ID TOP1_STAAU Reviewed; 689 AA. AC Q06AK7; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 14. 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; OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C66; RA Park J.E., Kim H.I., Lee J.S.; RT "Staphylococcus aureus topoisomerase I."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the CC conversion of one topological isomer of DNA to another (By CC similarity). 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 (By similarity). CC -!- SIMILARITY: Belongs to the prokaryotic type I/III topoisomerase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ923160; ABI81408.1; -; Genomic_DNA. DR BRENDA; 5.99.1.2; 95. 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:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR GO; GO:0006268; P:DNA unwinding during 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; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR006154; Toprim_sub. 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 Pfam; PF01396; zf-C4_Topoisom; 3. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. PE 3: Inferred from homology; KW ATP-binding; DNA-binding; Isomerase; Metal-binding; KW Nucleotide-binding; Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 689 DNA topoisomerase 1. FT /FTId=PRO_0000285934. FT ZN_FING 577 603 C4-type 1. FT ZN_FING 617 645 C4-type 2. FT ZN_FING 658 681 C4-type 3. FT ACT_SITE 298 298 For DNA cleavage activity (By FT similarity). SQ SEQUENCE 689 AA; 79100 MW; 3A42A3B958794887 CRC64; MADNLVIVES PAKAKTIEKY LGKKYKVIAS MGHVRDLPRS QMGVDTEDNY EPKYITIRGK GPVVKELKKH AKKAKNVFLA SDPDREGEAI AWHLSKILEL EDSKENRVVF NEITKDAVKE SFKNPREIEM NLVDAQQARR ILDRLVGYNI SPVLWKKVKK GLSAGRVQSV ALRLVIDREN EIRNFKPEEY WTIEGEFRYK KSKFNAKFLH YKNKPFKLKT KKDVEKITTA LDGDQFEITN VTKKEKTRNP ANPFTTSTLQ QEAARKLNFK ARKTMMVAQQ LYEGIDLKKQ GTIGLITYMR TDSTRISDTA KAEAKQYITN KYGESYTSKR KASGKQGDQD AHEAIRPSST MRTPDDMKSF LTKDQYRLYK LIWERFVASQ MAPAILDTVS LDITQGDIKF RANGQTIKFK GFMTLYVETK DDSDSEKENK LPKLEQGDKV TATQIEPAQH YTQPPPRYTE ARLVKTLEEL KIGRPSTYAP TIDTIQKRNY VKLESKRFVP TELGEIVHEQ VKEYFPEIID VEFTVNMETL LDKIAEGDIT WRKVIDGFFS SFKQDVERAE EEMEKIEIKD EPAGEDCEVC GSPMVIKMGR YGKFMACSNF PDCRNTKAIV KSIGVKCPKC NDGDVVERKS KKNRVFYGCS KYPECDFISW DKPIGRDCPK CNQYLVENKK GKTTQVICSN CDYKEAAQK //