ID A0A168KLN4_CORDF Unreviewed; 858 AA.
AC A0A168KLN4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=PH domain containing protein {ECO:0000313|EMBL:OAA81863.1};
GN ORFNames=LEL_01408 {ECO:0000313|EMBL:OAA81863.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81863.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA81863.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81863.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA81863.1}.
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DR EMBL; AZHF01000001; OAA81863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168KLN4; -.
DR STRING; 1081108.A0A168KLN4; -.
DR OrthoDB; 1363487at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR CDD; cd13311; PH_Slm1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
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; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 432..535
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 93515 MW; 2DFF75A473FF7880 CRC64;
MDTDAPHQLH HPPEPSSLAG HDPHHQLLNH HPHASYLEQE APPTTHDYGA YTADHYHFQP
PSGRFTEEWD ASQRGSSIID GHRPNNKLAM QRTASISSYA AGDDTNLPIR NNTLRKKGSV
RRAGSLGRSA SRRSNRAGSV RSLALQSSSD RDEGHSAFYC PVPTSGNPTT ILAERFQTWR
KFLKDLIAYF REIQSHYEQR AKSLTKLGNA ANNVPSPDSF LKSAGIDDAL QLLRSYNRTA
VQEAQKSKEI EEDVILALTG LRSDLQQKIK EIKQLSGDFK NSVEKEMGAT SKAVSALADV
LDKNEVDSSS TTGKQDPFLL RLAVDRQVER QIDEENYLHQ AYLNLEGSGR ELESIVVGEI
QKAYNAYAGI LKREADNALN VVGELREGPI AMPKDQEWIH FVTHEDQVVD PTMPLRAPDQ
IHYPGQDHLS AQEIRAGLLE RKSKYLKSYT AGWYVLSSTH LHEFKSADKN QAPVMSLYLP
EQKVGSHSED GSSSNKFILK GRQTGGMHRG HTWVFRAESH DTMLAWYEDI KALTEKSPEE
RHQFVRTHSR SLSRSSRRSA RSASSDGLDD EDEEPFTGGE VDTNPTARAD AAPRRPEPGG
RFPSDLQVMT QRGLHASQSP SSLSSGAQDY PSDANVIAAA GALPGSHSRD GAYQDNYGYG
GGSGYTPMDE VSSQAAIAHQ QAQYDGVNPY TSEPVQQREA EGGNLGGGHD AVPIVVANTR
VNGDGQEAYQ ATPDAAVAAE LSDPINSKTY TTTGVNDDEV KNISAAAAAA AIVDAEEVPR
SETPVAVQNK ALQVVPESET AAHITPLETP IGEDLPKRSN RPEGHRTDSI VTISNLDIPG
QFPKGGSTAN GSTTNATA
//
