ID A0A166IL98_9AGAM Unreviewed; 1245 AA.
AC A0A166IL98;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=PhoX domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SISSUDRAFT_1013638 {ECO:0000313|EMBL:KZT43860.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT43860.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT43860.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT43860.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KV428006; KZT43860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166IL98; -.
DR STRING; 1314776.A0A166IL98; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..301
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 437..519
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 865..983
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 320..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 138635 MW; 980CE9C055630FFC CRC64;
MNAALYARSA FAIGLIAIVY PFLARIWRSP LALIFILPPF LGLCLVILVF SNILIGLLLD
KYPETTREPK THAARPLAFS TPAAWQAATT RSRWELRSPH LLKPLLPELP GTSGALNDLM
ILIVRDFVLT WYTDISSSTT FPTAISYTLH GTLNNLLNRV AGLDIPDLIV YRILPKITAH
VEQFRQSETA LRGAGLERHL TQSDELDILL AGRYAANGGK LHPAISNLST MSTRQSEEAH
LRSLLAKALP LLMPPSEASS PAVLNATREI LACTVSAPAI DVLADPDFWN RLIDDMAGAA
IRQQKMISRV RHVLEVETAS PRAAGRTNHG ASRSESITSK TDPKNFESFL RSIRRMVSLL
DARRLRNDIL QEIRRIRSLL ANHENDEQIK GERTEEVVAF LDRLYTAKKE IENRISILGG
VDVSRSTQDT EPAAKPTLRD ILMNPSSLSY YMEYMDRQRK ALLVQFWLTV ESFKNPLEYV
DSSGSEDEED TKDIHDATSV ETVKEDLEML YNTYFSQDTI PVALQVISPK YVAAIRNFVL
EPSESTPAKA RKARHSMFMA QRQAERDMEQ YFGGFEQSGL WFRAIDDIPG FSQSASSKAT
KIPHREPSLA TPVASPPARQ GYSGPTISLG PGALPRRSDS ISPSAGRSHH NSKVRDSSSS
STSSIVRQSQ DPSHLEILAS PPGRSPLFSD DLSESITQES DLLSKSTQMA AIQRALSDIL
AEENLFETSQ SDANSRSDGR QSITSSLPQT QSQPFRDGAP EDDELDTQPP EHELSQSSME
TFHPAGPGDL LLSVDIAYLD SKIQDLQSQD SMMDALIRKA ELTGDEQELR LLSRSKIAMA
KELRELTFQK AQYEQQELDN RLLPGRTSIK IATSTTEEVD GKPVVRYLIE VNQLGADGTH
SSGWVLARRY NEFLAMHQRL REKYLVVRLL DFPGKRLVTS MSSSFLESRR VGLEKYIQNL
IALPLICETE ELQSFLSRDS PLHAAHHSRS QGSKPLSSGQ ALMRSMYKTV THSLDDMLFG
PSMLDVVIQR LTRQAADFAG IVGSGVHDED LVAQAFRATG PSAPEERLLR LTGDLTSLEG
ETSGSSFSAP ICDLILAIFE LNRKNNWLRR QAVVIILQQV LGGTIERKFR DTFKTFASDS
SLVSLLNTFR DALWPGGQFK TNNTPRTPEE RMTTRQSANR KLSALIPDLA ANMIGRSNAR
YGARRIFAVL QNRRLNQHII YTIIDEVFSA LFPETTMDTH EVTIS
//
