(data stored in ACNUC7421 zone)

SWISSPROT: Q750P3_ASHGO

ID   Q750P3_ASHGO            Unreviewed;       547 AA.
AC   Q750P3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   SubName: Full=AGL096Wp {ECO:0000313|EMBL:AAS54395.1};
GN   ORFNames=AGOS_AGL096W {ECO:0000313|EMBL:AAS54395.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54395.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54395.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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DR   EMBL; AE016820; AAS54395.1; -; Genomic_DNA.
DR   RefSeq; NP_986571.1; NM_211633.1.
DR   STRING; 33169.AAS54395; -.
DR   EnsemblFungi; AAS54395; AAS54395; AGOS_AGL096W.
DR   GeneID; 4622870; -.
DR   KEGG; ago:AGOS_AGL096W; -.
DR   HOGENOM; HOG000193875; -.
DR   InParanoid; Q750P3; -.
DR   KO; K00889; -.
DR   OMA; ANHTINE; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0031321; P:ascospore-type prospore assembly; IEA:EnsemblFungi.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:EnsemblFungi.
DR   Gene3D; 3.30.800.10; -; 1.
DR   Gene3D; 3.30.810.10; -; 1.
DR   InterPro; IPR023610; PInositol-4-P-5-kinase.
DR   InterPro; IPR027483; PInositol-4-P-5-kinase_C.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   PANTHER; PTHR23086; PTHR23086; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   4: Predicted;
DR   PRODOM; Q750P3.
DR   SWISS-2DPAGE; Q750P3.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW   Kinase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00781}.
FT   DOMAIN          150..538
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..24
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  62736 MW;  DD2CCF92910BD50A CRC64;
     MERQPESLRS ANQFSASSSP TSVESIGTAM KALGERRSLV ERGSYIEDLE DERVLLNRTL
     SGRRRVARRA TSVQQKHARI FAAEEQGENA RGAEAAPVRR RSSQFLNDGA MKASESATAE
     LKKMRESLLI KREMKRKQRH LLDDDRVLVG NKVSEGHVNF IIAYNMLTGI RVAVSRCSGL
     MKPLSQRDFH QTKKLAFDYH GNELTPSSQY AFKFKDYCPE VFRELRARFG LDPADYLMSL
     TSKYILSELN SPGKSGSFFY FSRDYKYIIK TIHHSEHKHL RHVLHDYYEH VKANPDTLIC
     QFYGLHRVKM PISFKNKVKN RRIYFIVMNN LFPPHLEMHT TFDLKGSTLG RYTKVSKEDE
     DARPVLKDLN WLEQHMNIQF GPHKGRVFLN QLKKDVDFLS RLNIMDYSLL LGIHDINLAA
     ANSEDIHAMI PESSAKHALT SAFPANSNSN ININNVITNA SNNHFFQRDE GGIRASDAEN
     KDLNIIYYIG IIDCLTNYSL LKKLETFWRG LSHDLYAVSA VPPNDYGLRF YKFIEDSVTQ
     GKTGHRD
//

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