ID A0A0D2BCD7_9EURO Unreviewed; 1395 AA.
AC A0A0D2BCD7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=PV05_11451 {ECO:0000313|EMBL:KIW49806.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49806.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49806.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49806.1,
RC ECO:0000313|Proteomes:UP000054342};
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 Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847323; KIW49806.1; -; Genomic_DNA.
DR RefSeq; XP_013310389.1; XM_013454935.1.
DR GeneID; 25333359; -.
DR HOGENOM; CLU_002541_1_0_1; -.
DR OrthoDB; 2788168at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; 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:UP000054342}.
FT DOMAIN 1204..1325
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 154358 MW; 5A76813D1DB6BC2B CRC64;
MASEVPPLRI QKGSNGTSPS KLPRVTNRPL SELSPMALRR NSPSFPQAKG KLFGIENSPA
DSSPFSGVSP RLFWQGRDPN SPAREIQKLS DTPPPPPTSP TKRSSIENLK KASRVKNSSM
FAMEQSTHYD PSRPTILDGR PHSMQFSRQQ SPFRGSDVNR KENVALVDNS PVHPQGKKPF
EEPDAATNLV APLSPSRLNS PPTKSSLSRK TGAGFRRSGF DPETGIWEDD DDIQNRQLPA
GRGLHRHQKS VTFDQKPPQV NEYEMTTPAP SSCASESREG SYETNDDDEE EEPSFERGSS
MDQDDSFDAS LEDTDKTPVV LPEHWRFMSP DTANTELARH EEDIFDDDCG SPAPTAQPGS
LASRPHQTSA SSVDSNGQSR PLPPLPPGGG RMSRTENLSG ALERLSISGR SLPTPPMAAS
ISKADIQKMG VSSSLTADDR LRLMAIQEQE RERRLRRMGS KENSPVRGAS LEETNLHHDF
QEEISESRNA TPQLSRASVL LALRGQPGDD SRESSEEVDE SSRQRDLSSY DPDVPIPSLE
DPTQQHIKEE ELEEPDLYSI PDLYSRRVVS DSETSANQDD DLTSQYSEAS QAHLAPPVNL
GTEDEQDTPK ALSPIREMSS KSENAGRVSL PEFADFGNGS SFDEGFASYL SLNNDRNKPG
AAAPQPSALP DLAALRQSIQ RSYTPEVQHR QHESHMAAAV EETAPGSPDS VVRHPHAEPS
ATANDGSDVS ETKSATHDDS DRSVSPSDTG SVLVHEKERS PVSPISAEFA DKPVAMQDEL
LHETTVDEQQ ARLDTKAREK NRVSSLVQLD IPHDSLDDGL GLGLEREFDR VVEAQKRGYL
MRQNTKIVYA SERVSQDESR SPELPSIQDE AFAPRSPDAN LVQASPRKTS QPTWTAEPWN
GKMRRKSIRV GGEKAVSKRK PAEGAMPPLP GQVSNVQETL DSVAEDEIAE DDDWEDGAER
GRLFVKVVGV KDLQMPFPKH ERTYFALTLD NGLHCVTTAW LDFARNAPIG QEFELVVLNE
LEFQLTLQMK LDEPKIERPQ SPSKPPSSPK KQGAFGRLFG SPKKKKESEL KAMQEAQAVR
RPVTPPSAYE LVQGLVAKDG SFARAYVSLS EHEKHTYGRP YTVDITCFNE WALEEVHVGS
SRSKKGVVTQ LQRRPPYEIG KLELQLLYVP KPKGAKDEDM PKSMNGAVRA LREAEERVQQ
QASIKSFEGY LSQQGGDCPY WRRRFFKLAG SKLTAFHETT LQPRATINLA KATRLIDDKS
ALVQKETSTK GGGRRKSGFA EEEEGYMFVE EGFRIRFANG EVIDFYADST AEKDEWMKAL
SQVVGKNVQG SAAQIKGWTE MVLRRERKLK AEISTGFRPG HARTETYGGR MSQANSPVKS
RSGPHEHRKT KSMHA
//