ID A0A267FEK5_9PLAT Unreviewed; 554 AA.
AC A0A267FEK5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092};
GN ORFNames=BOX15_Mlig014717g1 {ECO:0000313|EMBL:PAA72221.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA72221.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA72221.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA72221.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA72221.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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}.
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:PAA72221.1}.
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DR EMBL; NIVC01001103; PAA72221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267FEK5; -.
DR STRING; 282301.A0A267FEK5; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR013498; Topo_IA_Znf.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 1.
DR Pfam; PF06839; zf-GRF; 2.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS51999; ZF_GRF; 2.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Topoisomerase {ECO:0000256|RuleBase:RU362092};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 310..349
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 447..489
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 287..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 56245 MW; CCDAF96080FE8DA8 CRC64;
MDRHGIGTDA THAEHIETVK QRLYVGLQDA RYLVPGQLGI GLVEGYDAMG FQMSKPDLRS
ALEADLKAIC EGRRSKQDVL SFHIERYRRV FDEACRQANL LDARVGHYLD EQPAEAPQLP
AGEAGGQANS TNLVRRCPQC SAADMALKTK RDGSSYYVGC LAYPTCKRAV WLPESVRRAA
VSDQNCPTCS TPGGADGQVR KLTLQFSQAA PMPFRDLAEH TICVFCDPDY VGAFGGAAST
VGGGGGGGQP KPSTAISFHA NELQAASMQQ RLFLQPQDRQ TFAVQAPAPM QQQPPPQPPG
GASNAAPGTC ACGTPVRELT VRKEGPNKGR QFYKCATGTC NHFQWADAPP GGGGGGGGGF
AGASFSASST QYGGGGDFGS GGGGGFGGNS GFGGGGGGGF GGGGGGGSSG FGGGGGGGFG
GGGGGGSSGF GGGGGGSGGG AASGVSCKCG EPARERTVQK DGPNKGRPFF GCAKPMNQSC
NFFQWGDEPA GGGGGGGGGG GSGFANSSFG SGSSRGGFSR GGGGGGGLPK GQQPWQPTLR
RRRRRRRRQR RRWR
//
