ID A0A2T5M1J2_9EURO Unreviewed; 1226 AA.
AC A0A2T5M1J2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=PXA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=P175DRAFT_0473324 {ECO:0000313|EMBL:PTU22400.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU22400.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU22400.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU22400.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
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:PTU22400.1}.
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DR EMBL; MSFN02000002; PTU22400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5M1J2; -.
DR VEuPathDB; FungiDB:P175DRAFT_0473324; -.
DR OrthoDB; 5392990at2759; -.
DR Proteomes; UP000244073; 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..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..290
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 418..555
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 866..984
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 138074 MW; 3731B9EF69F06271 CRC64;
MALKRRDYVL LGLGAFIAWG LVVRWLPILR YLGYAVVLGA FLSFAALFGL VLLTTRTSSA
SRPPRAKTLP VAFVARHHWK KEVQAFEQRS LYRPQSLYPQ SFIVSESIDE LLSLITRDFI
SSWHKSISPG PAFVNEVDKV IRIAVGNLRD RLLAEDLVSL IVSRIFPILT AHLREFDIAE
RSVRGRHLTR NVTESEELDL AIASKYRDGN LHPAAVLSLS DQKAVEQEYL RKVTVGLLPR
LFPESVLNSR IVSVLIREIV SCAVLFPLVS VLSDPDTWNQ LMEAYGRTAL QDRKTVRKLR
AALDEHASPV PKSKRGHAFP RLSPNDSERA FERFVRAIRR CNNLSDARRF RALVASQLKR
ESMVEGQDPV YLRRLETGKR VLDQKVSKLS TPGSQPSHTA AAATHFRRKS SSAVQEASLV
DVMHDASGLS YFMEFMDRQR LMSLVQFWIV VDGFRNPLED DFGDETSPSS SSWTSTDRND
MALISETYLT KPELKVTDES RQAVKAFLRS GKRATPEQYR KARTVILTTQ SAVLEELQNV
YYPKFKKSDL YYKYLASDEA SHSGSQNPPP TSRQNPPSAI EARERRPLPP LMARTASQPG
PRPKKDLRRA AISSSDMGKL FDDDESPRRS FDSERSVPLF DDDYDTDPMA ASTQSLTRDS
QNGENETSES RVIENMEAAL NDIITNEPTN GKLEDLRSAD LSPSTLSIHD PNQRSPPGSM
ESSRVDSRVD DRVKPSIASL GLVDKSSRLG VFDDDLFPDQ QKFIEDEYEE PVGTDDKDSA
DEVHEAAPGD LGLTEAIEAL TADIEKLGSQ ESVVDTLTRK AELTNNTAEL RILRKSKASI
QREIHRKEMQ RQQYIIQESD NSLYGRSTVR IKSIVVGKEE DGREFAMYVI EVQRNAGEQM
PAASWAVARR YSEFHELHHQ LRMRYPSVRQ LEFPRRRMVM KLQKEFLQKR RLALEAYLQK
LLLLPEVCRS RDLRAFLSQR AIIPPRDETN PRDGETKDLV TRIYNSVADG MDDFLGNFGV
LDQLSIAGQN LISAATNQQQ QQPPPPPPPS TTTTTNAVTA AEAEAELNAF EDRELEPFIK
PICDLFLETF ELNKGNNWLR GRAVVVVLHQ LLGGTIERKV REGARSLVQD EPLLRYIALA
RETMWPGGVL RESKPRTPSE RLMSRTEASL VLATLIPDLA GNVVGRANAQ AAARRVFATL
NNPRLNAHLV FTLLDEIVLV LFGGRS
//
