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

4 structures for P37107

Entry ID Method Resolution Chain Position Source
2HUG NMR - B 530-543 PDB
3UI2 X-ray 318 A B 528-540 PDB
5L3R X-ray 250 A A/C 77-371 PDB
AF-P37107-F1 Predicted AlphaFoldDB

20 variants for P37107

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_5_1063241_A_T 6 F>Y No 1000Genomes
tmp_5_1063182_C_G,T 26 A>P No 1000Genomes
tmp_5_1063182_C_G,T 26 A>T No 1000Genomes
tmp_5_1063169_G_A 30 S>F No 1000Genomes
ENSVATH10550552 36 T>A No 1000Genomes
ENSVATH06918677 60 K>Q No 1000Genomes
tmp_5_1062688_C_T 97 V>I No 1000Genomes
ENSVATH13911814 125 R>K No 1000Genomes
tmp_5_1062514_C_T 131 V>I No 1000Genomes
tmp_5_1062469_G_C 146 P>A No 1000Genomes
tmp_5_1062282_T_G 165 E>D No 1000Genomes
ENSVATH10550497 221 D>A No 1000Genomes
ENSVATH10550495 278 D>G No 1000Genomes
ENSVATH03018896 290 T>I No 1000Genomes
ENSVATH06918662 391 A>V No 1000Genomes
ENSVATH00605413 452 M>I No 1000Genomes
ENSVATH03018892 482 G>A No 1000Genomes
tmp_5_1060305_G_A 552 S>L No 1000Genomes
ENSVATH06918654 554 K>N No 1000Genomes
ENSVATH06918653 555 P>S No 1000Genomes

No associated diseases with P37107

4 regional properties for P37107

Type Name Position InterPro Accession
domain Signal recognition particle, SRP54 subunit, GTPase domain 176 - 371 IPR000897
domain AAA+ ATPase domain 175 - 322 IPR003593
domain Signal recognition particle, SRP54 subunit, M-domain 402 - 500 IPR004125
domain Signal recognition particle SRP54, helical bundle 77 - 162 IPR013822

Functions

Description
EC Number 3.6.5.4 Acting on GTP; involved in cellular and subcellular movement
Subcellular Localization
  • Plastid, chloroplast stroma
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 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 stroma The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
signal recognition particle, endoplasmic reticulum targeting A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana.

4 GO annotations of molecular function

Name Definition
7S RNA binding Binding to a 7S RNA, the RNA component of the signal recognition particle (SRP).
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
protein domain specific binding Binding to a specific domain of a protein.

2 GO annotations of biological process

Name Definition
protein heterotrimerization The formation of a protein heterotrimer, a macromolecular structure consisting of three noncovalently associated subunits, of which not all are identical.
SRP-dependent cotranslational protein targeting to membrane The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2T9U1 SRP54 Signal recognition particle 54 kDa protein Bos taurus (Bovine) PR
P61010 SRP54 Signal recognition particle 54 kDa protein Canis lupus familiaris (Dog) (Canis familiaris) PR
P61011 SRP54 Signal recognition particle 54 kDa protein Homo sapiens (Human) PR
P14576 Srp54 Signal recognition particle 54 kDa protein Mus musculus (Mouse) PR
Q6AYB5 Srp54 Signal recognition particle 54 kDa protein Rattus norvegicus (Rat) PR
P49966 SRP-54B Signal recognition particle 54 kDa protein 2 Arabidopsis thaliana (Mouse-ear cress) PR
P49971 Signal recognition particle 54 kDa protein 1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
P49972 Signal recognition particle 54 kDa protein 2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MEALQFSSVN RVPCTLSCTG NRRIKAAFSS AFTGGTINSA SLSSSRNLST REIWSWVKSK
70 80 90 100 110 120
TVVGHGRYRR SQVRAEMFGQ LTGGLEAAWS KLKGEEVLTK DNIAEPMRDI RRALLEADVS
130 140 150 160 170 180
LPVVRRFVQS VSDQAVGMGV IRGVKPDQQL VKIVHDELVK LMGGEVSELQ FAKSGPTVIL
190 200 210 220 230 240
LAGLQGVGKT TVCAKLACYL KKQGKSCMLI AGDVYRPAAI DQLVILGEQV GVPVYTAGTD
250 260 270 280 290 300
VKPADIAKQG LKEAKKNNVD VVIMDTAGRL QIDKGMMDEL KDVKKFLNPT EVLLVVDAMT
310 320 330 340 350 360
GQEAAALVTT FNVEIGITGA ILTKLDGDSR GGAALSVKEV SGKPIKLVGR GERMEDLEPF
370 380 390 400 410 420
YPDRMAGRIL GMGDVLSFVE KATEVMRQED AEDLQKKIMS AKFDFNDFLK QTRAVAKMGS
430 440 450 460 470 480
MTRVLGMIPG MGKVSPAQIR EAEKNLLVME AMIEVMTPEE RERPELLAES PERRKRIAKD
490 500 510 520 530 540
SGKTEQQVSA LVAQIFQMRV KMKNLMGVME GGSIPALSGL EDALKAEQKA PPGTARRKRK
550 560
ADSRKKFVES ASSKPGPRGF GSGN