Reviewed, UniProtKB/Swiss-Prot P30189 (TOP1_DROME)

Names and origin

Protein names

Recommended name:
    DNA topoisomerase 1
    EC=5.99.1.2
Alternative name(s):
    DNA topoisomerase I

Gene names

Name:	Top1
ORF Names:	CG6146

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	972 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another.
Catalytic activity	ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Subunit structure	Interacts with Topors. Ref.5
Subcellular location	Nucleus By similarity.
Miscellaneous	Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils. When a topoisomerase transiently breaks a DNA backbone bond, it simultaneously forms a protein-DNA link, in which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus at one end of the enzyme-severed DNA strand.
Sequence similarities	Belongs to the eukaryotic type I topoisomerase family.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA topological change Inferred from direct assay. Source: FlyBase DNA unwinding during replication Inferred from electronic annotation. Source: InterPro cell proliferation Inferred from mutant phenotype. Source: FlyBase chromosome condensation Inferred from mutant phenotype. Source: FlyBase chromosome segregation Inferred from mutant phenotype. Source: FlyBase embryonic development Inferred from mutant phenotype. Source: FlyBase instar larval development Inferred from mutant phenotype. Source: FlyBase oogenesis Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from direct assay. Source: FlyBase nucleolus Inferred from direct assay. Source: FlyBase polytene chromosome puff Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: InterPro DNA topoisomerase type I activity Ref.1 Inferred from direct assay. Source: FlyBase protein binding Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Topors	Q9V8P9	1	EBI-108030,EBI-147805

