ECO:0000313|Proteomes:UP000055617};
RN   [1] {ECO:0000313|EMBL:ARA92472.1, ECO:0000313|Proteomes:UP000055617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA {ECO:0000313|EMBL:ARA92472.1,
RC   ECO:0000313|Proteomes:UP000055617};
RA   Liew K.J.;
RT   "Complete genome of the potential lignocellulosic biomass degrader
RT   Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT   Malaysia.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC       is introduced during the DNA replication and transcription, by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at a target
CC       site in duplex DNA. The scissile phosphodiester is attacked by the
CC       catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC       (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC       DNA strand. The free DNA strand then undergoes passage around the
CC       unbroken strand, thus removing DNA supercoils. Finally, in the
CC       religation step, the DNA 3'-OH attacks the covalent intermediate to
CC       expel the active-site tyrosine and restore the DNA phosphodiester
CC       backbone. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP-
CC         Rule:MF_00952};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}.
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DR   EMBL; CP020382; ARA92472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0DBS5; -.
DR   STRING; 1779382.AWN76_004345; -.
DR   KEGG; rbar:AWN76_004345; -.
DR   OrthoDB; 9804262at2; -.
DR   Proteomes; UP000055617; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   HAMAP; MF_00952; Topoisom_1_prok; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR025589; Toprim_C_rpt.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 4.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00952};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055617};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00952}.
FT   DOMAIN          3..127
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          176..181
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   REGION          467..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        325
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            33
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            152
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            153
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            156
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            161
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            327
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            524
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   860 AA;  96524 MW;  926581432B3AA78F CRC64;
     MKKRLVVVES PTKARTIRNF LPPEYQVEAS MGHVRDLPSS ASEIPSRLKD EAWARLGVRV
     DNGFEPLYVI PAGKRKVVNG LKAALEGAEE LYIATDEDRE GESIGWHLLE VLNPRVPVRR
     MVFHEITEEA ILEALRRTRS INQHLVDAQE TRRVLDRLVG YTISPLLWKK IAPRLSAGRV
     QSVAVRMLVL REKERIAFVP AQYWDLKADL VQDRQPFQAV MTHWRGIRLA TGRDFDADTG
     RLKPGLEAGK DVLLLGEADA RDLAERLPEA PWRVARVEER VVTRSPAPPF ITSTLQQEAS
     RKLNLSARQT MQVAQRLYEN GYITYMRTDS TVLSTEALEA ARRAVEQRYG RDYLSPSPRQ
     FAGKVRNAQE AHEAIRPAGK AMRTADDLGL SGVEARLYDL IWKRTVASQM ADARLRLVTA
     HIEAGEGDDV ATFRASGRSI VFPGFFRAYV EGSDDPEAAL EDREQPLPDL REGDTPACRH
     VEPVGHETKP PARYTEATLV KQLEQEGIGR PSTYATIIDT IMQRGYVRKQ GNQLVPTFTA
     FATNNLLEKQ FEQLVDTGFT AEMEQILDDI AEGKREATPY LRAFYKGEDG LERRVEQALD
     QVDAREVSTL SFPKWGPYVV RVGKYGPYVE GELDGERVTA SLPEDLAPGD LTAEQLEELL
     KAGNAEDRVL GIHPETDMPI LLRKGPYGPY VQLGDDEQEG KPKRMSLPKG VEPGEVTRQM
     AIDLLSLPRT LGKHPETGQD VRVNIGRYGP YAQHGSTFAS LKKDDDIFSI DLDRALELIA
     EKEAKNKPLR VLGTHPESGE VVEVWNGRYG PYVKHKRTNA TIPKDRDPEG ITMEEALELL
     REREASRGKR GGRRRSKAKG
//
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