Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O70157

Entry ID Method Resolution Chain Position Source
AF-O70157-F1 Predicted AlphaFoldDB

57 variants for O70157

Variant ID(s) Position Change Description Diseaes Association Provenance
rs241887321 13 H>Q No EVA
rs3389157721 37 L>V No EVA
rs3389102653 44 D>E No EVA
rs3389162818 77 L>P No EVA
rs3402300201 111 L>P No EVA
rs3389165001 132 T>N No EVA
rs3389166106 136 E>D No EVA
rs240593895 166 A>T No EVA
rs3402356764 190 C>R No EVA
rs3389177168 196 P>R No EVA
rs3389171273 214 I>V No EVA
rs3389171287 250 G>* No EVA
rs3389173400 280 T>S No EVA
rs3401072766 304 M>I No EVA
rs3389177139 379 L>S No EVA
rs3389166101 391 A>P No EVA
rs3389151199 408 S>I No EVA
rs3389177181 410 S>Y No EVA
rs259071846 425 G>A No EVA
rs47853877 425 G>S No EVA
rs3389175672 457 E>* No EVA
rs3389161340 467 A>T No EVA
rs3389173439 470 L>R No EVA
rs3389138745 476 N>S No EVA
rs3389126623 530 H>Y No EVA
rs3402356740 548 R>W No EVA
rs3402293024 549 M>L No EVA
rs3389173483 571 G>S No EVA
rs3389171300 583 D>E No EVA
rs3389151133 614 K>M No EVA
rs3389165021 664 D>E No EVA
rs3389102718 664 D>G No EVA
rs232465818 680 M>V No EVA
rs51299671 728 A>T No EVA
rs3389134744 737 I>T No EVA
rs48135735 761 Q>H No EVA
rs26971987 781 N>S No EVA
rs3389175714 788 N>Y No EVA
rs244858664 792 R>G No EVA
rs215120009 798 A>S No EVA
rs252813547 800 A>T No EVA
rs233622691 810 S>N No EVA
rs3411059825 829 Q>L No EVA
rs243774875 842 N>S No EVA
rs46144596 855 H>N No EVA
rs3389138800 865 A>V No EVA
rs3402275431 881 S>C No EVA
rs3389157674 888 S>I No EVA
rs46779599 897 T>A No EVA
rs47051744 898 P>S No EVA
rs3389162543 915 P>S No EVA
rs3389173437 930 Q>E No EVA
rs3389161298 937 W>C No EVA
rs3389175704 950 P>R No EVA
rs3389161283 957 G>* No EVA
rs263288118 998 F>L No EVA
rs3389162550 999 C>G No EVA

No associated diseases with O70157

10 regional properties for O70157

Type Name Position InterPro Accession
domain DNA topoisomerase, type IA, domain 2 172 - 269 IPR003601
domain DNA topoisomerase, type IA, DNA-binding domain 315 - 569 IPR003602
domain TOPRIM domain 35 - 181 IPR006171
domain Zinc finger, GRF-type 813 - 854 IPR010666-1
domain Zinc finger, GRF-type 898 - 941 IPR010666-2
domain DNA topoisomerase, type IA, central 143 - 156 IPR013497-1
domain DNA topoisomerase, type IA, central 196 - 617 IPR013497-2
domain DNA topoisomerase, type IA, zn finger 655 - 693 IPR013498
active_site DNA topoisomerase, type IA, active site 352 - 366 IPR023406
domain DNA topoisomerase 3-like, TOPRIM domain 35 - 193 IPR034144

Functions

Description
EC Number 5.6.2.1 Enzymes altering nucleic acid conformation
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
PML body A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.
RecQ family helicase-topoisomerase III complex A complex containing a RecQ family helicase and a topoisomerase III homologue (a member of the topoisomerase type IA subfamily); may also include one or more additional proteins; conserved from E. coli to human.

4 GO annotations of molecular function

Name Definition
DNA topoisomerase activity Catalysis of the transient cleavage and passage of individual DNA strands or double helices through one another, resulting a topological transformation in double-stranded DNA.
DNA topoisomerase type I (single strand cut, ATP-independent) activity Catalysis of a DNA topological transformation by transiently cleaving one DNA strand at a time to allow passage of another strand; changes the linking number by +1 per catalytic cycle.
single-stranded DNA binding Binding to single-stranded DNA.
zinc ion binding Binding to a zinc ion (Zn).

