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Database: UniProt
Entry: A0A0R3SNN8_HYMDI
LinkDB: A0A0R3SNN8_HYMDI
Original site: A0A0R3SNN8_HYMDI 
ID   A0A0R3SNN8_HYMDI        Unreviewed;       137 AA.
AC   A0A0R3SNN8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092};
DE            EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092};
GN   ORFNames=HDID_LOCUS6551 {ECO:0000313|EMBL:VDL58869.1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000655301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000655301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL58869.1, ECO:0000313|Proteomes:UP000274504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362092};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|RuleBase:RU362092}.
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DR   EMBL; UYSG01005931; VDL58869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3SNN8; -.
DR   STRING; 6216.A0A0R3SNN8; -.
DR   WBParaSite; HDID_0000655301-mRNA-1; HDID_0000655301-mRNA-1; HDID_0000655301.
DR   Proteomes; UP000046397; Unplaced.
DR   Proteomes; UP000274504; 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   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|RuleBase:RU362092};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          1..128
FT                   /note="DNA topoisomerase type IA central"
FT                   /evidence="ECO:0000259|Pfam:PF01131"
SQ   SEQUENCE   137 AA;  14823 MW;  08FB6D2ABB8526F7 CRC64;
     MPDCKYETTT VVLSIGDEKF TTRASRVIDP GYTRIFTWQA VGSTVAVEGQ DEEECDGPEI
     TLPAALTTPG SSFSLGEKPR LVEGQTGPPN YLSEAELITA MEKHGIGTDA SIPVHIENIV
     ERAYVEVRIS VVVVLLN
//
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