GenomeNet

Database: UniProt
Entry: A0A072PIP0_9EURO
LinkDB: A0A072PIP0_9EURO
Original site: A0A072PIP0_9EURO 
ID   A0A072PIP0_9EURO        Unreviewed;      1457 AA.
AC   A0A072PIP0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=A1O9_04463 {ECO:0000313|EMBL:KEF59617.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59617.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF59617.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59617.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF59617.1}.
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DR   EMBL; AMGV01000003; KEF59617.1; -; Genomic_DNA.
DR   RefSeq; XP_013262207.1; XM_013406753.1.
DR   STRING; 1182545.A0A072PIP0; -.
DR   GeneID; 25279394; -.
DR   VEuPathDB; FungiDB:A1O9_04463; -.
DR   HOGENOM; CLU_002541_1_0_1; -.
DR   OrthoDB; 2788168at2759; -.
DR   Proteomes; UP000027920; 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:UP000027920};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          1259..1380
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1404..1457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..953
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1457 AA;  160081 MW;  760E1B112EBCD205 CRC64;
     MASEVPPLRI QKGSNGSPSK LPRVTNRPLS ELSPMAIRRN SPSFPQAKGK LFTTSESSPA
     GSSPFSAASP RLFWQGRDPN SPARENSSIF DPLAPSPNKR SSIENLKKAS RVKNSSMFAI
     EQSTNYDPSR PTILDGRPLS VQSLGPQSPI RTSDALRKEN FAPAKSSPGQ YTAKASQEDA
     ASATTKIVSP LSPSRLNTSP AKSSLSKKTG ADFRRSGFDP ETGIWEDEDD VHNKQLPAGR
     GLHRHHKSVT FDQAPPQINE YEEPTPAPSS IASESREGSC ESVEDEDEDL SFERGSSMDH
     DDSFDASLED TEKTPVVLPE DWRFMSPDTA NKDLAHGEED VFDDDCGSPA PTAQPGALAY
     RPHQTSAGSV DSNGQNRPLP PLPPMSLGHK KSPSDRLSGA FERMSIGQRS LPTPPMATTI
     SKADIQKMGT TSSLTADDRL RLMALQEQDR ERRMRRLGSK EPTPVRAASV EDSVIVHGEP
     GPELVESRES TPQISRASVL QGLRGEFSCD SRESSADTDG PHTNRRFDPD VAIPSMEDPT
     HAHAQSAYIK EEDPEDQDLY SIPDAYNRRI VSESDQSANQ DDDMTSQYSQ PSVAGLPVSM
     PALEDGQHTP KAQSPQTAIN SRFLTSERVS LPDFTDFGGG NDFNVGLTPY LSRKEEKLVP
     PIPALSTTNV PDLAALRQSI QRSYSPDTQQ SVVPQSPVVH SFKQRSPGTP ESIVRHSVAV
     KAFGRTQVND FPEVSKSDTN SDRSISPSDS GSVIVNPKEA SPVSPISTEF PENNQVPASL
     SPEAVDQNAV EAKEPAQLQV PVNAKRVSSL VPLEIAHEEL DDGLGLGLEK EFDRVVEAQK
     VEFELSLQRL YYPFNGRFPS NESPPQTNFA NRSNRSYILE EDSFANRSPK QQRGYLMRQN
     TKIVVATERT SQDECRSPGL PTDGDANLLS PRSPANQVQA SPRKTSQPTW TAEPWNGKVR
     RKSIRVGGEK ALGQRKPVSG PAPPLPGQCS NVQESLGAVA EDELGEEEDW EDGAERGRLF
     VKVVGVKDLQ MPFPQHEQTY FALTLDNGLH CVTTAWLELS RSAPIGQEFE LVVLNDLEFQ
     LTLQMKLEEP KVERPQSPSK PPASPKKQGA FGRLFGSPKK KKELELRAQQ EAQAVRRPVT
     PPSAYELVQG LVAKDGSFAR AYVALSEHEK HTYGRPYTVD ITCFNEWALE EVQVGSSRSK
     KGVVQMQRRP PYEIGKLELQ LLYVPKPRGA KDDDMPKSMN GAIRALREAE EKVQQQANIR
     GFEGYLSQQG GDCPYWRRRF FKLAGPKLTA FHETTLQPRA TINLAKASRL IDDKSSLVQK
     ETSTKGGGRR KSGFAEEEEG YMFVEEGFRI RFANGEVIDF YADSTADKDE WMQALAQVVG
     KGVQGSSAPV KGWVEMVLKR EKKTKADGLS GSHPPRPAGH QRTETYHAGG MASHHNSPVK
     SKAGREEKHR KTKSMHA
//
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