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Database: UniProt
Entry: G1SQY7_RABIT
LinkDB: G1SQY7_RABIT
Original site: G1SQY7_RABIT 
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
//
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