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Guanine nucleotide-binding protein subunit alpha

 GPA1_EMENI              Reviewed;         353 AA.
Q00743; C8VS02; Q5BFM9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 125.
RecName: Full=Guanine nucleotide-binding protein subunit alpha;
Name=fadA; ORFNames=AN0651;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-42 AND
GLY-203.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=8895563;
Yu J.H., Wieser J., Adams T.H.;
"The Aspergillus FlbA RGS domain protein antagonizes G protein
signaling to block proliferation and allow development.";
EMBO J. 15:5184-5190(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
involved as modulators or transducers in various transmembrane
signaling systems.
-!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
gamma. The alpha chain contains the guanine nucleotide binding
site.
-!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
{ECO:0000305}.
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EMBL; U49917; AAC49476.1; -; Genomic_DNA.
EMBL; AACD01000010; EAA65427.1; -; Genomic_DNA.
EMBL; BN001308; CBF89057.1; -; Genomic_DNA.
PIR; S71965; S71965.
RefSeq; XP_658255.1; XM_653163.1.
ProteinModelPortal; Q00743; -.
SMR; Q00743; -.
STRING; 162425.CADANIAP00002024; -.
EnsemblFungi; CBF89057; CBF89057; ANIA_00651.
EnsemblFungi; EAA65427; EAA65427; AN0651.2.
GeneID; 2876430; -.
KEGG; ani:AN0651.2; -.
HOGENOM; HOG000038730; -.
InParanoid; Q00743; -.
KO; K04630; -.
OMA; VARMEDT; -.
OrthoDB; EOG092C25Q3; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:AspGD.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IMP:AspGD.
GO; GO:0019001; F:guanyl nucleotide binding; IMP:AspGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0035690; P:cellular response to drug; IMP:AspGD.
GO; GO:0048315; P:conidium formation; IMP:AspGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:AspGD.
GO; GO:0042318; P:penicillin biosynthetic process; IMP:AspGD.
GO; GO:1900198; P:positive regulation of penicillin biosynthetic process; IMP:AspGD.
GO; GO:0075306; P:regulation of conidium formation; IMP:AspGD.
GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
GO; GO:0010913; P:regulation of sterigmatocystin biosynthetic process; IMP:AspGD.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
GO; GO:0007165; P:signal transduction; IMP:AspGD.
GO; GO:0000909; P:sporocarp development involved in sexual reproduction; IMP:AspGD.
GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 1.
InterPro; IPR002975; Fungi_Gprotein_alpha.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
PRINTS; PR01241; GPROTEINAFNG.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Complete proteome; GTP-binding; Lipoprotein; Magnesium; Metal-binding;
Myristate; Nucleotide-binding; Palmitate; Reference proteome;
Transducer.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 353 Guanine nucleotide-binding protein
subunit alpha.
/FTId=PRO_0000203601.
NP_BIND 40 47 GTP. {ECO:0000250}.
NP_BIND 175 181 GTP. {ECO:0000250}.
NP_BIND 200 204 GTP. {ECO:0000250}.
NP_BIND 269 272 GTP. {ECO:0000250}.
METAL 47 47 Magnesium. {ECO:0000250}.
METAL 181 181 Magnesium. {ECO:0000250}.
BINDING 325 325 GTP; via amide nitrogen. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
MUTAGEN 42 42 G->R: Loss of intrinsic GTPase activity
leading to constitutive signaling.
{ECO:0000269|PubMed:8895563}.
MUTAGEN 203 203 G->R: Reduced growth without impairing
sporulation.
{ECO:0000269|PubMed:8895563}.
SEQUENCE 353 AA; 40721 MW; 5AEBA1BC84C77A09 CRC64;
MGCGMSTEDK EGKARNEEIE NQLKRDKMMQ RNEIKMLLLG AGESGKSTIL KQMKLIHEGG
YSRDERESFK EIIYSNTVQS MRVILEAMES LELPLEDARN EYHVQTVFMQ PAQIEGDSLP
SEVGNAIAAL WQDAGVQECF KRSREYQLND SAKYYFDSIE RIAQSDYLPT DQDVLRSRVK
TTGITETTFI IGDLTYRMFD VGGQRSERKK WIHCFENVTT ILFLVAISEY DQLLFEDETV
NRMQEALTLF DSICNSRWFV KTSIILFLNK IDRFKEKLPV SPMKNYFPDY EGGADYAAAC
DYILNRFVSL NQAEQKQIYT HFTCATDTTQ IRFVMAAVND IIIQENLRLC GLI


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