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Database: UniProt
Entry: A0A2V0PCH0_9CHLO
LinkDB: A0A2V0PCH0_9CHLO
Original site: A0A2V0PCH0_9CHLO 
ID   A0A2V0PCH0_9CHLO        Unreviewed;      1549 AA.
AC   A0A2V0PCH0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=Rsub_10090 {ECO:0000313|EMBL:GBF97229.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF97229.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF97229.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF97229.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:GBF97229.1}.
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DR   EMBL; BDRX01000094; GBF97229.1; -; Genomic_DNA.
DR   STRING; 307507.A0A2V0PCH0; -.
DR   InParanoid; A0A2V0PCH0; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
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; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GBF97229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          978..1143
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          1251..1533
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          310..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1256..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1549 AA;  159985 MW;  4D07F4D2309C1789 CRC64;
     MLLFASAAER AAPGGGGGGG CARDLGALLP AVAAAVEGLQ PRTLQVLGGS SSRMGIHDIQ
     AAQREDASTT RLFRNLWLQA ALHGLVDPTR PRAPVLAPRL WGHDGADAGD VEWQDAAGRV
     AGVTPLLVVG TDSYLEADMV ERLKVELGDQ LNAAGRLAER GAAAAALCRL VDSGAPGGAP
     PPAPGEKVLQ AFLLAVAMSE LCRAALAPLP DLDAEPIVAC PVSTTLGYLK GLLPAGAASD
     WVAAIARRAF GLYLARLVAL RSLQQAAALG DGARGGARAG PASAAAAGAA PALAYAEQLA
     RALIAHLGDG GGDGDARAAP RRRRRRRGGG GGAPDLGGIA DSMLEQLLVS FPALLHSRPV
     YAALLAQLQR EEGDSGLGAL AASSHGAVWE RTQAVVRAAA QAAPATTEAM VHSFLGSGGV
     GGGRARGAGR GGLGGLGALG SGSFGARHRG PLAGAGARGG DGGLGEEAAA RQAALRRAAD
     LLRVCGDARE ARAGDADGAS GGPDGGAYQG TLALSRKLHY SGYARGLINQ ALTAVQGSSD
     GGGGGARRGA SPGAESSGSS GLGGAAAQAA AIKEVASELS AALNADLDGH SRAAAALAAA
     PDDALLCATA LLASQPLLAG AQDWGAGEGD DAGEGSDREA AALDALRGEG LRLLRALCAA
     PLRRLTPDAT QLATFAWTWL STESPGMLVP LVCNLAGAWV WTVDQRLGLF SGQPRGPAAS
     AGGASAGDAA AGDAAAAVAA AAAADQEGEG EEAPADANDP DVLRAIAAHD VWLSYLAELW
     TVLRRRGGAV GAAARAQFAR LLHASLAEPA ALSAHAASLG PRFRLLQLAV NFARDLARDS
     GGAPPAAALL LFDQSLRAAL FWFAAPPGYY AAHTRGEARE QLASLEGFSQ LLASFPPGGW
     PTYSPTAAAA AGAGAAPAEH PVWRVAAPRV GGYVRLLQLL LGEEVKRVQV WNEPLEDAPI
     TGLPEKAPWD ELVPLAWEVD PSLALALRAR YPTVAGIARP LEALVLQHAE EPRVQREPDA
     ALVLATARSP ARDALLPLLA AWAPGRATLG LQLLCGPAGR EAAVRSYSVK CLLNERPEEV
     VFFLPQLVQL LRGDDGVVAG FFTAAASHSD LFAHRLIWAL MSEQRPPEEA FAPEVKRSGW
     QPPKDTGLWD ISTRIKGEIE GGMSPEQKEY WEAEGGYFDQ VTALSGYLYK FSKDERRGKL
     VEALTGFKPP RDDLYMPTNP EARIVSHIPS SGACMQSAAK VPILVAFNVE RPPPASASAG
     GAAPAAAPAP PHGPRASHGG PPRVSAKMAA IFKVGDDIRQ DVLAIQVITL LHAAFTRAGL
     GLYLRPYGCM PTGYECGIIE CVPNTRSRAA LGELSDRGLY DIFCAEFGAP GSAAFESARH
     NFIVSEAAYA VASFLLQAKD RHNGNIMLDD EGHIVHIDFG FILEISPGGN LGFESAAFKL
     SHEMAQLLDP GGRRASPQFR LFEEAVVRAY IAARTVAEPI ISSVALMAES GLPCFGRGAP
     VANLRRRFHL ELSDSQAAAW MRATVNDAYD KWTTGFYDYI QSLQNKIPY
//
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