ID A0A1W0E6I5_9MICR Unreviewed; 716 AA.
AC A0A1W0E6I5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
GN Name=Top3a {ECO:0000313|EMBL:OQS54792.1};
GN ORFNames=EHP00_1264 {ECO:0000313|EMBL:OQS54792.1};
OS Ecytonucleospora hepatopenaei.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Ecytonucleospora.
OX NCBI_TaxID=646526 {ECO:0000313|EMBL:OQS54792.1, ECO:0000313|Proteomes:UP000192758};
RN [1] {ECO:0000313|EMBL:OQS54792.1, ECO:0000313|Proteomes:UP000192758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1 {ECO:0000313|EMBL:OQS54792.1,
RC ECO:0000313|Proteomes:UP000192758};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
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,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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:OQS54792.1}.
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DR EMBL; MNPJ01000017; OQS54792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0E6I5; -.
DR STRING; 646526.A0A1W0E6I5; -.
DR VEuPathDB; MicrosporidiaDB:EHP00_1264; -.
DR Proteomes; UP000192758; Unassembled WGS sequence.
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-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 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 InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF06839; zf-GRF; 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; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 2.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192758};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 1..123
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 620..660
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 677..716
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
SQ SEQUENCE 716 AA; 83494 MW; 74AE7C1CDDA171BB CRC64;
MLSKNVQTTR GKFKYCPNHT FDYENDKMIF TSVVGHLYDS EFPPEYKNWN TCDEFELFDA
EIIKSIKEDL KGIKENIQNL SKNAQLVIIW TDCDREGENI GFQIKTLINK KIVVKRARFS
GISKHEIKNA FESLCEINLN ESNAVDARIE LDLRCGSVFT RLQTLHLQKA LGKENAFGSN
KKQVISYGQC QIPTLNFVVE RQKQIDAFVP ETFYSLKLVH NKNEFSWERG NVFDKNFVVH
MYNILFGAKY KVKSVNCKEI VKYSPLPLRT VELQKTCASF YKMSGDEIMT IAEKLYNRGY
ISYPRTETDS FQNNFGFKRI LEKLKEDEKY AEYLEAFEFK MPRKGKNDDQ AHSPIYPLKG
GNDLSGKDRN VYDFVARRFM GCCSKNATAD ETTIEICASF KAGNNNLVGE YFKLKGIKIK
QKNYLNIYIY ESWGDKEIKK CEKYTEGSDL NPEDMDLSII DSRTTSPCDL TEKDLIVLMD
KNGIGTDATI HEHISKIQAR NYAYKVGQYI RPTDLGMNLI NAYKTLELPI HECKIRKEME
ENLISVCAGK MRKEDLVQRE IKIYKEIYTR FKNQIEKYVE VMKVENDFKK TTKKNTGKTY
TDVVKKQKVE NFTKNESILC KCRENATRKQ CLKGKNKNRY FYGCFSFPKK CDFFMWEGEE
NKGMHFKRSE VVDEVKCDCG KSAVKKTSST EKNLGRQFYV CNKSYKQCKF FQWVEK
//
