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 Q33DR2

Entry ID Method Resolution Chain Position Source
AF-Q33DR2-F1 Predicted AlphaFoldDB

21 variants for Q33DR2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs1132205163 4 R>H No EVA
rs3391340348 8 W>R No EVA
rs3391342976 8 W>S No EVA
rs3391361080 9 R>P No EVA
rs3388530889 21 S>C No EVA
rs247403468 22 P>L No EVA
rs263478551 24 R>P No EVA
rs3388532830 30 V>M No EVA
rs3388530260 61 M>I No EVA
rs3412781068 61 M>L No EVA
rs3388530976 164 E>* No EVA
rs3388531979 212 A>D No EVA
rs3388530918 232 L>M No EVA
rs3388530310 277 C>S No EVA
rs3388526477 281 V>M No EVA
rs3388533683 331 L>S No EVA
rs3388530861 353 D>H No EVA
rs3388531931 357 A>V No EVA
rs3388530966 363 Q>H No EVA
rs3388528706 401 S>* No EVA
rs3388528758 408 D>E No EVA

No associated diseases with Q33DR2

2 regional properties for Q33DR2

Type Name Position InterPro Accession
conserved_site Polyprenyl synthetase, conserved site 171 - 185 IPR033749-1
conserved_site Polyprenyl synthetase, conserved site 293 - 305 IPR033749-2

Functions

Description
EC Number 2.5.1.91 Transferring alkyl or aryl groups, other than methyl groups
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
transferase complex A protein complex capable of catalyzing the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor).

6 GO annotations of molecular function

Name Definition
all-trans-decaprenyl-diphosphate synthase activity Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate.
all-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) activity Catalysis of the reaction: geranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-nonaprenyl diphosphate.
metal ion binding Binding to a metal ion.
prenyltransferase activity Catalysis of the transfer of a prenyl group from one compound (donor) to another (acceptor).
protein heterodimerization activity Binding to a nonidentical protein to form a heterodimer.
trans-hexaprenyltranstransferase activity Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate.

2 GO annotations of biological process

Name Definition
isoprenoid biosynthetic process The chemical reactions and pathways resulting in the formation of an isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
ubiquinone biosynthetic process The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5T2R2 PDSS1 All trans-polyprenyl-diphosphate synthase PDSS1 Homo sapiens (Human) PR
O22043 GGPP6 Geranylgeranyl pyrophosphate synthase 6, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAMRWSCWRR GCSWRPTAVG SPRRERPGCV EPLGTRAASD TRAQIPYFSL MKILMSASPT
70 80 90 100 110 120
MHSISQFHQR TPAMCSCRQT QSGEKYSDPF KLGWRDLKGL YEDIRKELHI STRELKDMSE
130 140 150 160 170 180
YYFDGKGKAF RPIIVVLMAR ACNIHHNNAR EMQASQRSIA LVAEMIHTAT LVHDDVIDDA
190 200 210 220 230 240
SSRRGKHTVN KIWGEKKAVL AGDLILSAAS VALARIGNTA VVSMLAQVIE DLVRGEFLQL
250 260 270 280 290 300
GSKENENERF AHYLEKTFKK TASLIANSCK AVSVLGCPDP VVHEIAYQYG KNVGIAFQLI
310 320 330 340 350 360
DDVLDFTSCS DQMGKPTSAD LKLGIATGPV LFACQQFPEM NAMIMRRFSL PGDVDRARQY
370 380 390 400
VLQSDGVQQT TYLAQQYCHK AVREIRKLRP STERDALIQL SESVLTRDK