GPAA_ASPFC
ID GPAA_ASPFC Reviewed; 353 AA.
AC B0XRA0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=G-protein complex alpha subunit gpaA {ECO:0000303|PubMed:30914505};
DE AltName: Full=Guanine nucleotide-binding protein subunit alpha {ECO:0000305};
GN Name=gpaA {ECO:0000303|PubMed:30914505}; ORFNames=AFUB_012620;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GPRM.
RX PubMed=30914505; DOI=10.1128/mbio.00215-19;
RA Manfiolli A.O., Siqueira F.S., Dos Reis T.F., Van Dijck P., Schrevens S.,
RA Hoefgen S., Foege M., Strassburger M., de Assis L.J., Heinekamp T.,
RA Rocha M.C., Janevska S., Brakhage A.A., Malavazi I., Goldman G.H.,
RA Valiante V.;
RT "Mitogen-activated protein kinase cross-talk interaction modulates the
RT production of melanins in Aspergillus fumigatus.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: G-protein complex alpha subunit that plays a role in
CC conidiation and regulation of the biosynthesis of secondary metabolites
CC such as dihydroxynaphthalene (DHN)-melanin, via interaction with the G
CC protein-coupled receptor gprM. {ECO:0000269|PubMed:30914505}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site (Probable).
CC Interacts with gprM (PubMed:30914505). {ECO:0000269|PubMed:30914505,
CC ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Leads to a strong increase of
CC dihydroxynaphthalene (DHN)-melanin production.
CC {ECO:0000269|PubMed:30914505}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; DS499594; EDP56551.1; -; Genomic_DNA.
DR SMR; B0XRA0; -.
DR EnsemblFungi; EDP56551; EDP56551; AFUB_012620.
DR VEuPathDB; FungiDB:AFUB_012620; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR PhylomeDB; B0XRA0; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002975; Fungi_Gprotein_alpha.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01241; GPROTEINAFNG.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Metal-binding; Nucleotide-binding; Transducer.
FT CHAIN 1..353
FT /note="G-protein complex alpha subunit gpaA"
FT /id="PRO_0000454888"
FT DOMAIN 32..353
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 173..181
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 196..205
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 323..328
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
SQ SEQUENCE 353 AA; 40769 MW; BCCA778E357C257D CRC64;
MGCGMSTEDK EGKARNEEIE NQLKRDKMMQ RNEIKMLLLG AGESGKSTIL KQMKLIHEGG
YSRDERESFK EIIYSNTVQS MRVILEAMES LELPLEDARN EYHVQTIFMQ PAQIEGDSLP
PEVGNAIGAL WRDTGVQECF KRSREYQLND SAKYYFDAID RIAQPDYLPT DQDVLRSRVK
TTGITETTFI IGDLTYRMFD VGGQRSERKK WIHCFENVTT ILFLVAISEY DQLLFEDETV
NRMQEALTLF DSICNSRWFV KTSIILFLNK IDRFKEKLPV SPMKNYFPDY EGGADYAAAC
DYILNRFVSL NQAEQKQIYT HFTCATDTTQ IRFVMAAVND IIIQENLRLC GLI
