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Database: UniProt
Entry: A0A1X6NFG3_9APHY
LinkDB: A0A1X6NFG3_9APHY
Original site: A0A1X6NFG3_9APHY 
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
//
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