ID A0A423W4P1_9PEZI Unreviewed; 745 AA.
AC A0A423W4P1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Fungal N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_07188 {ECO:0000313|EMBL:ROV98320.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV98320.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV98320.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV98320.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROV98320.1}.
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DR EMBL; LKEA01000026; ROV98320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423W4P1; -.
DR STRING; 356882.A0A423W4P1; -.
DR Proteomes; UP000283895; 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; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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:UP000283895};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 83902 MW; C4061394D0E1E461 CRC64;
MDPISAVGFV SSVVSIVELV RNGIATLSEL RDRYKIVDFK VNILITQLST LTTALDQVTN
VLSDNPGLPQ DAQLIRDLTT SLACVEAVIM LINERISPLQ QQLANGLSAM GKVNFLWDES
TLKDYLSLLD NQVNALNLLL TALQCRTTLE QKNMLEMSES RQVFSRVRDE TSSLLFLRDA
ESTGTRRSIG SQNWATVNTT FSFDHEIFTS KVYRMATRSS MMQALILEEH RHTSTENVTT
ESLGSTTRPT SVCDSVIDGA LRAPPRLREQ GFLPSYSDIT VTQEVHRFSS AIGTQTAQGP
GHGVIETEVT SASYAQRNET STQDQLVPAG PAPAIIMGSE PENSAPHLQS LLEPSRKSID
SDVWSLNTTG SQTYAERPRP VPTRTQSHIG PALPTIPQGR QADSIVSKHK VLVLGSEESG
KSTLIKSLNI LHSEYDENWL NENVQIRGPE ADRDWALARK TRALQAQLDL LRRELCNDFT
ISVVLVFWDD INLQHKLNQL RLNPCKRGER RHDYTCLNHS RHFMDSTRRI MQPDYVPSVQ
DILWSYNPSL GIHKSHYIID GIPYQFVDVG GARTEQGKWI KAFYDVQTVV FTFDVSCYDW
PSLDDGVKNR MVDSFDLWDR LVNANSFTKT NFVVMLTKED RLTRAKLTRS PFTTIFPDML
GDSQDPDNVL RHIVRHLQSI IQKKPDFDRS VLFCSARSIA QSTTDLAEIT LDAIKHAANQ
QQAFVKATHE PVLPGRFPRL KWRLY
//
