ID A0A194VTK1_9PEZI Unreviewed; 573 AA.
AC A0A194VTK1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Frizzled/smoothened-like sans CRD protein B {ECO:0000313|EMBL:KUI67258.1};
GN ORFNames=VM1G_02695 {ECO:0000313|EMBL:KUI67258.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI67258.1};
RN [1] {ECO:0000313|EMBL:KUI67258.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI67258.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM003100; KUI67258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VTK1; -.
DR OrthoDB; 1360712at2759; -.
DR Proteomes; UP000078559; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR PANTHER; PTHR42058:SF1; -; 1.
DR PANTHER; PTHR42058; G_PROTEIN_RECEP_F2_4 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..218
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 435..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 63021 MW; E2B860E098BDB775 CRC64;
MTTNITAFEC PAPFLNELQF GNGGYVEGRL CMSVGEISCC LPCPLTAWAY PDSFDTMGIA
ADWVAVASTV CCVFLLLSWL VLPIDKTHRH YLSICLTFAV VFMNLGFVIP LAGNPEQCYD
SITPNDMQTS SVCAASGTFI VIGGWAGVLW IFLRSLSLHL QICWQVVVGR NFMWFSHAVG
WGLPALGIIL ALTLSGVSFR FGATCHINHE NSLADLWIPL LVFAGLTIII QFATFGYCIK
VYLASLADNN ATTENSAGLP SYTNSIRTMT PRQAYRRVRR VIQLQWRGIA IVLIIIADVV
FFAVVFVFQD NTIEEVKNDP QIAEPWIDCL LAAGGDKNKC LNQTNSLVVS MATIGAVLVL
LAMNGIWLLV LLGRWSMVTG WVELFTHRPS QAKREFVSVD ARLDDMKMNT DPRSYEMLSR
DSGKNVMMDG MVTPDTVREG PIYPPIGSYL ASTTSPPNES PTPSGRRTPD YFGPQARYQA
PVRSFSSPRP PTREGRGSQA GWEATATYSN VGREFSRSPP PTGQYSQSPP PTGQYSQSPP
PTGQYSQSPP PSGHYHQDSY GQQDMNPLGM NRI
//