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
//