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Database: UniProt
Entry: Q0U398_PHANO
LinkDB: Q0U398_PHANO
Original site: Q0U398_PHANO 
ID   Q0U398_PHANO            Unreviewed;      1464 AA.
AC   Q0U398;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=SNOG_13766 {ECO:0000313|EMBL:EAT78790.2};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT78790.2, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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DR   EMBL; CH445352; EAT78790.2; -; Genomic_DNA.
DR   RefSeq; XP_001803972.1; XM_001803920.1.
DR   STRING; 321614.Q0U398; -.
DR   EnsemblFungi; SNOT_13766; SNOT_13766; SNOG_13766.
DR   GeneID; 5980894; -.
DR   KEGG; pno:SNOG_13766; -.
DR   VEuPathDB; FungiDB:JI435_137660; -.
DR   eggNOG; ENOG502REBM; Eukaryota.
DR   HOGENOM; CLU_002541_1_0_1; -.
DR   InParanoid; Q0U398; -.
DR   OrthoDB; 2788168at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd13278; PH_Bud4; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR36100; BUD SITE SELECTION PROTEIN 4; 1.
DR   PANTHER; PTHR36100:SF1; BUD SITE SELECTION PROTEIN 4; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT   DOMAIN          1226..1346
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1065..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1367..1464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..311
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..927
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1095
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1377..1430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1464 AA;  162832 MW;  FA7AEAA108528CBE CRC64;
     MSRNEAVSPL RINKTPTASP TKGSGRPLSE IGSAEHRRNS PSFNQTTKRV FLTKESSPFN
     NSPRLFWKEQ TVSPKNRFDS ENEFERETSP AQLSPKRNSI ENLKKQSRVK NSSMFEREQM
     NTYDPTAVHP LDRPLAAGRP LNASVQGNAY GGNGLNGLRE SRESSVSPTK GHRRTESETR
     IPILSPSKTS PAKLPTQSSF GSPSKENNSP HEGRMSPTKS SLVTNGRFNS PKYNQDSSMM
     SDDDEYKQQT SRPLRRHAKS VTFDTAPPRI TEFEMVTPDP SVTSVSREGS YESEEEEEED
     VSFDQDDSFD ASLEDTEKTP VVLPEDWRHM SPDAANTSLT DLYDDVFDRD NSPMPNAHPN
     GAMNSFRHGS TNSDGDTRPL PPLPGMLAQE GSRRRDSSIG LSAAAERASD SRRSLPQLPQ
     AAGISKSDLL NMREGSMSLE DRLRLMNFDG DRDVSTPTQE SHDKKVEDGV QVQVEELDGF
     TETETEIAVG QPSVVPRISR ESILRRVKSR NFEEEEDSFH YDAESSPERS YGDLADLDPD
     VPIPSRECSS NFDELAHQND NVPESEADSV IDAYSFADMT EVDGTEMSLL EDYERESSVV
     RHPVQHQPQE EDEVSQYSPD PEEQPTTHST IDSSGPPTPT AVSPAAAEKQ ARQEEMYSSF
     DGDKMDLSLD PLKASFATAP SPLDTAPKMD AMREFLRRPA TPETNEEVDA QSEPGTPDSV
     IRHPVVISPP AHEEEPEVPQ REATIRGGKL KTRPSLIPDE VDLAVARRQV SGEHAPPVPV
     RSPKRQSLTF EVGHVDDEDT QMSISNKENR MLDIDIGDDS HDLSFGLDKE FNHIIEAQKF
     PADSAARQDA APQMSGVDFV YRDGPANNFR QQKGYLMREN TKVVVASSRQ FSDEKPSESG
     TAATGPRKTS AERKPAWTKE PWNGKPRRKS IRTTSGRRVP TATGPVPPLP GQESAVQGGL
     DSVAEQGDDD DFEDGEERGR VFVKVVGVKD LDLPLPKTER THFQLTLDNG LHCVTTSWLE
     LGQSAPIGQE FELVVLDDLE FQLTLQTKLE PPAVPQLVAA PARTVNHKKS HSAFRNLLSS
     PKKRKEQERK AQEEADRIAL QEQQEAQAAA KRNHQATAWD LLHDLVGPDG SFARAYVCLN
     NHENQAYGRP LTVDIPCFNE WAVDTTGASS VKSKRGTVVR RPPYRVGKLT VQLLYVPKPK
     GAKDEDMPKS MNACIRELKE AEEVKDINWE GCLSQQGGDC PYWRRRFFRL QGTKLTAYHE
     ATRQPRATIN LAKATKLFDD KGALQQPSST KTGGRRKSGF AEDEEGYMFV EEGFRIRFAN
     GEVIDFYADT REQKEGWMKV LAETVGRDIT AKKGWISMIL EKERKEKAAR SQAGVPAQQA
     RPLQENSNAN RPTHQRTQSH DVFAAPQSKS VPSSPVKGHS RTQSNAPTPP AKDHRMSHAP
     PPRPREANKT GSSGRREQVR SMIF
//
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