(data stored in SCRATCH3701 zone)

SWISSPROT: TOP1_RICTY

ID   TOP1_RICTY              Reviewed;         779 AA.
AC   Q68X45;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952};
DE   AltName: Full=Omega-protein;
DE   AltName: Full=Relaxing enzyme;
DE   AltName: Full=Swivelase;
DE   AltName: Full=Untwisting enzyme;
GN   Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; OrderedLocusNames=RT0317;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00952};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00952};
CC       Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00952};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00952}.
DR   EMBL; AE017197; AAU03797.1; -; Genomic_DNA.
DR   RefSeq; WP_011190781.1; NC_006142.1.
DR   SMR; Q68X45; -.
DR   STRING; 257363.RT0317; -.
DR   PRIDE; Q68X45; -.
DR   EnsemblBacteria; AAU03797; AAU03797; RT0317.
DR   KEGG; rty:RT0317; -.
DR   eggNOG; ENOG4105C73; Bacteria.
DR   eggNOG; COG0550; LUCA.
DR   eggNOG; COG1754; LUCA.
DR   HOGENOM; HOG000004020; -.
DR   KO; K03168; -.
DR   OMA; PECKYTR; -.
DR   OrthoDB; 223233at2; -.
DR   BioCyc; RTYP257363:G1G0L-322-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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; 1.10.290.10; -; 1.
DR   Gene3D; 1.10.460.10; -; 1.
DR   Gene3D; 2.70.20.10; -; 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; IPR013498; Topo_IA_Znf.
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   PANTHER; PTHR42785; PTHR42785; 2.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 2.
DR   Pfam; PF01396; zf-C4_Topoisom; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; SSF56712; 1.
DR   TIGRFAMs; TIGR01051; topA_bact; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68X45.
DR   SWISS-2DPAGE; Q68X45.
KW   DNA-binding; Isomerase; Magnesium; Metal-binding; Topoisomerase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..779
FT                   /note="DNA topoisomerase 1"
FT                   /id="PRO_0000273106"
FT   DOMAIN          1..111
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   ZN_FING         600..627
FT                   /note="C4-type"
FT   REGION          166..171
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   ACT_SITE        304
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   METAL           7
FT                   /note="Magnesium 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   METAL           80
FT                   /note="Magnesium 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   METAL           80
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   METAL           82
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            31
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            142
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            143
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            146
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            158
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            306
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            499
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   779 AA;  89083 MW;  D300A268969CEA89 CRC64;
     MKLVIVESPA KAKTINKYLG DEFKVIASFG HIRDLPSKKG SVLPDKNFAM EYDISDKASK
     YVDAIVKYAR KAEAVYLATD PDREGESISW HVAEVIKEKN KVESDDFFKR VAFNEITKKA
     IIHAVENPRK LDTNLVNAQQ ARRALDYLVG FTLSPLLWRK LPGCKSAGRV QSVALRLICD
     REDEIERFKA EEYWDISLKM QNSNNELFTA KLTHVNDQKL KKFSIINEKE AKDLTRKLKL
     QKFYVEKIEK KQQKRQPQPP FITSSLQQEA ARKLGFSAKK TMQIAQKLYE GVDIGKETIG
     LITYMRTDGV TLSNDAIADI RKLIDKNYGN KYLPINPRIY QSKVKNAQEA HEAIRPTNIT
     YTPDNLKQKL EKDYYKLYEL IWQRTIACQM ENVIMDLVIA NLASENKEYL AKANGSIIAF
     DGFYKVYRES LDDEDEEDNK MLPPLKAQEH IKTKEVIPNK HFTEPPPRYS EASLVKKLEE
     LGIGRPSTYA SILSVLQDRK YVTLEKKRFI PEELGRLVTV FLVGFFKKYV EYDFTAGLEN
     ELDEIAAGKL EWKTSLNNFW SGFNNNIESV NEQKITEIIN YLQKALDYHL FGENKESKVC
     PSCKTGQLSL KLGKFGAFLA CSNYPECTFK KSIVSGNDNN EDEGNLSTIL NDNKILGTDK
     DGVEIYLKTG PYGPYIQLGE QCGKVKPKRT PVPTNLKQSE ITLEVALKLL SLPLKIGIHK
     DSGEEIIIGY SKFGPYIKYM CKFISVPKKY DFLNLNLDDA IKLIENNKAK LEKKHRSMV
//

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