ID A0A830G1F0_9EURY Unreviewed; 842 AA.
AC A0A830G1F0;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
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=GCM10009017_21320 {ECO:0000313|EMBL:GGM70940.1}, J2752_002199
GN {ECO:0000313|EMBL:MBP1955276.1};
OS Halarchaeum rubridurum.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Halobacteriaceae.
OX NCBI_TaxID=489911 {ECO:0000313|EMBL:GGM70940.1, ECO:0000313|Proteomes:UP000614609};
RN [1] {ECO:0000313|EMBL:GGM70940.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 16108 {ECO:0000313|EMBL:GGM70940.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGM70940.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 16108 {ECO:0000313|EMBL:GGM70940.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MBP1955276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 22443 {ECO:0000313|EMBL:MBP1955276.1};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2021) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GGM70940.1}.
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DR EMBL; BMOO01000005; GGM70940.1; -; Genomic_DNA.
DR EMBL; JAGGKO010000004; MBP1955276.1; -; Genomic_DNA.
DR RefSeq; WP_188872597.1; NZ_BMOO01000005.1.
DR AlphaFoldDB; A0A830G1F0; -.
DR OrthoDB; 30963at2157; -.
DR Proteomes; UP000614609; Unassembled WGS sequence.
DR Proteomes; UP000765891; Unassembled WGS sequence.
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:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:TreeGrafter.
DR GO; GO:0006281; P:DNA repair; IEA:TreeGrafter.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR FunFam; 1.10.290.10:FF:000003; DNA topoisomerase; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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; IPR013498; Topo_IA_Znf.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR006171; TOPRIM_dom.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR NCBIfam; NF005555; PRK07220.1; 1.
DR PANTHER; PTHR11390:SF26; DNA TOPOISOMERASE 1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; Zn_ribbon_Top1; 2.
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 SUPFAM; SSF57783; Zinc beta-ribbon; 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 {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:UP000614609};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..133
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 151..573
FT /note="Topo IA-type catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52039"
FT REGION 189..194
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 360..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 48
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 165
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 320
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 507
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 842 AA; 93032 MW; 26E5DECE02D27153 CRC64;
MELIITEKDN AARRIADILS EGGTSTERSG GVDVYQWGGR RCIGLSGHVV GVDFPPEYSD
WRDVEPAELT DAPVTKTPTQ ESIVNVLKRL AGEADSVIIA TDYDREGELI GKEAYELVRE
ANADVPVSRV RFSSITENEV KSAFADPDDL DFDLAAAGEA RQIIDLIWGA ALTRFLSLSA
RQVGDDFISV GRVQSPTLKL IVDKEREIEA FDPEDYWELF ADLEKEGSTF EAQYFYRDED
DNEAERVWNE DDATAAFDVL REAATAVVES VRRRTRTDDP PAPFNTTQFI RAASSLGYAA
GRAMSIAEDL YTAGYITYPR TDNTVYPDDL DPADLLDALS AQRDFAASVE RLEELDELEA
TRGDEETTDH PPIHPTADLP SKGDLSEDEW EVYELVVRRF FATLAEPAEW EHLRVVADAE
GEQLKANGRR LVEEGYHAVY PYFGTDENHV PDVAEGEELA IADARMEAKQ TQPPRRYGQS
RLIETMESMG IGTKSTRHNV IEKLYDRGYI ENDPPRPTRL AMAVVEAAEE YADLVVSEEM
TAELEADMTA IAEGEKNLDS VTEESREILG RVFEALDESR EEIGEHLRES LKADKRLGPC
PKCGSDLLVR RSRQGSYFVG CDGYPDCRFT LPLPSTGEPV VLDAECEEHG LNEVKMLAGR
NTFVHGCPLC AAEEAAETED RIIGPCPECG ENAAPEGERG EGGDAAGAHG GELAIRKLQS
GSRLVGCTRY PDCEYSLPLP RRGDIEVTDT YCEEHDLPEL VVHDEGSDEP WELGCPICNY
EEYRARQGLD GIEGIGPKTK EKLAAAGIEN LDDLVDADAE GVAEDVEGVS AERVEDWQAK
AD
//
