ID A0A158Q751_9BILA Unreviewed; 858 AA.
AC A0A158Q751;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
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};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000363601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000363601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-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|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 AlphaFoldDB; A0A158Q751; -.
DR STRING; 1147741.A0A158Q751; -.
DR WBParaSite; EEL_0000363601-mRNA-1; EEL_0000363601-mRNA-1; EEL_0000363601.
DR Proteomes; UP000050640; Unplaced.
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 CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 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; IPR023406; Topo_IA_AS.
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 InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 5..149
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 378..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 96449 MW; B002E24AD68C3C62 CRC64;
MAPLKVIMVA EKPMLAESIA KILADGKVNK RKGWNNVCSV SEYHGQFQGQ SALFKVTSTC
GHIMSLDFPS KMNNWEKVDP VQLFSSPTAK KEANPKMRMN EYLASEAKGC DFLVLWLDCD
KEGENICFEV IEAVKNSVKK PRTGNIMENI YRAHFSAITA NHIKSAMRNL GRPNINESLS
VDARQELDLR IGCAFTRFQT RYFQGKYGNL DSTTISFGPC QTPTLGFCVT RHDLITQFKP
EPYWVLDTVF ETSTGEKLKP THARGRIFDK DVSQLFFDRV KKQNEGVVVD VSSSKFRKER
PQALNTVELL RVASSGLGLS PAQAMSTAEY LYTRGFISYP RTETTAYPSN FDFSEALHHQ
QNDSRWKDIV KKLLSKGITT PRNGEDKGDH PPISPLRGND GSLTGDALKI YDYVTQHFIA
TLMKPCTYLV TDVKIDVANE IFVAKSKSVI NLGYTEIMFW QKIDEDTQYY NIVKGTKVNL
KDAKICEYAT TPPDYLTESE LISLMEKHGI GTDASIPVHI NNICQRNYVT VESKRRLKPT
KLGIALVHGY WKIDSELVLP TMRSEVESQL NLIAKGYADF CSVKNHVLEN FRLKFIYFVE
NIALVDSLFE DSFTSLASSG KPFSRCGKCR RFMKLVASKP QRLHCPNCQD TYSLPSGKDG
LLRLHGENKC PLDDFDLIYW QGPGGKLSMS YALCPYCYNN PPFEGMRKGS GCHECSNPVC
PHSFLTLGVV QCPRQCGSGR GVLVLDPQSA PKWRISCNKC SAVVAIFEGA LRVKVLPKQC
EDCGAQLFFA EYKNKYSLPE EKTTYRGCVF CDKAISHLVN LNHAYSADEP VQRRHTNVRQ
KRGGGASTKS RGRIAPKR
//
