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

6 structures for P38336

Entry ID Method Resolution Chain Position Source
6AGB EM 348 A D 1-279 PDB
6AH3 EM 348 A D 1-279 PDB
6W6V EM 300 A D 1-279 PDB
7C79 EM 250 A D 1-279 PDB
7C7A EM 280 A D 1-279 PDB
AF-P38336-F1 Predicted AlphaFoldDB

4 variants for P38336

Variant ID(s) Position Change Description Diseaes Association Provenance
s02-728909 10 D>E No SGRP
s02-729067 63 V>A No SGRP
s02-729193 105 K>R No SGRP
s02-729229 117 D>G No SGRP

No associated diseases with P38336

No regional properties for P38336

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P38336

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
nucleolar ribonuclease P complex A ribonuclease P complex located in the nucleolus of a eukaryotic cell, where it catalyzes the 5' endonucleolytic cleavage of precursor tRNAs to yield mature tRNAs. Eukaryotic nucleolar ribonuclease P complexes generally contain a single RNA molecule that is necessary but not sufficient for catalysis, and several protein molecules.
ribonuclease MRP complex A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication.
ribonuclease P complex A ribonucleoprotein complex that catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs.

3 GO annotations of molecular function

Name Definition
ribonuclease P RNA binding Binding to RNA subunit of ribonuclease P.
RNA binding Binding to an RNA molecule or a portion thereof.
rRNA primary transcript binding Binding to an unprocessed ribosomal RNA transcript.

7 GO annotations of biological process

Name Definition
intronic box C/D RNA processing Any process involved in the conversion of a primary box C/D type small nucleolar RNA (snoRNA) transcript that resides within, and is processed from, the intron of a pre-mRNA into a mature box C/D snoRNA.
maturation of 5.8S rRNA Any process involved in the maturation of a precursor 5.8S ribosomal RNA (rRNA) molecule into a mature 5.8S rRNA molecule.
nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay A minor degradation pathway nuclear-transcribed mRNAs that begins with an endonucleolytic cleavage to generate unprotected ends.
RNA phosphodiester bond hydrolysis, endonucleolytic The chemical reactions and pathways involving the hydrolysis of internal 3',5'-phosphodiester bonds in one or two strands of ribonucleotides.
rRNA processing Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
tRNA 5'-leader removal Generation of the mature 5'-end of the tRNA, usually via an endonucleolytic cleavage by RNase P.
tRNA processing The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O95707 POP4 Ribonuclease P protein subunit p29 Homo sapiens (Human) PR
10 20 30 40 50 60
MDRTQTFIKD CLFTKCLEDP EKPFNENRFQ DTLLLLPTDG GLTSRLQRQQ RKSKLNLDNL
70 80 90 100 110 120
QKVSQLESAD KQLEKRDYQR INKNSKIALR EYINNCKKNT KKCLKLAYEN KITDKEDLLH
130 140 150 160 170 180
YIEEKHPTIY ESLPQYVDFV PMYKELWINY IKELLNITKN LKTFNGSLAL LKLSMADYNG
190 200 210 220 230 240
ALLRVTKSKN KTLIGLQGIV IWDSQKFFIM IVKGNIIDEI KCIPKKGTVF QFEIPISDDD
250 260 270
DSALRYSILG DRFKYRSVDR AGRKFKSRRC DDMLYYIQN