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Database: UniProt
Entry: A0A0F8XPN1_9EURO
LinkDB: A0A0F8XPN1_9EURO
Original site: A0A0F8XPN1_9EURO 
ID   A0A0F8XPN1_9EURO        Unreviewed;       819 AA.
AC   A0A0F8XPN1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=PH domain protein {ECO:0000313|EMBL:KKK25512.1};
GN   ORFNames=ARAM_004155 {ECO:0000313|EMBL:KKK25512.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK25512.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK25512.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK25512.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK25512.1}.
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DR   EMBL; JZBS01000732; KKK25512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8XPN1; -.
DR   STRING; 308745.A0A0F8XPN1; -.
DR   OrthoDB; 1363487at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd13311; PH_Slm1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR046868; BAR_4.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR046869; SLM1/RGC1-like_PH.
DR   InterPro; IPR043453; Slm1_PH.
DR   PANTHER; PTHR31941:SF1; ACTIVATOR OF SKN7 PROTEIN 10-RELATED; 1.
DR   PANTHER; PTHR31941; CYTOSKELETAL SIGNALING PROTEIN SLM1; 1.
DR   Pfam; PF20400; BAR_4; 1.
DR   Pfam; PF20399; PH_20; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          431..536
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..124
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..786
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..808
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  89798 MW;  421E6A4CFE088808 CRC64;
     MATLVRSQTP VQDTYGAISQ PQDTLMPSRG YSVRSGSRPN SFAASSSGYN VAHGAVVEPS
     PLGHYGRFQE EFDIASSRGS IDGPSGMQRS ASQMSHSRSA TPTRAGTLKK KSSLSKRGSM
     RRSGSRRSLR AGSVRSLVLG DKDKYAAGGE EDVNSAFYVP VPTGGNPTEV LATRFQSWRK
     ILKDLIVFFK ELQKSYETRA KLYLSTSNII NNTSLPPTFI KSGGLGDATE ILRDFHRQGY
     LEANKAAEIE SEVVNQLMGL RNDLQKKTKE IRALSGDFRN SVDKEVETTR KSVRHLHEAL
     GLVDTDPAAT SGKGDPFIIR LSVDKQIEKQ LEEENYLHRA YLNLENSGRE LESIVVSEIQ
     KAYNAYASIL KREAEETLDT AEKLRVGPIA MPHDHEWNSF IANTDDLVDP RVPLRDIENI
     TYPGRDHPAA AEVRSGMLER KSKYLKSYTP GWYVLSPTHL HEFKSADRVA WQTPVMSLYL
     PEQKLGSHSQ PDSTSHKFML KGRQTGTMHR GHSWVFRAES YETMMTWYKD IESLISKTGE
     ARNAYVRRHV RSVSGTSFRT MSGSSDGVMD EDEADRTPYS AGSVVMSQER PTSQPRQPGG
     RFPSDVQIDR HSQAPLSPSS GESLGETDLL AAGSSPEGVP FGGQNSMSDR ELDSSLLNQS
     QVQPVGNPTR FPIDGHDSYY GEWMGTGAAS HQPPMAHQPP TSMATASPLI PTRTILNIRT
     LSLGASTAFT SSNVTDHTHN TIPTSVDESV GSEHISTAKP AQPILLASAI PRSAPSETSP
     PNTMGRPSLE IPQRPTAQSK NSLSTIELRI PGNYPHAAA
//
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