ID C5P0G2_COCP7 Unreviewed; 785 AA.
AC C5P0G2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Phosphatidylinositol 4-kinase {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN ORFNames=CPC735_068520 {ECO:0000313|EMBL:EER29170.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29170.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER29170.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|RuleBase:RU367084};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU367084};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU367084};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367084};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}. Vacuole
CC membrane {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367084}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|RuleBase:RU367084}.
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:EER29170.1}.
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DR EMBL; ACFW01000009; EER29170.1; -; Genomic_DNA.
DR RefSeq; XP_003071315.1; XM_003071269.1.
DR AlphaFoldDB; C5P0G2; -.
DR GeneID; 9696809; -.
DR KEGG; cpw:CPC735_068520; -.
DR VEuPathDB; FungiDB:CPC735_068520; -.
DR HOGENOM; CLU_009049_2_0_1; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR PANTHER; PTHR12865:SF1; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2; 1.
DR PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367084};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367084};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 172..595
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 89591 MW; 6D96593F7CF0CB23 CRC64;
MAPSKNRPAT SGYARLAQAD EDREFEYESD EDPYAVPPTL SSSVPRYAPI RPTGHMQASR
QSSPSRYRSR RPYYGKSRRG RTDSSGVDIK AINMRLEKWA EEIASKFKIH RVKGKTNEEE
QLEIHHTVFQ APEGVRPVTA ASLEADPPET KRMAESEFND IVESVRVAIE LGVHPKMISQ
GSSGSYFARN SEGKVVGVFK PKDEEPYASR NPKWTKWIHR NLFPCFFGRA CLIPNLSYVS
EAAAYVLDTR LKTHLVPYTD IVWLSSKSFY YDFWDRRRAW RGKKPLPAKQ GSFQVFLKGY
KDANIFLREH PWPDQTSGGF RAEDAPRRKK RPWNEACRPS GIQSDDEDEY QDARMLSPSP
QDDGPRKFYW TENLKQSFRE ELEKLVILDY IMRNTDRGLD NWMIKVDWHT EEVSIVSDPP
KANGINHLDD EDHMPPPRPI SANSERTNSP MYPYRRHETM VATSRTGTPS NAPELLNASI
SVGAIDNSLS WPWKHPDAWR SFPFGWLFLP VSLIGQPFSP KTRDHFLPLL TSTAWWSGTQ
TALRRVFSQD SDFKESMFAR QIAVMKGQAW NVVETLKQAD HGPLELTRRT RVCVWDDLVD
IPVAIPLRVP SGEAQRRHAL DHLESQEEMD ISSAMASEPG PHRDLLSFGS PTNELPNPNR
FELSRDTTSF ESGRTRDRAT SPISFSQADF GNLDRLGESG RELASSWATL PPRPTERQSK
RYGKRPSHRK QASMSRRDST IVFGGDDLEG DLGYAAAEEM EGHERKVIVE RLEAVKSKNP
VFTWC
//
