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Database: UniProt
Entry: A0A267DE24_9PLAT
LinkDB: A0A267DE24_9PLAT
Original site: A0A267DE24_9PLAT 
ID   A0A267DE24_9PLAT        Unreviewed;      1055 AA.
AC   A0A267DE24;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   28-JUN-2023, entry version 19.
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=BOX15_Mlig014717g3 {ECO:0000313|EMBL:PAA46937.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA46937.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA46937.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA46937.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA46937.1};
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|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}.
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:PAA46937.1}.
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DR   EMBL; NIVC01004644; PAA46937.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267DE24; -.
DR   STRING; 282301.A0A267DE24; -.
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   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; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   InterPro; IPR001878; Znf_CCHC.
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; PF01751; Toprim; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 1.
DR   Pfam; PF06839; zf-GRF; 2.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
DR   PROSITE; PS51999; ZF_GRF; 2.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00047}.
FT   DOMAIN          1..122
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   DOMAIN          780..819
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   DOMAIN          917..959
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   DOMAIN          1035..1050
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          341..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  111804 MW;  F88A82C155948D70 CRC64;
     MRRRDGQSRY NKIYEFQCNL LGQQCQMTMT SVSGHLMNYD FTQQHRKWLS CHPSALFDAP
     VVKQIQRDYQ PIRDTLTQLA KSAQRLVIWT DCDREGENIG MEIVNVCMAS NPRLDVYRAK
     FSEITRPAVQ RALASLTRMD ERVSDAVDAR QELDLRIGAA FTRFQTLRLR QVFPAVLADQ
     LVSYGSCQFP TLGFVVERFK EAERFQPEPF WRLRVLAESP DTGQSVEFLW KRGRVYDQAV
     GQMFLAHVLE SPIATVISVE SKPKNRWRPC ALDTVEFEKL ASRKLRINAK EAMHIAERLY
     TQGYISYPRT ETNIFPRDFN LRGLVQTQTA DNRWAQFAQR VAEHGPSPRN GKKSDQAHPP
     IHPLKCGDGL ANNEAKVFEL IARHFLACCS KDAVGREVKV GIDINGEGFE AKGLTIIERN
     YLEVYIYDKW VDKELPLFQQ GQQFQPSNIS LIDGCTTAPA LLTEADLIAL 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 GGGGGGGGGG GFQKANSHGN RRSGGGGGGG
     GGSDGGGGDG QKKQRKCGAC GQPGHTRNRC AMFIN
//
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