ID TOP1_XYLFT Reviewed; 815 AA. AC Q87AQ6; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 15-JUN-2010, entry version 49. DE RecName: Full=DNA topoisomerase 1; DE EC=5.99.1.2; DE AltName: Full=DNA topoisomerase I; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Untwisting enzyme; DE AltName: Full=Swivelase; GN Name=topA; OrderedLocusNames=PD_1767; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22421331; PubMed=12533478; RX DOI=10.1128/JB.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., RA Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., RA Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., RA Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., RA Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., RA Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., RA Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's RT disease and citrus variegated chlorosis strains of Xylella RT fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the CC conversion of one topological isomer of DNA to another. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. CC -!- SUBUNIT: Monomer (By similarity). CC -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA CC backbone bond, it simultaneously forms a protein-DNA link, in CC which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus CC at one end of the enzyme-severed DNA strand. CC -!- SIMILARITY: Belongs to the prokaryotic type I/III topoisomerase CC family. CC -!- SIMILARITY: Contains 1 Toprim domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009442; AAO29601.1; -; Genomic_DNA. DR RefSeq; NP_779951.1; -. DR RefSeq; NP_779952.1; -. DR SMR; Q87AQ6; 3-569, 4-614. DR STRING; Q87AQ6; -. DR GeneID; 1143108; -. DR GeneID; 1143109; -. DR GenomeReviews; AE009442_GR; PD_1767. DR KEGG; xft:PD1767; -. DR eggNOG; COG0550; -. DR HOGENOM; HBG512935; -. DR OMA; YGPYLKK; -. DR ProtClustDB; PRK08780; -. DR BioCyc; XFAS183190:PD_1767-MONOMER; -. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:EC. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR GO; GO:0006268; P:DNA unwinding involved in replication; IEA:InterPro. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR000380; Topo_IA_core. DR InterPro; IPR003602; Topo_IA_DNA_bd. DR InterPro; IPR005733; TopoI_bac. DR InterPro; IPR006154; Toprim_dom_subgr. DR InterPro; IPR006171; Toprim_domain. DR Gene3D; G3DSA:1.10.460.10; Topo_IA_cen_sub1; 2. DR Gene3D; G3DSA:1.10.290.10; Topo_IA_cen_sub3; 1. DR PANTHER; PTHR11390; Topo_IA; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; Topo_IA_core; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Isomerase; KW Nucleotide-binding; Topoisomerase. FT CHAIN 1 815 DNA topoisomerase 1. FT /FTId=PRO_0000145173. FT DOMAIN 3 115 Toprim. FT ACT_SITE 308 308 For DNA cleavage activity (By FT similarity). SQ SEQUENCE 815 AA; 91802 MW; 2F23C4675BEA8363 CRC64; MPKHLLIVES PAKAKTINKY LGKDFTVLAS YGHVRDLVPK EGAVDPENGF AMRYDLIDKN EKHVEAITKA AKTADSIYLA TDPDREGEAI SWHISEILKE RGLLKDKPMQ RIVFTEITPR AIKEAIQKPR MIASDLVDAQ QARRALDYLV GFNLSPVLWR KVQRGLSAGR VQSPALRMIV EREEEIEAFI TREYWSIHAE CTHPAQHFSA KLIKLDGKKF EQFTITDSDT AAAAQRRIQQ AAQGRLHITD VTNKERKRRP APPFITSTLQ QEASRKLGFT TRKTMQIAQK LYEGIALGEE GSVGLITYMR TDSVNLSLDA LSEIRDIIAR DYGTNALPDK PNVYTTKSKN AQEAHEAVRP TSALRTPTQV APYLSNEEHR LYELVWKRTV ASQMIPAILN TTSVDLAAGN EHVFRATGTT VVVQGFLAVY EEGKDNKNAE DDDEGRKLPV MKTGENVPLE RILTEQHFTQ PPPRYTEAAL VKALEEYGIG RPSTYASIIQ TLLFRKYVDM EGRSFRPTDI GRAVSKFLSS HFTQYVDYDF TAHLEDELDA ISRGEEEWIP LMKKFWVPFK ELVEDKKDSL DKTDAGSVRL LGIDPTSGKE VSARIGRFGP MVQIGTVDDE EKPRFASLRP NQSIYSISLE EAIELFKMPR VLGEDQSQQV SVGIGRFGPF AKRGSTYVSL KSEDDPYTID LARATLLINE KEEIARNRII KDFENSQIQV LNGRFGPYIS DGKLNGKIPK DREPASLTLE EAQQLLINTG KPARKNFSTK KTATKNETRK QTTKKRTTDA KATKKVSDKP VKKQIKKRIA PNITQ //