ID A0A1X6NFG3_9APHY Unreviewed; 1227 AA.
AC A0A1X6NFG3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=PhoX domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=POSPLADRAFT_1030261 {ECO:0000313|EMBL:OSX67093.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX67093.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX67093.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX67093.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KZ110591; OSX67093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6NFG3; -.
DR STRING; 670580.A0A1X6NFG3; -.
DR OrthoDB; 5392990at2759; -.
DR Proteomes; UP000194127; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06876; PX_MDM1p; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR013937; Sorting_nexin_C.
DR PANTHER; PTHR22775; SORTING NEXIN; 1.
DR PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..301
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 439..476
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 854..972
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 594..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 818..845
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 594..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 137314 MW; 6DD025CC96D0D18F CRC64;
MVFSTRQTFF AVTALAIVVP TAVRIVSSPL TLILLLPVLA VVSALGFLAL NIFLGYLLDV
HRLPPHNALP SAARPLAFST PAAWQAVLTR SQWSHKAPQS LPPLYRDSPV ISAALNDILI
MIVRDFVLVW YKDISSSPSF PTAVSSVLHS SMEQVLTRVM TLDISALIVK CIVPKVTAHI
EQFRQSEVAL RGAGLERRLT QSEELDLLLA SRYAGRGGEK LHRAVDNLSS TFTKQTEENH
LRGLVDRALP YILPEKEARS EAVKIVVREI VACSVLYPIM EMLADPDFWN RSIDSVAGAA
IRQQRLVSKV RNILEAQLPR PNPSVTVPRP STTETITIRT DARQFESFLR SINRCSSLLD
ARRLKNDIMG EIRRTRALLS NHEKDDWING EKTEDIVAFL DRLYTAKRKV EKRIVLLGGE
SDPRQPTTAP EAGMQSHLTL RDVLRNPSSL SYFMEFMDRR HRSLLVQFWL TVESFKNPLE
SVDSGSSDED DDAVLDPTRS ATLKEDISMM NELYFSGTTP DPVLSSISQK HVNAIRTFGL
GEETPTPVEE RRVRRSVMLT QRQIEREMEQ DFEDFQRSEL WFRVVGDLEA IARRGMDHPP
SRSDDHAISR TASEASEQSL LSMTSVPRSF SSPLFSTPTA QKPVRMELPS SNASTPNTTF
KGSLSNLEVL MSPIAESPSV SSSRAPLFDD PEDAKMTEQS RRMAAIQAAL TDIIALDKRD
EHPVGSAESI SSAKLSSSLI SEGKRNSTLD YDVEEEEDRP DDDGEHGHGS FQLAGPGDLQ
LSHEIARLTH KIETLQSQDA MLDTLIKKAE LTGDAQELRL LRKSRSSLTR ELRELRFQKT
QYEQQESANR LLSDHTKVAI VNSTVGEEDG KSVVRYLIEV QQLAQDGTFS SGWVVARRYN
EFFNMHNKLR ERYALVRNLD FPGKRLVTAL SSSFVDQRRV ALEKYLQNLI ANPAVCESEE
LRGFLSRESP FIANESIAST SKTAPPARGK GIVRSMYQSV TESIDDMFFG PSMLDVIIQR
LTTQAAEFAG IVGSGVHDED LVAQALKASG KSTPDDALFQ LSGDLRPLQG ETSTSTFSSP
ICDLVLAVFE LDKKNNWLRR QAIVIILQQV FGDTIERKIR ETFAMYVDEL HLVNYINIFR
DGLWPGGQLK PPSVPRTAEE KLRTRDEANR KLSALMPDLV ANMIGRSNAR RGARRIFAVL
QNRRLNQHLL YTIVDEIFAA LFPDSPS
//