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Database: UniProt
Entry: A0A059JAL5_TRIIM
LinkDB: A0A059JAL5_TRIIM
Original site: A0A059JAL5_TRIIM 
ID   A0A059JAL5_TRIIM        Unreviewed;       976 AA.
AC   A0A059JAL5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=PXA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H109_03467 {ECO:0000313|EMBL:KDB24683.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB24683.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB24683.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB24683.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KDB24683.1}.
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DR   EMBL; AOKY01000245; KDB24683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059JAL5; -.
DR   STRING; 1215338.A0A059JAL5; -.
DR   HOGENOM; CLU_007315_0_0_1; -.
DR   OMA; INGWIIH; -.
DR   Proteomes; UP000024533; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775:SF47; MEIOTICALLY UP-REGULATED GENE 122 PROTEIN; 1.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   SMART; SM00313; PXA; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024533};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        68..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          147..329
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   DOMAIN          487..603
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..678
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  105212 MW;  5387F65CB1EC1201 CRC64;
     MATKEDDTAV TASNESLAQP KSATVPPSST SQSLVDQVSL FVAHADGTTL ISISAGVVAV
     SYVLFGRLAL LLVGAIGGVI LHIWWEGQDN GTNGDNEETA KRKRHELSLE VANRLTALYA
     DNGSKQEDDE DPLNRSGEPS LDYSRMGPAT EAALTALTNS VIADYVSWWY KPILPSEDEF
     PEACRNTLVS MVLAVSSRIS RKRPADMFLQ FATNSTSFMI VFFSELSAAV GTATTGSRPV
     ADSIDEYLDK NPESSLANVL SSTQQEKKLG LVGTDILKTF LEPSVYNCGP LRIFLREVLS
     RLILQPTIDM CSDAEYINTW IVYLLEQGEP QLLNAIDAGL EQADDVKQKN PTSTGTPTTN
     VLEGKASNIV TNLGDQKLAE QMQPMRQPVD ANFAQHKDIS AVGMPKELPI SADSEETGGN
     SAVYTHLPTD SSSSNTTDHQ PTPGSSTSLN EDSLDNPPID SQTTPILNTS ATSLITMQTS
     QFHGSSVAII EDFNEDDKSN IRSKPTSEYL IQIEPSNSKL TGWMIARKYS DFEILHETLR
     RISVVSGISD FSLQHNELPG WKGRNRNGLR ISLEKYLQAA LQYEQLAECE GMKKFLEKGR
     QSGLEPESAS SKSGFPFAAP VAVFENVGKG VMGVLGTAPK GVANSKKVIV GGVSGIFGAS
     GNDNRKRASS NAASRPTAVR GTSMDILPSP MTNVTAHSKN LSMSNLQDRP RTTFQRQPTH
     LENESGDIGF GLPTSVTHAD SSLASSCEDL ADEGNVTPLS SSDTPDTVHV ALPSEANVES
     NKELATRDIP ESASSGDVEP SPKKSSEGRS YAPVSEEEAV VVVELLFAVI NEVYSLSSAW
     NIRKRLLNAS KSFLLRPGNP SLEAIRTLLQ DSIIDGNTSD EALAGYITKL RKSSLPTEED
     MKAYPPPLSP EQKEQLRIKA RTLLISRGMP PALMGIMGAN ATGEALGKIF DCLQIPSVGR
     AFVFAILLQA IRVMTQ
//
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