ID M2Y556_GALSU Unreviewed; 1101 AA.
AC M2Y556;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Phosphatidylinositol 4-kinase {ECO:0000313|EMBL:EME30989.1};
DE EC=2.7.1.67 {ECO:0000313|EMBL:EME30989.1};
GN ORFNames=Gasu_17510 {ECO:0000313|EMBL:EME30989.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30989.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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DR EMBL; KB454495; EME30989.1; -; Genomic_DNA.
DR RefSeq; XP_005707509.1; XM_005707452.1.
DR AlphaFoldDB; M2Y556; -.
DR STRING; 130081.M2Y556; -.
DR EnsemblPlants; EME30989; EME30989; Gasu_17510.
DR GeneID; 17089678; -.
DR Gramene; EME30989; EME30989; Gasu_17510.
DR KEGG; gsl:Gasu_17510; -.
DR eggNOG; KOG0903; Eukaryota.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EME30989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EME30989.1}.
FT DOMAIN 817..1086
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 125163 MW; D04444A3F0DF5446 CRC64;
MATAEAQPVD VNRTSENLYN SSDEEQAEQG QTLLACLICG CTNGSGQTNG RSGGIRRRRE
ASAVDLSSWA EPRSSRGVFS LEDALAPVVK AYKNFIEKVG GDVTLVASSF DSESEDSDTE
HRSRGQDSGD IQAVTREEFQ METHKETTEN QNIKVSDKTG EAVQSSANET SGAIALSPRR
AAAKIEQERR SKRFQRHSEV ERQLSETDPQ TALKYRLKAL FRRVAHPKDT YLNSSGSAGG
QIVDGEFLLL AKVYVVQCEE EELDSFARND PASLKHLLPF LLNSLLYGTY DIQREYLQQP
SELTRTTSRF GSAEKDSTRN SRKEFASLNH LRHEMRFLQE ARLLKLISNY NVTDSYRGAF
RLHGKVRRQR LKEARERAAA RKAQLEDGTG SFGSTTLSGT IFGERGYMDS LEPFVLKQCM
RSVEFALHCF WYFQSSLVTG PEELYSRTLR LLLSVEAAVV HHQIPYNIFL QESNGEILEP
SMTHASGVSS QENNLNHWNM PPSSSGIRNS LDLHENSVRE WWNSRMERSS MFHAEIDFIK
GLTDISAQLR KIPRESRQEA LRKELEKLNA FLPRNVAIPT ENRMHRILRV VPEYSVALST
KERCPFLLVY EMEDLSSEGV SSPRKTHREE ESSSHELWSV EEEFGRQSEG DERDSDEINF
TKKFAITKRL GRESSHQMRR TERAAMKKEA VALAAGGAFE NEPNRPEESF NFQPNVNTDV
VLSRERSELG EGTNDVTIAQ ITFNNTEEPN RTVQNESGWT GMVEVDLQDP TGQNNQVSNT
QSFKSNLTCS PSEGQLSGRR EDAPDSNTHA AFGEPFAEKE KRLKDTSPFS YLRRWRLGSC
IVKAHDQLRQ EMFATRLIAE FARIYAASGL PLWLRPYNII ATSSDSGIIE TVRDSTSLDS
IKRNTPNFTT LADFFHRKFG ERGSPRQKMA LRNFVESMAG YSVVQYLLQI KDRHNGNILI
DSEGHIIHID FGFLLSNSPG GNFEFEKSPF KLSAELVQVM GGVHSAAFRQ FRKLCVQGYV
ECCHHRDKIV LMVDMFYSGN ENLPCFTSGR DAVIENLRKR FMPGHTRLQR AQRMMRLIDE
SIDNWHTRWY DRYQRLFTGI H
//
