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 Q9FGM0

Entry ID Method Resolution Chain Position Source
AF-Q9FGM0-F1 Predicted AlphaFoldDB

26 variants for Q9FGM0

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH03419196 25 P>S No 1000Genomes
ENSVATH12733129 28 F>L No 1000Genomes
ENSVATH07407405 43 F>L No 1000Genomes
tmp_5_21567770_G_T 51 H>Q No 1000Genomes
ENSVATH12733128 52 N>S No 1000Genomes
ENSVATH07407403 68 A>T No 1000Genomes
tmp_5_21567651_A_G 91 L>S No 1000Genomes
tmp_5_21567604_C_G 107 V>L No 1000Genomes
tmp_5_21567592_C_T 111 E>K No 1000Genomes
ENSVATH07407402 118 E>D No 1000Genomes
tmp_5_21567562_C_T 121 V>I No 1000Genomes
tmp_5_21567529_C_T 132 D>N No 1000Genomes
ENSVATH07407401 134 K>E No 1000Genomes
tmp_5_21567358_C_T 189 D>N No 1000Genomes
tmp_5_21567313_T_G 204 I>L No 1000Genomes
ENSVATH07407399 249 P>S No 1000Genomes
ENSVATH07407392 268 D>E No 1000Genomes
tmp_5_21566723_C_A 272 V>L No 1000Genomes
tmp_5_21566506_C_T 311 V>M No 1000Genomes
tmp_5_21566327_C_T 318 G>S No 1000Genomes
tmp_5_21565416_C_T 420 G>E No 1000Genomes
ENSVATH12733091 546 M>L No 1000Genomes
ENSVATH07407369 722 V>F No 1000Genomes
tmp_5_21563296_A_C 753 S>A No 1000Genomes
tmp_5_21563100_G_A 782 R>C No 1000Genomes
tmp_5_21563052_G_C 798 Q>E No 1000Genomes

No associated diseases with Q9FGM0

5 regional properties for Q9FGM0

Type Name Position InterPro Accession
domain Peptidase M41 608 - 783 IPR000642
domain AAA+ ATPase domain 394 - 529 IPR003593
domain ATPase, AAA-type, core 398 - 526 IPR003959
conserved_site ATPase, AAA-type, conserved site 497 - 515 IPR003960
domain AAA ATPase, AAA+ lid domain 549 - 590 IPR041569

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side
  • Plastid, chloroplast thylakoid membrane; Single-pass membrane protein; Stromal side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
chloroplast envelope The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
chloroplast thylakoid Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana.
chloroplast thylakoid membrane The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
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.
plastid Any member of a family of organelles found in the cytoplasm of plants and some protists, which are membrane-bounded and contain DNA. Plant plastids develop from a common type, the proplastid.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
metal ion binding Binding to a metal ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

3 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
PSII associated light-harvesting complex II catabolic process The chemical reactions and pathways resulting in the breakdown of one or more components of the light-harvesting complex of photosystem II.
response to heat Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O88967 Yme1l1 ATP-dependent zinc metalloprotease YME1L1 Mus musculus (Mouse) PR
Q8LQJ8 FTSH5 ATP-dependent zinc metalloprotease FTSH 5, mitochondrial Oryza sativa subsp japonica (Rice) PR
A2ZVG7 FTSH9 ATP-dependent zinc metalloprotease FTSH 9, chloroplastic/mitochondrial Oryza sativa subsp japonica (Rice) PR
O80983 FTSH4 ATP-dependent zinc metalloprotease FTSH 4, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q8W585 FTSH8 ATP-dependent zinc metalloprotease FTSH 8, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSSSTLQASL FLRPPLHTSS FKLYPCLFSS SSLSFCPQSL SSFYRLSSVL HNSRFRPLPC
70 80 90 100 110 120
SLRQDNVASD SDFIPKDSAF EVTDSAESNR LVSDTEVSEL ETNDRFVGGE ETKSGGEEAE
130 140 150 160 170 180
VSNGVTEGKE EDQKKSKFRI VVLMMALWAA IKRAIEKVME WEWLSWWPFS RQEKRLEKLI
190 200 210 220 230 240
AEADANPKDA ALQGALLAEL NKHIPEAVVQ RFEQREHTVD SRGVAEYIRA LVITNAISEY
250 260 270 280 290 300
LPDEQTGKPS SLPALLQELK HRASGNMDES FVNPGISEKQ PLHVTMVNPK VSNKSRFAQE
310 320 330 340 350 360
LVSTILFTVA VGLVWIMGAA ALQKYIGSLG GIGTSGVGSS SSYSPKELNK EITPEKNVKT
370 380 390 400 410 420
FKDVKGCDDA KQELEEVVEY LKNPSKFTRL GGKLPKGILL TGAPGTGKTL LAKAIAGEAG
430 440 450 460 470 480
VPFFYRAGSE FEEMFVGVGA RRVRSLFQAA KKKAPCIIFI DEIDAVGSTR KQWEGHTKKT
490 500 510 520 530 540
LHQLLVEMDG FEQNEGIIVM AATNLPDILD PALTRPGRFD RHIVVPSPDV RGREEILELY
550 560 570 580 590 600
LQGKPMSEDV DVKAIARGTP GFNGADLANL VNIAAIKAAV EGAEKLSSEQ LEFAKDRIVM
610 620 630 640 650 660
GTERKTMFVS EDSKKLTAYH ESGHAIVALN TKGAHPIHKA TIMPRGSALG MVTQLPSNDE
670 680 690 700 710 720
TSVSKRQLLA RLDVCMGGRV AEELIFGLDH ITTGASSDLS QATELAQYMV SSCGMSEAIG
730 740 750 760 770 780
PVHIKERPSS DMQSRIDAEV VKLLREAYER VKSLLKRHEK QLHTLANALL EYETLTAEDI
790 800
KRILLPKQEG EKFEEQQQEE GDLVLA