ID   TOP1_AERPE              Reviewed;         673 AA.
AC   Q9YB01;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 139.
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};
GN   OrderedLocusNames=APE_1794;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; BA000002; BAA80797.1; -; Genomic_DNA.
DR   PIR; H72563; H72563.
DR   AlphaFoldDB; Q9YB01; -.
DR   SMR; Q9YB01; -.
DR   STRING; 272557.APE_1794; -.
DR   EnsemblBacteria; BAA80797; BAA80797; APE_1794.
DR   KEGG; ape:APE_1794; -.
DR   PATRIC; fig|272557.25.peg.1202; -.
DR   eggNOG; arCOG01527; Archaea.
DR   Proteomes; UP000002518; 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   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; IPR005739; TopoI_arch.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   NCBIfam; TIGR01057; topA_arch; 1.
DR   PANTHER; PTHR11390:SF26; DNA TOPOISOMERASE 1; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW   Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN           1..673
FT                   /note="DNA topoisomerase 1"
FT                   /id="PRO_0000145176"
FT   DOMAIN          1..134
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   DOMAIN          149..568
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   ZN_FING         595..615
FT                   /note="C4-type"
FT   REGION          189..194
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   REGION          352..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   BINDING         4
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            55
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            159
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            163
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            313
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            501
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   673 AA;  75571 MW;  D26799337623C584 CRC64;
     MVAEKPKAAA KIAYALSDGR GVLRCSEYGV PYWIVRRDGA AIVVAPSAGH LFGPHTDSRG
     FPVFDFEWRP IFEFDRGAGY LSKFYRMLSR ILPGASLYVN ACDYDIEGSV IGFKIIEAFG
     DVNRARRMKF STLAPQDIRR AYARMERLDV EMIEAGMARS EMDWLWGINV SRALMEAARR
     AAGRRVILSA GRVQSPTLVE AYRRWREINL HVPKASVAVK ITAEKGGGVF DARPHGWKPQ
     SLETARSIKS ELRKNPWLAV EEVRSERSIL RPPPAFNLGD LQKEANRILG LPPLRTQSIA
     EELYLEALIS YPRTNSQKLP PSINYRAILD KLAHGPLGRE ARELLKETGG VLRPVQGSKD
     DPAHPAIHPT GEKPSQRLSK EHMAVYELIV RRFLAAFSRE AIVSKSSVLL RDFQGRVWRA
     EGLRVEDLGW LKYYHYSTPG EKPMPPLDRG DKARVVRVDV RVEWSQTPVR LDKASLLRWM
     ESVNIGTEGT RARIIETLYK RGYLEGSRKS EVTPLGEAVA VIIQTLFPEL SKPDLTRRFE
     SMIEDIRSGR RTRQEVIDMS KKTISKLLES FLDRLDTAVR EIGVSLGSVE VEAACHLCGR
     KAVSAVSGYR LCSHHMEAFD RLRKALPNLA STISSTPREA LEAIARGRSR AGAWVRDVAA
     LALRDDGLYK ALL
//