5 GO annotations of biological process

Name Definition
chromosome separation The cell cycle process in which paired chromosomes are detached from each other. Chromosome separation begins with the release of cohesin complexes from chromosomes; in budding yeast, this includes the cleavage of cohesin complexes along the chromosome arms, followed by the separation of the centromeric regions. Chromosome separation also includes formation of chromatid axes mediated by condensins, and ends with the disentangling of inter-sister catenation catalyzed by topoisomerase II (topo II).
DNA topological change The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.
double-strand break repair via homologous recombination The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.
mitochondrial DNA metabolic process The chemical reactions and pathways involving mitochondrial DNA.
resolution of recombination intermediates The cleavage and rejoining of intermediates, such as Holliday junctions, formed during DNA recombination to produce two intact molecules in which genetic material has been exchanged.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P13099 TOP3 DNA topoisomerase 3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q13472 TOP3A DNA topoisomerase 3-alpha Homo sapiens (Human) PR
Q9Z321 Top3b DNA topoisomerase 3-beta-1 Mus musculus (Mouse) PR
C7J0A2 TOP3A DNA topoisomerase 3-alpha Oryza sativa subsp japonica (Rice) PR
Q9LVP1 TOP3A DNA topoisomerase 3-alpha Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MIFPVTLLAF QWHRRPGGRA LSRAAMEVAF RGVRKVLCVA EKNDAAKGIA DLLSNGRMRR
70 80 90 100 110 120
KEGLSKFNKI YEFDYHLYGQ NVTMIMTSVS GHLLAHDFQM QFRKWQSCNP LVLFEAEIEK
130 140 150 160 170 180
YCPENFIDIK KTLERETHHC QALVIWTDCD REGENIGFEI IHVCKAVKPN LRVLRARFSE
190 200 210 220 230 240
ITPHAVRTAC ENLTEPDQRV SDAVDVRQEL DLRIGAAFTR FQTLRLQRIF PEVLAEQLIS
250 260 270 280 290 300
YGSCQFPTLG FVVERFKAIQ AFVPEVFHKI KVTHDHKDGT VEFNWKRYRL FNHTACLVLY
310 320 330 340 350 360
QLCMEDPMAT VVEVRSKPKS KWRPQALDTV ELEKLASRKL RINAKETMRI AEKLYTQGYI
370 380 390 400 410 420
SYPRTETNIF PKDLNLVALV EQQTVDPHWG AFAQTILERG GPTPRNGSKS DQAHPPIHPT
430 440 450 460 470 480
KYTSGLQGDD RRLYEFIVRH FLACCSQDAQ GQETTVEIDI AQERFVAHGL IILARNYLDV
490 500 510 520 530 540
YPYDHWSDKL LPVYEQGSHF QPSTVEMVDG ETSPPQLLTE ADLIALMEKH GIGTDATHAE
550 560 570 580 590 600
HIETIKARMY VGLTSDKRFL PGHLGMGLVE GYDSMGYEMS KPDLRAELEA DLKLICEGKK
610 620 630 640 650 660
DKFQVLRQQV QKYKQVFIEA VAKAKKLDEA LSQYLGERTE MAQQEEIYPA MPEPVRKCPQ
670 680 690 700 710 720
CNKDMVLKTK KSGGFYLSCM GFPECRSAVW FPDSVLEASR DNSVCSVCQP PPVYRLKLKF
730 740 750 760 770 780
KRGSLPPAMP LEFVGCIGGC DETLKEIFGL RFPRALPRAS QPSGHLQASQ ALNRMDSSQH
790 800 810 820 830 840
NLSQPLVNRH TRPSKTVAQA LLPPTTAGES NSVTCNCGRE AVLLTVRKQG PNQGRHFYKC
850 860 870 880 890 900
SNGDCNFFLW ADSSHSTGGG TPTSASGPPG SSVGCPSSVG SHMDGFGSLG SDSDGGTPCL
910 920 930 940 950 960
CGQPAVTRTV QKDGPNKGRQ FHTCAKPREQ QCGFFQWVDE NVAPGSFAAP AWPGGRGKAQ
970 980 990 1000
RPEAASKRPR AGSSDAGSTV KKPRKCSLCH QPGHTRTFCP QNR