ID A0A183RBW4_9TREM Unreviewed; 114 AA.
AC A0A183RBW4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0001348501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0001348501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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 AlphaFoldDB; A0A183RBW4; -.
DR STRING; 6188.A0A183RBW4; -.
DR WBParaSite; SROB_0001348501-mRNA-1; SROB_0001348501-mRNA-1; SROB_0001348501.
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; 3.40.50.140; -; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01751; Toprim; 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|RuleBase:RU362092};
KW Topoisomerase {ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 6..108
FT /note="Toprim"
FT /evidence="ECO:0000259|Pfam:PF01751"
SQ SEQUENCE 114 AA; 13112 MW; 1FBF0B470959F90E CRC64;
MQTVFMVAEK PSLAESIAKS LSNKRNSSRR GFNGACSIHE WTGQFMSEQV RFKMTSVCGH
VMNVDFLSRY NSWDKVDPAE LFVAPIEKKE ANPKLKMVDF LRHEVFYIFN STIV
//
