ID A0A183LXK8_9TREM Unreviewed; 484 AA.
AC A0A183LXK8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
GN ORFNames=SMRZ_LOCUS8533 {ECO:0000313|EMBL:VDO81942.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000853401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000853401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO81942.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDO81942.1,
RC ECO:0000313|Proteomes:UP000277204};
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|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}.
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DR EMBL; UZAI01003734; VDO81942.1; -; Genomic_DNA.
DR STRING; 48269.A0A183LXK8; -.
DR WBParaSite; SMRZ_0000853401-mRNA-1; SMRZ_0000853401-mRNA-1; SMRZ_0000853401.
DR Proteomes; UP000277204; 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 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; 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 PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 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:UP000277204};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 22..110
FT /note="DNA topoisomerase type IA"
FT /evidence="ECO:0000259|SMART:SM00436"
FT DOMAIN 156..431
FT /note="DNA topoisomerase type IA DNA-binding"
FT /evidence="ECO:0000259|SMART:SM00437"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 55524 MW; 22161C5DC1A70C9F CRC64;
MDCTDGLFEN TPFSLKDFYL NFYFRAVHRA VNRLTIPDYN ASTAVDVRQE LDLRIGAAFT
RFQTLRLRRV FPQALSDQLI SYGSCQFPTL GFVVERFREV DQFVSEPFWR IVVTVSRDEK
TTEFQWQRGR LFDQDCCRAY YEHLHQNRYG QIVEVIKRPK TKWRPTALDT VELEKLASRK
LHMGARYAMQ LAERLYNKGF ISYPRTETKI FPPDLDLKSL VRVQINDSRW SDFASRILEH
GPNPKNGKSS DKAHPPIHPL KVGDSLQGDE ARLYELVTRH FLACLSADAE GAETIVRLCI
GKPTLPRTFN SSLSTANLLT SEDGELFESK GLMILALNYL EVYIYDRWAE KDMPVFQLGE
WILPDNIQIL TGQTCPPPLL TEADLISLMD RHGIGTDATH AEHIETIKQR LYVGLEQNKF
LVPGQLGMGL VEGYDSMGFE MSKPNLRSEF EADLKFQSSR GNIQCRVASQ MHISIYCAVS
LVLR
//
