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Database: UniProt
Entry: A0A3M7PKL8_BRAPC
LinkDB: A0A3M7PKL8_BRAPC
Original site: A0A3M7PKL8_BRAPC 
ID   A0A3M7PKL8_BRAPC        Unreviewed;       535 AA.
AC   A0A3M7PKL8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   22-FEB-2023, entry version 15.
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};
DE   Flags: Fragment;
GN   ORFNames=BpHYR1_005959 {ECO:0000313|EMBL:RMZ99619.1};
OS   Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC   Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC   Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX   NCBI_TaxID=10195 {ECO:0000313|EMBL:RMZ99619.1, ECO:0000313|Proteomes:UP000276133};
RN   [1] {ECO:0000313|EMBL:RMZ99619.1, ECO:0000313|Proteomes:UP000276133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYR1 {ECO:0000313|EMBL:RMZ99619.1};
RX   PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA   Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA   Gomez A.;
RT   "Genomic signatures of local adaptation to the degree of environmental
RT   predictability in rotifers.";
RL   Sci. Rep. 8:16051-16051(2018).
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:RMZ99619.1}.
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DR   EMBL; REGN01010134; RMZ99619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7PKL8; -.
DR   STRING; 10195.A0A3M7PKL8; -.
DR   Proteomes; UP000276133; 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: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; 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; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
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   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   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000276133};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          3..147
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          367..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         535
FT                   /evidence="ECO:0000313|EMBL:RMZ99619.1"
SQ   SEQUENCE   535 AA;  61590 MW;  C43A1D0758F40BD3 CRC64;
     MLKILNVAEK NNAAKSIASL LSKGTCRKRE SAAPFNQIYE FEYNLFNQNC LMVMTSVSGH
     LLSLEFSNKY KRWDSCDPIE LFDAKIERVC PKKYQKVMLS LQREVQSCQK LIIWTDCDRE
     GENIGYEIIE ACSNVHNNLD VYRAKFSEIT ASSVAKSICD LKRPNRLASD AVEVRKELDL
     RVGAAFTRFQ TLHLTKAFPD QLTGSLISYG SCQFPTLGFV VERYKQREKF VSKPFWKVCV
     FDEKDNQKVE FLWDKERMFD YQVCWNFFNK LISHQSLAVQ SVIRRPKNKC RPVALNTIEL
     LKLASRKLNI NAKKTMTIAE NLYSEGLISY PRTETNIFTE TFDFRGIIES QTSDQNWGLF
     AKNILDRPNP RNGTKSDQSH PPIYPTKYTN NLKGKEKKIY DLIVRNFLAC CSEDAKGSET
     AVSIDVSHEK FTASGLMVFE RNYLDVYPYE RWVNKKIPEF ENGQTFSPKS IQLNKGMTQA
     PRLLTEADLI DLMEKHGIGT DSTLAEHIET IKKRSYVRIE RNLFVPTVLG LGLVE
//
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