ID A0A1V6NZM8_PENDC Unreviewed; 996 AA.
AC A0A1V6NZM8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=PXA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENDEC_c026G06881 {ECO:0000313|EMBL:OQD70175.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD70175.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD70175.1}.
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DR EMBL; MDYL01000026; OQD70175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6NZM8; -.
DR STRING; 69771.A0A1V6NZM8; -.
DR OMA; INGWIIH; -.
DR OrthoDB; 2727031at2759; -.
DR Proteomes; UP000191522; 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; SM00312; PX; 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:UP000191522};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..344
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 500..616
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 109196 MW; 929C7D9A133F1CA1 CRC64;
MDPSSDDVIA SESTKTAPDL TNPPDQMRSD SLPEQHVSTA GLLQEAMDFA LNFLSTSSNE
KIVSVFALLA IIIYIVLGRV GLLLIGIALG VMLHASWEGA HGQGEEGLQL SKKRKELALE
VSKRLLDRPK RLTSAEIDTQ DNDDLVTAPE DLTATDLNYT TFRPATAAAL RSLTDAVVKD
YVKYWYEPIL PKESVFPESC RRTLTHFVTT VSSHLSRKRT EDTFLQFLTN SSSIIIVFLN
ELAAAFSAGS SSIEAREIVD QYLENAPDSS LANVLSEEQQ RKKLSMIADD ILSNFLDPKA
YGCSPMRDFL REVFSGVVLE STVMSLSRPE FINDWIVYLL EDGESEIMHA IDAGVEGARN
QGVSTPKVSE EAKGALPESK NDQVLSHNTE HHNHSDKATE EAMVEAKRLS AMIASQDVHG
AHEPPAETAQ YAKMRPSTDE TDRSSMQLAN GSQESNISSE AGAMEDQMPF TNSEKPSSIA
ISSLREDSPA PSLSLHGALV MVDDDGAGSE KGHIKSRPTW DYLLQVEPTS TRSTGWMVFR
KYSDFQSLHE MLETVSRLNR ITSFSEQFPT LPAWKGRTRE ALARDLERYL QQAMKHEPLA
ETDRMRRFLE KEVGTSEVTS GKPGFSFPSH SAFENMGKGV LGALTNAPKG VAGGGRAVFD
GMTGVFGGVG HSRKPTNNER LSHHQKSPSR SERGHPSSSG SVGDLNRVNS STEFSTEDHF
DSSRSSGEDH STLASSPTAS SLGMQREEIM SKSLSARDFG NGINPVVSEQ DAWPSESTLA
PSEARKSLGS IGSGKAVEVK EYSDPVPSKP GSKTESTGEW EPGSQNARRQ RQPITADETQ
IAVELIFAVI NELYTLSSAW NIRRTLLNAA KTYILRPGSP TLETIRELLQ DSMIESHTSD
DALGEYLKKL RENALPTEEE LKAWPPPPSE QEKAQLRDKA RRLFVQRGIP QALTSVMGAA
ASREALEKIF DSLQVETVAR GFVFSVLLQG LRVLTL
//
