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Database: UniProt
Entry: A0A0D2KAI7_9EURO
LinkDB: A0A0D2KAI7_9EURO
Original site: A0A0D2KAI7_9EURO 
ID   A0A0D2KAI7_9EURO        Unreviewed;      1467 AA.
AC   A0A0D2KAI7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=Z520_10847 {ECO:0000313|EMBL:KIX93428.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX93428.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX93428.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX93428.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN848094; KIX93428.1; -; Genomic_DNA.
DR   RefSeq; XP_016627551.1; XM_016781339.1.
DR   STRING; 1442371.A0A0D2KAI7; -.
DR   GeneID; 27716593; -.
DR   VEuPathDB; FungiDB:Z520_10847; -.
DR   OrthoDB; 2788168at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          1272..1393
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          979..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1416..1467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..289
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1452..1467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1467 AA;  161347 MW;  01503ACEA5F846F1 CRC64;
     MASEVPPLRI QKGGGNGPSS SPSKLPRITN RPLSELSPMA IRRNSPSFPQ SKNSPVTSSP
     FSTNSPRLFW QGRDPSSPAR EHTETPPASS PPKRSSIENL KKASRVKNSS MFALEQSTHY
     DPSRPAILDG RPQSMQFPRQ SSPIRGSDAG RKENFAPLDK TSPGQAQASQ QEDESKATAN
     SVTPLSPSRL NSSPAKSSLS KKTGSAFRSS GFNPETGIWE DDEDFQDRQL PAGRGLHRHQ
     KSVTFDQAPP QINEYEMTTP APSSIASGSR EGSYESTDDD EDEDEEASFE RGSSIDHDDS
     FDASLEDTEK TPVVLPEDWR FMSPESANTD LSRHEEDVFE EDCGSPAPTA QPSIPSFRPH
     QTSASSVDSN GQSRPLPPLP PVAGSQGHSR SDSLTGALER MSVASRSLPS PPLATTISKA
     DIQKIGTGTS LSAEDRLRLM ALQEQERERR MRRMGSKDAI PLRSSSNEES LVESCDSRPN
     QSESGNSTPR LSRASILEGL RGQVAAASRE SSEEIPDASQ SRDLSSLDPD VPIPSLEDPT
     QPRIKVEEDE EPDLYSIPDM YMGRTASGSD VSTNHDDDLT SQYSQPSMAS FPAQMTEEGE
     DTPKAQSPAR ELNTKPVTSE RMSLPDFTDF GKTSSFDIGL APYLSNKEEI VKPANVVTPP
     SQLPDLAALR QSIQRPYTPE VQLNAFQSRS TFSPEQAVPA TPESVVRHSA PRTTSPGNVD
     NESEEDERAA QAESDRSISP SESGSVLVHD KELSPVSPIS ANFDENAEVA KGDSTNAEVV
     DENRPETDID GEKKRVSSLV PLDIPTAGLD EGLGLGLEKE FDRVVETQKV EFELSLQRLY
     YPFHGRFPSS ELPEAKEWKG GNPMENIPVL PKPRGARPLR GAHLAISPDR YIDEESFANR
     AGRRQRGYLM RQNTKIVVAS ERISQDECRS PGLPTATEDG LLGVPAEANH VHASPRKTSQ
     PTWTAEPWNG KIRRKSIRVG GEKAVSKRKP VEGPVPPLPG HASNAQEGLD AVAEDEIGEE
     EEWEDGAERG RLFVKVVGVK DLQMPFPQHE RTFFALTLDN GMHCVTTAWL DLARSAPIGQ
     EFELIVLNEL EFQLTLQMKL EEPKVERPQS PSKPPASPKK QGAFGRLFGS PKKKKESDVR
     AQQEAQAARR PVTPPSAYEL VQGLVAKDGS FARAYISLSE HEKQAYGRPY TVDITCFNEW
     AMEEVHVGSS RSKKSVTQLQ RRPPYEIGKL ELQLLYVPKP RGAKDDDMPK SMNGAVRALR
     EAEERLAQQA NIKEFEGYLS QQGGDCPYWR RRFFKLAGTK LTAFHETTLQ PRATINLAKA
     TRLIDDKTAL TQRETSTKGG GRRKSGFAEE EEGYMFVEEG FRIRFANGEV IDFYADSTAE
     KEEWMQALSQ VVGKGVQSGS APIKGWTEMV LRREKKMKAS GPAQRPKVGH QRTETYHAGG
     GMSQANSPVK AAVSREERHR KTKSMYA
//
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