GPA1_SPOS1
ID GPA1_SPOS1 Reviewed; 353 AA.
AC O74259; U7PQT7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 4.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha;
GN Name=SSG-1; ORFNames=HMPREF1624_06103;
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=ATCC 58251 / de Perez 2211183;
RX PubMed=10817227; DOI=10.1080/mmy.38.2.109.121;
RA Delgado N., Rodriguez-del Valle N.;
RT "Presence of a pertussis toxin-sensitive G protein alpha subunit in
RT Sporothrix schenckii.";
RL Med. Mycol. 38:109-121(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183;
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF085339; AAC34129.1; -; mRNA.
DR EMBL; AF068248; AAC67526.1; -; Genomic_DNA.
DR EMBL; KI440847; ERS97932.1; -; Genomic_DNA.
DR AlphaFoldDB; O74259; -.
DR SMR; O74259; -.
DR STRING; 1391915.O74259; -.
DR PRIDE; O74259; -.
DR EnsemblFungi; ERS97932; ERS97932; HMPREF1624_06103.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000018087; 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 2: Evidence at transcript level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..353
FT /note="Guanine nucleotide-binding protein subunit alpha"
FT /id="PRO_0000203610"
FT DOMAIN 32..353
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..26
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..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 175..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 134..135
FT /note="RG -> AV (in Ref. 1; AAC34129/AAC67526)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="T -> K (in Ref. 1; AAC34129/AAC67526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 41132 MW; 83BF528AA752F60E CRC64;
MGCGMSVEEK EGKARNEEIE NQLKRDRMQQ RNEIKMLLLG AGESGKSTIL KQMKLIHEGG
YSRDERESFK EIIYSNTVQS MRVILEAMES LELPLEDQRM EYHVQTIFMQ PAQIEGEVLP
PEVGNAIEAL WKDRGVQECF KRSREYQLND SARYYFDNIA RIAAPDYMPD DQDVLRSRVK
TTGITETTFI IGDLTYRMFD VGGQRSERKK WIHCFENVTT ILFLVAISEY DQLLFEDETV
NRMQEALTLF DSICNSRWFI KTSIILFLNK IDRFKEKLPI SPMKNYFPDY EGGDDYAAAC
DYILNRFVNL NQHESKQIYT HFTCATDTTQ IRFVMAAVND IIIQENLRLC GLI
