ID A0A316YR40_9BASI Unreviewed; 1168 AA.
AC A0A316YR40;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=PX-domain-containing protein {ECO:0000313|EMBL:PWN91759.1};
GN ORFNames=FA10DRAFT_265600 {ECO:0000313|EMBL:PWN91759.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN91759.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN91759.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN91759.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819635; PWN91759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YR40; -.
DR STRING; 215250.A0A316YR40; -.
DR InParanoid; A0A316YR40; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000245768; Unassembled WGS sequence.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF1; SORTING NEXIN; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 617..762
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 31..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 126262 MW; 69B809B508A957FE CRC64;
MRPAPPPKPS HLSVAITGTL SSDALRTYIR KQSTQTINSG KAPTPSTIRR LMDARDRDQD
DDTNGYEDDD DDDDDDDDEN VRWGTAKAAI TPIKPAYANL ADLFSPAHGE QQRQQHQTRA
AMASTSSQAT LKATNSSSIG GTGSFRTARG GSENGNGQRF SALGEEEMEA GILIEDCDVS
TFRLSKPRSR AVLPASSVFD IERSREPSVV SNAAFFHDDK SNPVAGGQLM HARDGSRFER
AGPSTKSPVA AQNSELPEPA ANTVPSRQKN LLVAGPPPPR PSSMVFAPSQ DEGSADDQAK
DAPTPEICEP PAAGLNAGSS QVTQGGRSAR ALYAFAGEAH FNELGLRAGQ VFEILNEDIG
GGWSLAALQE DAGHWTKGLV PKGWYAYIQD FTLSPPTVEA RKSSEPSPMS LDLEGPKTPQ
GNSHVGSSLH TMSPSTSSQE PAHSRNDSYL SPVQDWDRGR PASGIGEMSG SRLGAIQALN
MVKSRSEGSQ VRTRETQETI SPANSTSSLP VSESGDTLAS HASSMAEGAA PLVTPATTPG
SPAPMMHREG SKKKATLLGG RSMNRFSPFV ATGVEDYILF GSKAKIEQAD GETARQKQFD
IVTSPQGGPT WKSPGFGIYV EIHTPEVQVD ERGREYIAFV VHASYTFFSE REQQDDIGLS
EDPMADPTQR PASPTYMSSV YRRYNHFKWL SSHLSRVYPF FVLSLPPLPS ANHVAGKAQR
FEASFVEKRR RELQAWLVSV VRHPILRTDE AVRFFLETEH DGEEWAQGAK QINQRAAAAF
TTDVFSKTLH PLFGVDSTEA AIEARQVAAF LSTYEKAMGA DGTAPRGGVL GSWRDMREGG
RISSDNYRNL SYALLRMMTG TALGAGTRPA ASNGSALGSG VFPPMGNVGR RDEHGATNEQ
RAWCWRDGCG ECKSLTKALQ GTVDALQQVA DLYDGHAHGV LHDEHDRLWN LSKAQSQHAS
LLEIHKATLA KYREATGEPD PLAEAEGSQT LSSETASTDE QMATRCETVL NMTMSEVDRV
HRQRVEDWNG VGRSMLDGQI ALYEDVLHTL REARTRFEEE TKKTSASEAT TTGEERVPIL
PSPFEMELGN PVQSAPLNLP SAMLMQPSKA VRPVSLAGEV LSDLFGGASA FRGPPTKTSS
SLGQIDESGS GHSQQHESGS SMYFTIWR
//
