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 Q4R366

Entry ID Method Resolution Chain Position Source
AF-Q4R366-F1 Predicted AlphaFoldDB

No variants for Q4R366

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4R366

No associated diseases with Q4R366

2 regional properties for Q4R366

Type Name Position InterPro Accession
domain Protein-only RNase P, C-terminal 340 - 576 IPR031595
domain Mitochondrial ribonuclease P catalytic subunit, PIN domain 404 - 526 IPR033495

Functions

Description
EC Number 3.1.26.5 Endoribonucleases producing 5'-phosphomonoesters
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial ribonuclease P complex A ribonuclease P complex located in the mitochondrion of a eukaryotic cell, where it catalyzes the 5' endonucleolytic cleavage of precursor tRNAs to yield mature tRNAs. The subunit composition of mitochondrial ribonuclease P complexes varies between species. The complex contains a single RNA molecule and a single protein molecule in yeast (PMID:12045094), but comprises three proteins and lacks an RNA component in humans.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
ribonuclease P activity Catalysis of the endonucleolytic cleavage of RNA, removing 5' extra nucleotides from tRNA precursor.

1 GO annotations of biological process

Name Definition
mitochondrial tRNA 5'-end processing The process in which the 5' end of a pre-tRNA molecule is converted to that of a mature tRNA in the mitochondrion.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTFYLFGIRS FPKLWKSNPY LGLGPGHSYV SLFLSDSCGI RSQQRLFSLK TMSPQNTKAT
70 80 90 100 110 120
NLIAKARYLR KEEGSNKQVS SVPHFFSAGA AKKRSQMNPQ SKDHALPSVR NTIQLPTQPL
130 140 150 160 170 180
NSEEWDKLKA DFKGKTSFER FIISQMAHSH SSVDVAKSLL AWVAAKNNGI VSYDLLVGYL
190 200 210 220 230 240
YLCVFHMQTS EVIDVFEIMK TRYKTLEPGG YSLLIQGLIH SDRWRESLLL LEDIKKVITP
250 260 270 280 290 300
SKKNYNDCIQ GALLHQDINT AWNLYQELLG HDFVPMLETL KAFFDFGKDI KDDNYSNKLL
310 320 330 340 350 360
DILSYLRNNQ LYPGESFAHS IKTWFESVPG KQWKGQFTTV QKSGQCLGCG KTIESIQLSP
370 380 390 400 410 420
EEYEFLKGRI MRDVIDGGDQ YKKTTPQELK RFENFVKSCP PFDIVIDGLN VAKMFPKARE
430 440 450 460 470 480
SQVLLNVVSQ LAKQNLRLLV LGRKHMLRQS FQWRKDEMAE VQKQASCFFA DNISKDDPFL
490 500 510 520 530 540
LYATLHSGNH CRFITKDLMR DHKACLPDAK TQRLFFKWQQ GHQLAIINGF PGSKLTFQHI
550 560 570 580
LSYDTVVQTT GDSWHIPYDE DVVERYSYEV PTKWLCLHQK T