GenomeNet

Database: UniProt
Entry: A0A3M7SPQ1_BRAPC
LinkDB: A0A3M7SPQ1_BRAPC
Original site: A0A3M7SPQ1_BRAPC 
ID   A0A3M7SPQ1_BRAPC        Unreviewed;       710 AA.
AC   A0A3M7SPQ1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE            EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101};
DE   AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
GN   ORFNames=BpHYR1_037393 {ECO:0000313|EMBL:RNA37834.1};
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:RNA37834.1, ECO:0000313|Proteomes:UP000276133};
RN   [1] {ECO:0000313|EMBL:RNA37834.1, ECO:0000313|Proteomes:UP000276133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYR1 {ECO:0000313|EMBL:RNA37834.1};
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: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by transiently
CC       cleaving and rejoining one strand of the DNA duplex. Introduces a
CC       single-strand break via transesterification at the specific target site
CC       5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is
CC       attacked by the catalytic tyrosine of the enzyme, resulting in the
CC       formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
CC       expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC       passage around the unbroken strand thus removing DNA supercoils.
CC       Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC       intermediate to expel the active-site tyrosine and restore the DNA
CC       phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}.
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:RU365101};
CC   -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}.
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:RNA37834.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; REGN01000969; RNA37834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7SPQ1; -.
DR   STRING; 10195.A0A3M7SPQ1; -.
DR   Proteomes; UP000276133; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00659; Topo_IB_C; 1.
DR   CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1.
DR   Gene3D; 1.10.132.10; -; 1.
DR   Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR   Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 1.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR   InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR   InterPro; IPR001631; TopoI.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR025834; TopoI_C_dom.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR008336; TopoI_DNA-bd_euk.
DR   InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR   InterPro; IPR013499; TopoI_euk.
DR   InterPro; IPR048045; Topoisomer_I_DNA-bd.
DR   PANTHER; PTHR10290:SF23; DNA TOPOISOMERASE 1; 1.
DR   PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
DR   Pfam; PF14370; Topo_C_assoc; 1.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR   SUPFAM; SSF46596; Eukaryotic DNA topoisomerase I, dispensable insert domain; 1.
DR   SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101};
KW   Hydrolase {ECO:0000313|EMBL:RNA37834.1};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276133};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          264..641
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          214..241
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          548..615
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        13..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  82249 MW;  7F9E92E8D4D16C76 CRC64;
     MSSSAAKMSK TSRSSTKSDK KPSIKKEKIE VELKKAAAKS EPAKNGNGHV KVKAEAKSEP
     KQRVKEEAKT PVKQEAKNGK KRAAQADLSQ SESPRKRKKK EEEEEVWRWW EEKKYADGRK
     WTTLEHKGPL FEADYVPLPK HVHFLYNGER VQLKSEAEEV MTFYAKMLDH DYTKKEAFNT
     NFFNDWRKFM TQSERELIKD LAKCDFGQVA DYFKQKSEER KAMSKEEKKA LKEEAAEVKK
     QYGFCVWDGH KQPIGNYKIE PPGLFRGRGE HPKMGMVKKR INPEDVIINC GKESKVPEAP
     PGRKWKEVRH DNMVAWLASW TENVQGNSKY VMLNAASRVK GERDWQKYEK ARKLHRWIDK
     IRQNYSEDWK SKEMKVRQRA VAIYFIDKLA LRAGNEKDDD EADTVGCCSL RVEHIKLHKS
     VEGVGEHVVE FDFLGKDSIR YQNKVAVEKQ VYKNLLLFVE NKNGEDELFD RLNTTILNSY
     LNECMDGLSA KVFRTYNASR TLQEQLDQMT DKHDSINDLV LTYNRANRAV AILCNHQRAV
     PKTFAKSMEN MQKKIQDKKD AIADAEAELK KAKSDLKNLK SVAAKKKFET AENKVKKLVE
     GLRKLEMQVT DKEENKDIAL GTSKLNYLDP RISIGWCKKH NVPIEKVYSK TQRDKFRWAI
     DMATADYHFF NYEGEIVLRD LSHLEGMDGG ANTTQEADET QQDDEEEDDD
//
DBGET integrated database retrieval system