ID A0A162JYV7_9HYPO Unreviewed; 1208 AA.
AC A0A162JYV7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phox-associated domain protein {ECO:0000313|EMBL:OAA50968.1};
GN ORFNames=BBO_00915 {ECO:0000313|EMBL:OAA50968.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA50968.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA50968.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA50968.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:OAA50968.1}.
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DR EMBL; AZHA01000002; OAA50968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162JYV7; -.
DR OrthoDB; 5392990at2759; -.
DR Proteomes; UP000076863; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..287
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 417..556
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 871..989
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 564..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 135421 MW; 633BC2B4E4082C83 CRC64;
MALKRRDVII ASIVAFIAWG YVVSWFGALR WAGYAFGGGL LVGLFALLGA LILFARNPDD
RRPRPRAALF LAPQRWRDEV AALRKRQAYE RPSLDLPSQR VAMAVDNLLD LVLRDFVRVW
YTNISPNSEF PDEVDRAIRL AIISLLDCLR DKDIVELSIS RVVPILTAHF RDFYEAERSI
RGKKLNKSVT ESDELDLAIA AKYNKGKLHP AASLSFPDMK IVQQDYLRGL IARVLPKVMP
RHMLSSRAVS IIVKEIVSCA VLSPVMQLLS EPDTWNQIME NMGRSMLQDR STVRKLRAAL
DQHASPAPRV VKTTATPRIS SGDSERKFEK FIRAIRKVSN LSDARRFRNE VASQLKRDSL
EENPDQVYLR RLEMGKRLLD QRVAHLAAGG DRSGHTSAPT AQRMIKSTST SRLENAGLVE
LLRDSSGLSY FMEFMDRQKM MTLVQFWLVV DGIRNPLEDD GPDNEALPSN LPMWTNSDWL
DVRQIQQAYM SKSELNVPEP SQTNVKEFLQ AGKAATPAQY FRARRSILQV QSMALETMKN
QYFQAFKKSD LYYKCLASQE TSSITQSAPM ALSASEMGTP HQVNGRSNGR TSKPKSLARL
NLIARRVGSS TDLASNGGES DAMDPLAATR RSLDEDASNP IYYDDEIEHD NMADSNPNLE
QDDSQQHKPD TQAVQAVEKA LNNIMENERP QTAADLRASL FTTDETIGGS SSGGLFGDDE
DSSRGSIDVG RPTAGGGEKP SLSSLGLVSA ASRIGVFVDD DLFADEDKHL SDERDDVNDD
DIDDEDEVHA AAPGDLGLAE AITVLTNDID RLIAQEAILD SLTRKAELTN NTAELRILSK
SKASLDREVR RKELQRQQYV VQESDNSLYG RSTVNIKSIQ VGREDDGREF ALYVIEVQRD
AGEQMPAASW VVARRYSEFH DLHQKLRSRY PSVRHLDFPG RRVVMKFQSE FLRKRRVALE
KFLQELLLLP DVCRSRELRA FLSESAITQG ENLLDREDRK DIVSRLYDSV TDGMEDILGN
IPVLDQISVA GQNLITAATN QLNSGPLHAD QESFPAAEAE AELNAFESKE LEPFIKPICD
IFLEVFELNR GNNWLRGRAV VVVLQQLLGG TIERKVRDTF KMLAQEEPLL RYIGLVRDNM
WPQGQLARDK KPRSAAEKRK TRTEASLMLA TLVPDLAGSV VGRVNAQAAS RRLFATFNNS
RLKQVHGH
//
