ID G1SQY7_RABIT Unreviewed; 978 AA.
AC G1SQY7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 24-JAN-2024, entry version 67.
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 Name=TOP3A {ECO:0000313|Ensembl:ENSOCUP00000005547.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005547.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005547.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005547.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005547.3};
RG Ensembl;
RL Submitted (JUL-2023) 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; G1SQY7; -.
DR SMR; G1SQY7; -.
DR STRING; 9986.ENSOCUP00000005547; -.
DR PaxDb; 9986-ENSOCUP00000005547; -.
DR Ensembl; ENSOCUT00000006415.3; ENSOCUP00000005547.3; ENSOCUG00000006409.3.
DR eggNOG; KOG1956; Eukaryota.
DR GeneTree; ENSGT00940000156701; -.
DR HOGENOM; CLU_002929_1_2_1; -.
DR InParanoid; G1SQY7; -.
DR TreeFam; TF105287; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000006409; Expressed in autopod skin and 19 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IEA:Ensembl.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051304; P:chromosome separation; IEA:Ensembl.
DR GO; GO:0006265; P:DNA topological change; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IEA:Ensembl.
DR GO; GO:0071139; P:resolution of recombination intermediates; IEA:Ensembl.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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 InterPro; IPR013498; Topo_IA_Znf.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
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 SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS50880; TOPRIM; 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:UP000001811};
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:PRU01343}.
FT DOMAIN 36..180
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 801..843
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 873..915
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 390..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 109058 MW; 0B78A5754776DA19 CRC64;
MIFPVARCAL RWWLRRPGER ASSRAAMEVA LRGARKVLCV AEKNDAAKGI ADLLSGGRMR
RREGLSKFNK IYEFDYHLCG QNVTMIMTSV SGHLLAHDFQ MQFRKWSSCN PLALFDAEIE
KYCPDNFVDI KKTLERETRQ CQALLIWTDC DREGENIGFE IIHVCKAVKP GLQVLRARFS
EITPRAVRAA CENLTEPDQR VSDAVDVRQE LDLRIGAAFT RFQTLRLQKI FPQVLAEQLI
SYGSCQFPTL GFVVERFKAI QAFVPEVFHR IKVTHAHRDG VVEFHWKRHR LFNHTACLVL
YQLCMEDPTA TVVEVRSKPK SKWRPQALDT VVCSRRNIAI SLSVCLCRYI SYPRTETNIF
PKDLNLTALV EQQTQDPRWG AFAQSILERG GPSPRNGNKS DQAHPPIHPT KYASSLQGDD
QRLYEFIVRH FLACCSQDAQ GQETTVEINI AQERFVAHGL VILARNYLDV YPYDHWSDKL
LPIYEQGSRF QPSTVEMVDG ETSPPQLLTE ADLIALMEKH GIGTDATHAE HIETIKARMY
VGLTPDKRFL PGHLGMGLVE GYDSMGYEMS KPDLRAELEA DLKLICEGKK DKSVVLRQQV
QKYKQVFIEA VAKAKKLDEA LSQYFGEGTE VAQQEELYPS LPEPIRKCPQ CHKDMVLKAK
KHGGFYLSCT GFPECRSAVW FPDSVLEASR DESVCPVCQP HPVYRVKFKF KRGSLPPTMP
LEFVGCVGGC DETLREILDL RFSRGPPRAS QPASQPSGHL QASQYLNRMD SRRHGHAQPP
DGRQSGPSKA PARALPGPHG RRHGRRHGEQ LCGCATAEGP NQGRQFYKCG AGGCSFFLWA
DSSPPAGGPP ASAPRPPPGS GGHGEGGAGA ASCLCSQPAV TRTVQKDGPN KGRQFHTCSK
PREQQCGFFQ WADENTAPGT FGAAPWPGGR GRAQGPEARS KRPRAGSSDA PGATAKKPRK
CSLCHQPGHT RPFCPQNR
//