Q9HFW7

PR
Gene name
gna-3 (NCU05206)
Protein name
Guanine nucleotide-binding protein alpha-3 subunit
Names
GP3-alpha
Species
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
KEGG Pathway
ncr:NCU05206
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-59 (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 Q9HFW7

Entry ID Method Resolution Chain Position Source
AF-Q9HFW7-F1 Predicted AlphaFoldDB

No variants for Q9HFW7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9HFW7

No associated diseases with Q9HFW7

3 regional properties for Q9HFW7

Type Name Position InterPro Accession
domain Guanylate kinase-like domain 12 - 191 IPR008144
domain Guanylate kinase/L-type calcium channel beta subunit 11 - 194 IPR008145
conserved_site Guanylate kinase, conserved site 46 - 63 IPR020590

Functions

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

1 GO annotations of cellular component

Name Definition
heterotrimeric G-protein complex Any of a family of heterotrimeric GTP-binding and hydrolyzing proteins; they belong to a superfamily of GTPases that includes monomeric proteins such as EF-Tu and RAS. Heterotrimeric G-proteins consist of three subunits; the alpha subunit contains the guanine nucleotide binding site and possesses GTPase activity; the beta and gamma subunits are tightly associated and function as a beta-gamma heterodimer; extrinsic plasma membrane proteins (cytoplasmic face) that function as a complex to transduce signals from G protein-coupled receptors to an effector protein.

5 GO annotations of molecular function

Name Definition
G protein-coupled receptor binding Binding to a G protein-coupled receptor.
G-protein beta/gamma-subunit complex binding Binding to a complex of G-protein beta/gamma subunits.
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
metal ion binding Binding to a metal ion.

4 GO annotations of biological process

Name Definition
adenylate cyclase-activating G protein-coupled receptor signaling pathway A G protein-coupled receptor signaling pathway in which the signal is transmitted via the activation of adenylyl cyclase activity and a subsequent increase in the intracellular concentration of cyclic AMP (cAMP).
adenylate cyclase-modulating G protein-coupled receptor signaling pathway A G protein-coupled receptor signaling pathway in which the signal is transmitted via the activation or inhibition of adenylyl cyclase activity and a subsequent change in the intracellular concentration of cyclic AMP (cAMP).
conidium formation The process of producing non-motile spores, called conidia, via mitotic asexual reproduction in higher fungi. Conidia are haploid cells genetically identical to their haploid parent. They are produced by conversion of hyphal elements, or are borne on sporogenous cells on or within specialized structures termed conidiophores, and participate in dispersal of the fungus.
sporulation resulting in formation of a cellular spore The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGACMSKNDE ETEQKKRSQK IDRDLEEDSK KLRKECKILL LGSGESGKST IVKQMKIIHL
70 80 90 100 110 120
KGYSDEELTN YRPTVYKNLL ECAKAVVNAM HQFDIQPADP SLRPYVEFLQ DYNMEGCPPG
130 140 150 160 170 180
QSIDPKVGTA IQALWNDPAK EQLMERQTEF YLMDSAEYFF TEVMRIVAED YRPNEMDVLR
190 200 210 220 230 240
ARTKTTGIYE TRFKMGQLSI HMFDVGGQRS ERKKWIHCFE NVTSIIFCVA LSEYDQVLLE
250 260 270 280 290 300
ESSQNRMMES LLLFDSVVNS RWFMRTSIIL FLNKVDIFKQ KLGRSPLGNY FPDYSGGNDV
310 320 330 340 350
NKAAKYLLWR FNQVNRAHLN LYPHLTQATD TSNIRLVFAA VKETILNNAL KDSGIL