O42816

PR
Gene name
SRP54
Protein name
Signal recognition particle 54 kDa protein homolog
Names
Species
Candida albicans (Yeast)
KEGG Pathway
EC number
3.6.5.4: Acting on GTP; involved in cellular and subcellular movement
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

421-545 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O42816

Entry ID Method Resolution Chain Position Source
AF-O42816-F1 Predicted AlphaFoldDB

No variants for O42816

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O42816

No associated diseases with O42816

4 regional properties for O42816

Type Name Position InterPro Accession
domain Signal recognition particle, SRP54 subunit, GTPase domain 118 - 313 IPR000897
domain AAA+ ATPase domain 117 - 327 IPR003593
domain Signal recognition particle, SRP54 subunit, M-domain 346 - 447 IPR004125
domain Signal recognition particle SRP54, helical bundle 2 - 87 IPR013822

Functions

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

1 GO annotations of cellular component

Name Definition
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.

3 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.

1 GO annotations of biological process

Name Definition
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVLADLGSRL RGALSSVESG SDDEIQQMIK DICSALLESD VNVKLVAKLR GNIKNKIDES
70 80 90 100 110 120
NVSKETSAMN KRKKLQKIIF DELCALVDSN VEPPKPKKLS TSTKTINGKK VRLSKESSHV
130 140 150 160 170 180
IMFVGLQGAG KTTSCTKLAV YYKKRGFKVG LVCADTFRAG AFDQLKQNAI KANIPYYGSY
190 200 210 220 230 240
LEPDPVKIAF EGVQKFKQEK FDIIIVDTSG RHRQEEQLFT EMVQIGEAVQ PTQTIMVMDG
250 260 270 280 290 300
SIGQAAESQA RAFKESSNFG SIILTKMDGH AKGGGAISAV AATKTPIVFI GTGEHVGDLE
310 320 330 340 350 360
IFKPTTFISK LLGIGDIQGL IEHVQSLNLH QDEGHKQTIE HIKEGKFTLR DFQNQMNNFL
370 380 390 400 410 420
KMGPLTNIAS MIPGLSNIMS QVGDEETSKK IKNMIYIMDS MTTKELECDG RIFIKEPSRI
430 440 450 460 470 480
VRVARGSGCA VVEVEMILQQ HRMMSTMAKS AMAAQGGQPG QPGNPMANNP QMQRMMQQAQ
490 500 510 520 530 540
SNPNFMQQAM NMLGGAGGGA GGAGGLAGMM NNPAMMQQAQ QMMRSNPQMM QQAQQMMKNP
550
GMMQKMMQQF GGMGGM