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TOP3A_DROME
ID   TOP3A_DROME             Reviewed;        1250 AA.
AC   Q9NG98; Q6AWG6; Q9VIV1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=DNA topoisomerase 3-alpha;
DE            EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE   AltName: Full=DNA topoisomerase III alpha;
GN   Name=Top3alpha; ORFNames=CG10123;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RA   Plank J.L., Reineke J.C., Wilson T.M., Hsieh T.-S.;
RT   "Drosophila melanogaster topoisomerase III alpha.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 a target site in duplex
CC       DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC       of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-
CC       enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free
CC       DNA strand than undergoes passage around the unbroken strand thus
CC       removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH
CC       attacks the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone (By similarity). Weakly relaxes
CC       negative supercoils and displays a distinct preference for binding
CC       single-stranded DNA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10131};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
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DR   EMBL; AF255733; AAF71288.1; -; mRNA.
DR   EMBL; AE014134; AAF53813.2; -; Genomic_DNA.
DR   EMBL; BT015282; AAT94511.1; -; mRNA.
DR   RefSeq; NP_523602.2; NM_078878.3.
DR   AlphaFoldDB; Q9NG98; -.
DR   SMR; Q9NG98; -.
DR   IntAct; Q9NG98; 4.
DR   MINT; Q9NG98; -.
DR   STRING; 7227.FBpp0080787; -.
DR   PaxDb; Q9NG98; -.
DR   PRIDE; Q9NG98; -.
DR   DNASU; 35236; -.
DR   EnsemblMetazoa; FBtr0081246; FBpp0080787; FBgn0040268.
DR   GeneID; 35236; -.
DR   KEGG; dme:Dmel_CG10123; -.
DR   CTD; 35236; -.
DR   FlyBase; FBgn0040268; Top3alpha.
DR   VEuPathDB; VectorBase:FBgn0040268; -.
DR   eggNOG; KOG1956; Eukaryota.
DR   GeneTree; ENSGT00940000156701; -.
DR   HOGENOM; CLU_002929_1_2_1; -.
DR   InParanoid; Q9NG98; -.
DR   OMA; WYKTCLP; -.
DR   OrthoDB; 373433at2759; -.
DR   PhylomeDB; Q9NG98; -.
DR   BioGRID-ORCS; 35236; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 35236; -.
DR   PRO; PR:Q9NG98; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0040268; Expressed in egg chamber and 22 other tissues.
DR   Genevisible; Q9NG98; DM.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IDA:FlyBase.
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:0048589; P:developmental growth; IMP:FlyBase.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:FlyBase.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IMP:FlyBase.
DR   GO; GO:0042246; P:tissue regeneration; IMP:FlyBase.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 1.10.290.10; -; 1.
DR   Gene3D; 1.10.460.10; -; 1.
DR   Gene3D; 2.70.20.10; -; 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; IPR010666; Znf_GRF.
DR   PANTHER; PTHR11390; PTHR11390; 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; SSF56712; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isomerase; Metal-binding; Reference proteome; Repeat;
KW   Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN           1..1250
FT                   /note="DNA topoisomerase 3-alpha"
FT                   /id="PRO_0000145195"
FT   DOMAIN          27..171
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   ZN_FING         1033..1075
FT                   /note="GRF-type 1"
FT   ZN_FING         1150..1192
FT                   /note="GRF-type 2"
FT   REGION          769..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..989
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1019..1035
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        356
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        111
FT                   /note="K -> E (in Ref. 1; AAF71288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1250 AA;  136137 MW;  108E4AC18EA5677A CRC64;
     MKAVLTCFRP VVASHRRYCA NPGQAMKYLN VAEKNDAAKT IAGLLSNGAA QRREGYSVYN
     KVFDFEAPVR GQNAKMVMTS VSGHMMQLAF QVSYKNWRTV DPRSLFDAPV KKGVGSDYEP
     IKRTLEREVR GCQGLIIWTD CDREGENIGY EIIDVCRAIK PNISVYRATF SEITTVAVRR
     ALQQLGQPDK RQSDAVDVRT ELDLRTGAAI TRFQTMRLQR LFPEKIADKL ISYGSCQIPT
     LGFVAERYKE IEAFVSEPFW KIKVLHTIDD LTVEFNWARN RLFDKEACEN YLLLCLAEPD
     PRALVESVTV KPKHKWRPTP LDTVEMEKLG SRKLKLSAKE TMTIAEKLYT KGFISYPRTE
     TNQFSKEFAL APLVEMQTGH RDWGAFAQRV IEWGPNPRNG NKSDQAHPPI HPTKLAENLQ
     GNEARVYELV VRHFLACVSK DAVGSETLVH IDIAGEKFTA NGLVIHERNY LDVYVYDKWS
     AKQIHHYENG QRFEPTEVSL HEGATTAPPL LTEADLIALM EKHGIGTDAT HAEHINTIKE
     RGYIGVLDKG FLVPGVIGMG LYEGYDAMEL ALAKPQLRAE FELDLKLICQ GQKDPKVVLT
     EQIAKYKQAY QQITDKITAM DAKISARINE TPAANSAVQE GADGSAPSHG IIQSIFQCPK
     CNEAPLALKP KKNQQGWYIG CNNFPDCKNA VWLPTECKDA SVLDECCPTC GDGYRMLKFR
     LSTPYYRGVF GTPSGWYKTC LPCDNLFRTT FNINLDSVKK VGGIVGEVRG GGGGPGPGPG
     GGGSGRGAGS GGWSSGPGGG GSGGGGGSGG WGSGTGGGGS GGWGSGTGGG GLGGGKGKKP
     GGESKKSATK KPPNEPKPKK TKEPKAAPNK KTSSKSSGSI RSFFTSAAPT NSASNGLDEF
     FDSNDGFEDA MLAAAESVES SSQPKTISMV PLDDDIAAAF AADDDAEFEA LVNGGTMPTE
     SNGDQQLDKS LSEWIKEQDK ADERPMLWGT RERASLGTAA PTPPPKPAAK RPRWDSVERD
     STPPSSVPES ETVLCTGCQQ PARQNTVRKN GPNLGRLYYK CPKPDECNFF QWADEPPSSA
     KSKNSTGSAP QSTTSWGSNR VVTLPSIQQS NSQRGQSSMR SNSSSTVTIT QTKTKQQERN
     TATPGDGEEV MCNCGQLASQ LTVRKDGPNQ GRPFYACPTR EKSCGFFKWG DEDQNQGASS
     TSWGSANRNP PGRSQPTAIT SDGPKTRRCG LCRKEGHTRN KCPRKDEFDM
 
 
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