ID V2XLZ8_MONRO Unreviewed; 501 AA.
AC V2XLZ8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative g-protein alpha subunit {ECO:0000313|EMBL:ESK94762.1};
GN ORFNames=Moror_14155 {ECO:0000313|EMBL:ESK94762.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK94762.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK94762.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94762.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the G-alpha family.
CC {ECO:0000256|ARBA:ARBA00005804}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK94762.1}.
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DR EMBL; AWSO01000121; ESK94762.1; -; Genomic_DNA.
DR RefSeq; XP_007845871.1; XM_007847680.1.
DR AlphaFoldDB; V2XLZ8; -.
DR STRING; 1381753.V2XLZ8; -.
DR KEGG; mrr:Moror_14155; -.
DR HOGENOM; CLU_014184_1_1_1; -.
DR OrthoDB; 1864818at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
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:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF302; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-8 SUBUNIT-RELATED; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 122..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 57148 MW; 33CE053DDD81B8C2 CRC64;
MFTTEDTSDP FYLLLRPPPN ETPAQTEARL KREADARRIS DAIDEELKHC KAQAKKETNV
VKVLLLGQAE SGKSTTLKNF RMRYDPASWE KERNGWRAVV QLNLVRSIIT ILGLIEAELS
GEVPENQDNE AQHGEEDDDR TTVESLPDTD NALKFTDRHQ LLMIRLAPLR SVEAHLQRVL
GAGSESVRQS TGQPLPMAAT PFDTPVRDPA AKRSLGEFSV RCWYDVVNPE GRKNATGADW
NPQADLHNAT ISIADCKDDM KALWDDKIVQ AAIARRKLRL PDSAGFFLHE LDRIASRDFS
VTDDDIVRAR LRTVGIQEYK VRFKNSPIDA PRVDGAWEWR IFDVGGCRTC RSAWLPFFEN
TNAIIFLCPV SCFDERLEED YRVNRLEDST LLWRSICSSK LLTRTQLILF MNKCDLLKKK
LKQGVMVKDY LTSYGDRTNE VMTFVKYLRE KFKEILKVNS PEPRASYIYP TTVTDTQATA
KTLESVRDGV LRENLIKSQL M
//