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 972	972	DNA topoisomerase 1		PRO_0000145205
Regions
	Compositional bias	32 – 39	8	Poly-His
	Compositional bias	40 – 198	159	Ser-rich
Sites
	Active site	930	1	O-(3'-phospho-DNA)-tyrosine intermediate By similarity
Amino acid modifications
	Modified residue	303	1	Phosphoserine Ref.6
	Modified residue	304	1	Phosphotyrosine Ref.6
Experimental info
	Sequence conflict	40	1	S → H Ref.3
	Sequence conflict	46	1	S → SSS Ref.3
	Sequence conflict	201	1	H → Q in AAF48440. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P30189-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 3764B8BDEEFA30CD	FASTA	972	111,688
	10 20 30 40 50 60 MSGDVAAENS IHIQNGGSCE VVQSNGVTTN GHGHHHHHHS SSSSSSKHKS SSKDKHRDRE 70 80 90 100 110 120 REHKSSNSSS SSKEHKSSSR DKDRHKSSSS SSKHRDKDKE RDGSSNSHRS GSSSSHKDKD 130 140 150 160 170 180 GSSSSKHKSS SGHHKRSSKD KERRDKDKDR GSSSSSRHKS SSSSRDKERS SSSHKSSSSS 190 200 210 220 230 240 SSSKSKHSSS RHSSSSSSKD HPSYDGVFVK PEPVSQQLMH SGSVDAFQMQ QLGSYEAAAA 250 260 270 280 290 300 GTNFNGNGNV AGANYKNGYE ESIVDIKKEE ESFNNLSQAS SCDYSMSQFR ADEPPFVVKH 310 320 330 340 350 360 EQSYAEEDST MNYNDHDDDA DEMNDDEEDV PLAMRKRKQE ATDRPDGGMD NDDDDDIPLL 370 380 390 400 410 420 ARKKVKKEKI KKESKEKSKK RVKEEPSDDY GNVKPKKKKM KKEPEPAVSP GKRQKAKAKV 430 440 450 460 470 480 EEEEVWRWWE EEKRADGVKW STLEHKGPVF APRYERVPRN VRFYYDGKPL ELSEETEEAA 490 500 510 520 530 540 TFYAKMLNHD YCTKEVFNNN FFKDFRKSMT PREREIIKDF RKCNFQEMFN YFQAESEKRK 550 560 570 580 590 600 AASKEEKLIK KNENEALMKE FGFCMIDGHK EKIGNFRLEP PGLFRGRGEH PKMGMIKRRI 610 620 630 640 650 660 QASDVSINCG KDSKVPSPPP GSRWKEVRHD NTVTWLASWI ENVQGQVKYI MLNPSSKLKG 670 680 690 700 710 720 EKDHIKYETA RRLDKVIDKI RATYRDEWKS KEMRVRQRAV ALYFIDKLAL RAGNEKDEDQ 730 740 750 760 770 780 ADTVGCCSLR VEHVQLHKEL NGKENVVVFD FPGKDSIRYY NEVEVEKRVF KNLELFMEHK 790 800 810 820 830 840 KEGDDLFDRL NTQVLNEHLK ELMEGLTAKV FRTYNASKTL QSQLDLLTDP SATVPEKLLA 850 860 870 880 890 900 YNRANRAVAI LCNHQRSVPK SHEKSMENLK EKIKAKREAI EKCESEYHSR DEKKGKQLER 910 920 930 940 950 960 LRDQLKKLEL QETDRDENKT IALGTSKLNY LDPRISVAWC KKHDVPIEKI FNKTQRTKFL 970 WAVHMADENY RF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a gene encoding DNA topoisomerase I in Drosophila melanogaster." Hsieh T.-S., Brown S.D., Huang P., Fostel J. Nucleic Acids Res. 20:6177-6182(1992) [PubMed: 1335568] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation and characterization of a Drosophila gene essential for early embryonic development and formation of cortical cleavage furrows." Zhang C.X., Lee M.P., Chen A.D., Brown S.D., Hsieh T.-S. J. Cell Biol. 134:923-934(1996) [PubMed: 8769417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Oregon-R.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"Drosophila Topors is a RING finger-containing protein that functions as a ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix repressor protein." Secombe J., Parkhurst S.M. J. Biol. Chem. 279:17126-17133(2004) [PubMed: 14871887] [Abstract] Cited for: INTERACTION WITH TOPORS.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND TYR-304, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M74557 mRNA. Translation: AAA28951.1. U80064 Genomic DNA. Translation: AAC24158.1. AE014298 Genomic DNA. Translation: AAF48440.1.
PIR	S35521.
RefSeq	NP_001014742.1. NP_511161.2.
UniGene	Dm.2912
3D structure databases
SMR	P30189. Positions 426-972.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30189. 2 interactions.
STRING	P30189.
Proteomic databases
PRIDE	P30189.
Genome annotation databases
Ensembl	FBtr0074005; FBpp0073822; FBgn0004924; Drosophila melanogaster. [Genome view] FBtr0074006; FBpp0073823; FBgn0004924; Drosophila melanogaster. [Genome view] FBtr0100294; FBpp0099689; FBgn0004924; Drosophila melanogaster. [Genome view]
GeneID	32458.
KEGG	dme:Dmel_CG6146.
Organism-specific databases
CTD	32458.
FlyBase	FBgn0004924. Top1.
Phylogenomic databases
eggNOG	inNOG04814.
InParanoid	P30189.
PhylomeDB	P30189.
Enzyme and pathway databases
BRENDA	5.99.1.2. 48.
Gene expression databases
Bgee	P30189.
GermOnline	CG6146. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011010. DNA_brk_join_enz. IPR018521. TopoI_AS. IPR001631. TopoI_C. IPR013499. TopoI_C_euk. IPR014711. TopoI_cat_a-hlx-sub_euk. IPR014727. TopoI_cat_a/b-sub_euk. IPR013030. TopoI_DNA-bd_mixed-a/b_euk. IPR008336. TopoI_DNA_bd_euk. IPR009054. TopoI_insert_euk. [Graphical view]
Gene3D	G3DSA:3.90.15.10. TopoI_cat_a-hlx-sub_euk. 1 hit. G3DSA:1.10.132.10. TopoI_cat_a/b-sub_euk. 1 hit. G3DSA:2.170.11.10. TopoI_DNA-bd_mixed-a/b_euk. 1 hit.
Pfam	PF02919. Topoisom_I_N. 1 hit. [Graphical view]
PRINTS	PR00416. EUTPISMRASEI.
SMART	SM00435. TOPEUc. 1 hit. [Graphical view]
PROSITE	PS00176. TOPOISOMERASE_I_EUK. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	778562.

Entry information

Entry name

TOP1_DROME

Accession

Primary (citable) accession number: P30189
Secondary accession number(s): Q9VXW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	February 9, 2010
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project