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Database: UniProt
Entry: U7PV06_SPOS1
LinkDB: U7PV06_SPOS1
Original site: U7PV06_SPOS1 
ID   U7PV06_SPOS1            Unreviewed;      1243 AA.
AC   U7PV06;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=PXA domain-containing protein {ECO:0000259|PROSITE:PS51207};
GN   ORFNames=HMPREF1624_04658 {ECO:0000313|EMBL:ERS99458.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS99458.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
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DR   EMBL; KI440845; ERS99458.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PV06; -.
DR   STRING; 1391915.U7PV06; -.
DR   eggNOG; ENOG502RM76; Eukaryota.
DR   HOGENOM; CLU_007315_0_0_1; -.
DR   OrthoDB; 2727031at2759; -.
DR   Proteomes; UP000018087; 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; 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; PF02194; PXA; 1.
DR   SMART; SM00313; PXA; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS51207; PXA; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        111..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..395
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..654
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1030..1058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1243 AA;  132412 MW;  1FE997EE90A1E6A2 CRC64;
     MDDRKISVND PDRDLSLDSA SPTFAASSSP SGLSPVSSPP LPQRPNLASQ SLSAPPSPLP
     NSPQSPSPNT KPGSTASDDD IPTRIFRFLS TATVESLSAV GVGLAATTYF VLGRVGLVLI
     GAFGGIALFV AWEARNPDVT RAIRGEASSD LLARVIEYRR KDQENGDEVS GESVGAEAAF
     DPAQEDLALG RAFENFRPET RQALNGLVEA VVRDYVKWWY QPIVPSDQSF PLSCRRVLTS
     FLVSVSNHLS RKRPADAFLD FLTNSTSIVI VLFSELATAF AEHAAQTPQQ QGSAPPQGPD
     ANPTISAADA IYSYLASNPN SNLANLLSQR QQASKFRMVA DDLLSFLDRQ CYDCDPARTF
     LREIAATSVL ETTLQTCSKP EWINGWIVHL LEGGEPDFSQ AIDVGMQTRT DAAATASSSK
     DATSNSATAH MHHASIDIDG NVGNIALPKS RRSSFEADKA HQSRRKESVP LSHKKQLSRA
     DEEMEEAMEE MKRMNEMIAA EEKARRTTTE TKSATEAEDR LADAMQHNAD ELGIQANDER
     KDHHGHGPPS PSAASDQISP KASLSLSGDE STTRTARTVS TPITPRSSTQ GSPSQSSFAK
     SEAASGTAAN GSENTENPHP STADEASQFT SFDQLVPPAR EEDESSDSEG RKKQEQAPPP
     LTLHNANVTI HDEPVTDKGR IKSRPAWDFL IQIEPANAHY PGWMIVRKYA DFEKLHEVLR
     RIATISGATA FTEQHGVLPN WKIHTRGSLR GELERYVRDA CWYQPLAESE GMKRFLEKDT
     NNMPAASKTG LNAFETMGKN MLDALSNAPK GVAEGGKVMV GGVTGVFGNL GNLGTNIGLG
     GSSGQKKQHA SSGSLANVAG SPSPGGATTS PPASVLQDVT AYTNRLSVST PPRMDSGFSG
     AGSRRSRDSM DSQRSSVVAS QTGRVVPMGR RMSYQSQSGL MDAGANGEVG EAGADGRGRT
     NNNNSNNMWG DYAPVSSGSR GSQHNSRASS SGGYPRSPSS TSLSGTRLPM GATSAFATDA
     LEDMPGSSLT SPVRVGSSNN LTSLPAGGAG SGSGATTPHG TRPLHRVATS GTTIAKQFAA
     LTEGETRVAV ELLFAVINEL YTLSSAWNIR RTLLTAAKSF LLRPGNPSLA SIQSLLQSSV
     LDANTTDAGM AGYLNTLREN TMPTDAERAA WPAEMTAEEK ERLRVKARRL LIRSGVPAAL
     MGVMGQSATS DALGRIFDCL QVEEVARGLI FGLMLQAARI VTH
//
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