Q06678

PR
Gene name
MRPL35 (YDR322W, D9798.5)
Protein name
54S ribosomal protein L35, mitochondrial
Names
Mitochondrial large ribosomal subunit protein mL38, YmL35
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YDR322W
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-89 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for Q06678

Entry ID Method Resolution Chain Position Source
3J6B EM 320 A 1 1-367 PDB
5MRC EM 325 A 1 20-367 PDB
5MRE EM 375 A 1 20-367 PDB
5MRF EM 497 A 1 20-367 PDB
AF-Q06678-F1 Predicted AlphaFoldDB

8 variants for Q06678

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-1110665 27 T>I No SGRP
s04-1110983 133 D>G No SGRP
s04-1111102 173 V>I No SGRP
s04-1111207 208 I>V No SGRP
s04-1111243 220 E>K No SGRP
s04-1111411 276 L>I No SGRP
s04-1111453 290 V>I No SGRP
s04-1111623 346 K>N No SGRP

No associated diseases with Q06678

No regional properties for Q06678

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q06678

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
  • Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial large ribosomal subunit The larger of the two subunits of a mitochondrial ribosome. Two sites on the ribosomal large subunit are involved in translation: the aminoacyl site (A site) and peptidyl site (P site).
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.

3 GO annotations of molecular function

Name Definition
peptidase inhibitor activity Binds to and stops, prevents or reduces the activity of a peptidase, any enzyme that catalyzes the hydrolysis peptide bonds.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.
structural constituent of ribosome The action of a molecule that contributes to the structural integrity of the ribosome.

3 GO annotations of biological process

Name Definition
mitochondrial translation The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
regulation of proteolysis Any process that modulates the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
regulation of Ras protein signal transduction Any process that modulates the frequency, rate or extent of Ras protein signal transduction.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O82088 SP Protein SELF-PRUNING Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MLRRSIHTTK ILQKPNATSH IWSDFTTRPS SLSIQSSKVK NYLFQKKASL DPPSISRRSN
70 80 90 100 110 120
RIKYSPPEHI DEIFRMSYDF LEQRSSKFYE LANKTKNPLK KDALLIKAEI NNPEVQYNFQ
130 140 150 160 170 180
FNNKLNNVKD IIDYDVPVYR HLGKQHWESY GQMLLMQRLE TLAAIPDTLP TLVPRAEVNI
190 200 210 220 230 240
KFPFSTGVNK WIEPGEFLSS NVTSMRPIFK IQEYELVNVE KQLYTVLIVN PDVPDLSNDS
250 260 270 280 290 300
FKTALCYGLV NINLTYNDNL IDPRKFHSSN IIADYLPPVP EKNAGKQRFV VWVFRQPLIE
310 320 330 340 350 360
DKQGPNMLEI DRKELSRDDF DIRQFTKKYN LTAIGAHIWR SEWDAKVAAV REKYGLPPGR
VFSRVRR