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Database: UniProt
Entry: A0A0V1ME58_9BILA
LinkDB: A0A0V1ME58_9BILA
Original site: A0A0V1ME58_9BILA 
ID   A0A0V1ME58_9BILA        Unreviewed;       765 AA.
AC   A0A0V1ME58;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 29.
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   Name=TOP1 {ECO:0000313|EMBL:KRZ70161.1};
GN   ORFNames=T10_100 {ECO:0000313|EMBL:KRZ70161.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ70161.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ70161.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ70161.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ70161.1}.
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DR   EMBL; JYDO01000119; KRZ70158.1; -; Genomic_DNA.
DR   EMBL; JYDO01000119; KRZ70160.1; -; Genomic_DNA.
DR   EMBL; JYDO01000119; KRZ70161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1ME58; -.
DR   STRING; 268474.A0A0V1ME58; -.
DR   Proteomes; UP000054843; 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: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:SF3; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          360..737
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          644..711
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        18..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  89068 MW;  4380B60122354CBD CRC64;
     MTTVEGESLF RAQNGDAYRI TSHPSQQSDH EQKMCTVKTE TEQQSSEQTT TSTDHLWTAS
     SSVDDLAQRN GLIVSSSELK IKVKVKQEPQ DGKFNAVSGN TRKQQIPREL AETSVKCEES
     SSKSQSKKRK TKADDNTSSS VQKKKVKIKE IEPQPIKPPK GKRKVKSEKE IDQTSKNKAD
     SGSEVKQEKG KRVKKEEQET EVWRWWEEEK RDDSVKWKFL EHKGPVFAPP YEPLPSSVNF
     YYDGKPMKLS EGAEEVATFY SKMLDHEYTT KDVFNKNFFH DWRKMMNPKE RETITDLSRC
     NFREMNEYFT KKSEERKALS KDEKKKLKDE QEAQRLIYGY AVVDGHKEKI GNYKIEPPGL
     FRGRGTHPKM GRLKRRIQPE DVIINCSKDA KVPEPPPGHS WKEVRYDNTV TWLASWTENI
     MGSNKYVMLN PSSKIKGEKD WEKYETARKL KDVVEKIRSE YRTDWKSKEM KVRQRAVALY
     FIDKLALRAG NEKEDNETAD TVGCCSLRCE HIKLHKELDG QQNVVEFDFL GKDSIRYYNR
     VPVESRVFKN LRIFMEHKSP DDDLFDRLNT ATLNKHLQNL MPGLTAKVFR TYNASITLQQ
     QLELLTKGDT NTAERLLAYN RANRQVAILC NHQRSVPKTH GKQMENIQKK IEEKEKQIKE
     MKKMVKSAKA EHNASGTAKT KKVLEQKKKN LHRSEEQLLK LKVRATDKEE NKEIALSTSK
     LNYLDPRISV AWCKKWDVPI DKIYNRTQRE KFRWAIDMAG PEFIF
//
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