ID W5M2K4_LEPOC Unreviewed; 763 AA.
AC W5M2K4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101};
DE AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002612.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002612.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC introduced during the DNA replication and transcription by transiently
CC cleaving and rejoining one strand of the DNA duplex. Introduces a
CC single-strand break via transesterification at the specific target site
CC 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is
CC attacked by the catalytic tyrosine of the enzyme, resulting in the
CC formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
CC expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC passage around the unbroken strand thus removing DNA supercoils.
CC Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC intermediate to expel the active-site tyrosine and restore the DNA
CC phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}.
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:RU365101};
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}.
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DR EMBL; AHAT01010624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01010625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01010626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M2K4; -.
DR STRING; 7918.ENSLOCP00000002612; -.
DR Ensembl; ENSLOCT00000002618.1; ENSLOCP00000002612.1; ENSLOCG00000002229.1.
DR eggNOG; KOG0981; Eukaryota.
DR GeneTree; ENSGT00940000166270; -.
DR InParanoid; W5M2K4; -.
DR OMA; RTANCQL; -.
DR Proteomes; UP000018468; Linkage group LG23.
DR Bgee; ENSLOCG00000002229; Expressed in ovary and 11 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR CDD; cd00659; Topo_IB_C; 1.
DR CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR025834; TopoI_C_dom.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR InterPro; IPR008336; TopoI_DNA-bd_euk.
DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR InterPro; IPR013499; TopoI_euk.
DR InterPro; IPR048045; Topoisomer_I_DNA-bd.
DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
DR PANTHER; PTHR10290:SF14; DNA TOPOISOMERASE I; 1.
DR Pfam; PF14370; Topo_C_assoc; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR Pfam; PF02919; Topoisom_I_N; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SMART; SM00435; TOPEUc; 1.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF46596; Eukaryotic DNA topoisomerase I, dispensable insert domain; 1.
DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 355..713
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 305..332
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 639..673
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 88708 MW; AEF3DF065C26B930 CRC64;
MGDTQTSSKD KEVKAKESKD KGFGKEEFRA GGDVSKSKKV QRNSTLGNTE GAEKEGKGIS
RKKKEKLTKR ENPDADLEDF VRAAQIQVKV EPEEEDFCIN KKDKVKKRLR EQEEPGGSLL
ESAKKKKKVK MEVEEAEQEP EKQRKKKKES KVKKAKKEQE GRPVSAREGG KHKKSKEEVE
AAKALKIKKK EEEELQRWRW WEEEKYEDGI KWKFLEHRGP WFPAEYQRLP DNVKFYYDGK
LVTLSSAAEE VAVFFAQMLD HEYTTKEVFR NNFFSDWRKE MTLEEKMIIT DLNKCDFSEI
YKMHKEKVEA RKNQGKEEKQ KTKDANQKLL EEYGYCTLDH HRERIGNFKI EPPGLFRGRG
DHPKQGMLKK RIQPEDVIIN CSKDSKIPQP PLGHQWKEVR CDNTVTWLAS WTENVQGLCK
YVMLNANSKL KGEKDWEKYE IARKLKSCVE TIRTQYQADL KSKQMGIRQR AVALYFIDKL
ALRAGNEKEE GETADTVGCC SLRVEHISLH PELDGEKYVV EFDFLGKDCI RYYNKVPVEK
AVFKNLKLFM EDKQPGDDLF DRLNTAMLNK HLHSLMAGLT AKVFRTYNAS ITLQQQLKEL
TNALDNIPEK ILSYNRANRA VAILCNHQRA PPKTFEQSMA NLQAKIDNRK EQLSLAKKEL
KQAKKDAKDH ADDKLLANVF MLHAKETVDK CPWKMNCISL QMLNRTANCQ LTSCSCMALL
YSNRPTAVRE CRKMEVSLEK IYNKTQRDKF AWAIDMTESD FVF
//
