GenomeNet

Database: UniProt
Entry: G8BG05_CANPC
LinkDB: G8BG05_CANPC
Original site: G8BG05_CANPC 
ID   G8BG05_CANPC            Unreviewed;      1917 AA.
AC   G8BG05;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   OrderedLocusNames=CPAR2_204320 {ECO:0000313|CGD:CAL0000149231,
GN   ECO:0000313|EMBL:CCE42789.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE42789.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE605206; CCE42789.1; -; Genomic_DNA.
DR   STRING; 578454.G8BG05; -.
DR   EnsemblFungi; CPAR2_204320-T; CPAR2_204320-T-p1; CPAR2_204320.
DR   CGD; CAL0000149231; CPAR2_204320.
DR   VEuPathDB; FungiDB:CPAR2_204320; -.
DR   eggNOG; KOG0902; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 2.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05167; PI4Kc_III_alpha; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR045495; PI4K_N.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   Pfam; PF19274; PI4K_N; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1361..1545
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          1638..1901
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          472..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1917 AA;  218004 MW;  9E7408924CCD3885 CRC64;
     MDFYGITRGT IRGEALKKLA ELTVEHVPSN LKEINTGIQK DDFAKLLTST PRDLPLRKSI
     GSSINDQKMS NVAIAPKEYE TLVALCDATD KPIKLTSQIK TLIDKFRVYL FELPDQQFAY
     SIVAKSVAVA PWTLLGEKLT IALINLAYQS NKQYFDEVVE VFHQFIDKFF DNVDLQLSNF
     LTLTGVIDGL NQNAQFLTYS SRTFRIFTNL DSAIDNSEIL GAIEDYSDYL YDDPNPYQEL
     LERDFCLNFS PVLYLEKLSR LMCSILVEIV ASKSQHLLPY LLTQAAKKYD EDESNGRAII
     GPGRDHLSFP RAHMEIIKIL TDLALRKLEF LDRGETYIVY STNNRLKLGY LAKSFNLQVL
     SCGMFTDNLD LATSKELFKA NIEIKDAMLD PDLGLTTFQF GSLLVFKDES IGPLLTRVFT
     SVIANPRLES SYCLEASKCV GLGSKRLPQD AVVTTIYSLT NLLFVTNEGL QGPSKSARRA
     ARNHTGGADN ASTRDFVSSP LSSSRTSMTS FSQLFSKGSL SGDFDENDYQ KVCENAVTAI
     IEVSEACDDE SIPALACTIL SQKVTKVESP IGPLILRGLC SCAPYVPERE FIILIRLLNK
     LTVDSFERKN ATLLGHLNES RLILSSKLKP DNHLYFVYLH ELLQSIISKG DVQQLEHHRS
     HNEISEVGDQ IAIYLKPLAE LLPDVHLGQE PLKIEKTETI NLFRNIWFNM VVHGYNLNSK
     NTKVFKDELE RIAYNSPPLA SERSWDRTET SIELNTVLRR GSSNHNIKDH KTFLGDIFEV
     HRTMSYPKLM FLSATVFCET LRVRTGDCSK ILYYFTDPTS KISGIDKYLG PIAFKIVRDY
     IGLINTGANK QFTADHIANQ LTTMLTLTTH PVTEMQDASI QCCDLLINKV SASLCHKKSL
     FALFDILTLL FQSIADADVH EYDPTTSFRA RCTGIKITLS DDYDWRCSTF NRFHEKAKGW
     VELLLYKSNI DVKSLIQSYV AANEELQYEA PIQFGLSFAL KMSGTISSHD RDIQAITYAN
     ISALDTTPSI VSQLNWRSNF VSQFMNKLPL RTDEESDFAF KAIREKVYNI KSRLFNEFTE
     NPSHDEIMNL LTEIAGLTLL SDINNAELVR YMVEIPFILF EPSVMIPASG VWFAVMKDKP
     KLSMLLLSEL AQKWEESIEL RKGLFSQELD IVHPEFDKME YAPSNRSTDL RLAENAQRSF
     EPHLELVRLF SSNFEATLNQ SDHLLKLFTR FVEVGLKNLK FASYHPLSRL VRFELVRFAF
     EVLQVHLKLG SRICKYLTEL IFDGALTWFR QRFVYPFSAN KLKFKSEAIV MNEVARMAGA
     VSVFRSKDIE MKRTIFLQFL DDEVYKFNVW LTSLNPTDTS GSIIGSSHQV SSTQITRAYE
     IDPILAINLA MRYKSKAHDD LIQQLIIKNP LAAIPYPDAV QFFIGINLGV HMPSHQLLFW
     SPVAPIDAIT LFLPPFGANP YILQYTMRSL ETHDVNLTFF YVPQIVQSLR HDAKGYVERF
     IIETAKVSQL FAHQIIWNML ANSYKDDDST EPDDLKPVLD RIQEHMLKEL SDKDLQFYHK
     EFGFFNEVTD ISGKLKPYIK KSKAEKKAKI DEEMALIKVE PGVYLPSNPD GVLVDINRKS
     GKPLQSHAKA PFMATFKIKK ELTDYDEHGK PQQVEIEKWQ SAIFKVGDDC RQDVLALQLI
     SMFRTIWSDA GLDLYVYPYR VTATAPGCGV IDVLPNANSR DMLGREAVNG LFEYYITKFG
     PQKSIEFQKA RNNLVKSLAA YSIISYLLQF KDRHNGNIMY DDQGHILHID FGFCFDIVPG
     GVKFEAAPFK LTHEMVMVLG GSDDTQAFKW FEELCIKGYL ACRPYMELIV RTVVPMLESG
     LPCFKDTTIK NLRSRFVPGK SDKEAAVYFR KLIKKSMESF YTKGYDEFQR ITNGIPY
//
DBGET integrated database retrieval system