ID A0A177C2T9_9PLEO Unreviewed; 767 AA.
AC A0A177C2T9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Phosphatidylinositol 4-kinase {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN ORFNames=CC84DRAFT_1128213 {ECO:0000313|EMBL:OAG00950.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG00950.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG00950.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG00950.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV441558; OAG00950.1; -; Genomic_DNA.
DR RefSeq; XP_018031315.1; XM_018175792.1.
DR AlphaFoldDB; A0A177C2T9; -.
DR STRING; 1460663.A0A177C2T9; -.
DR GeneID; 28759278; -.
DR InParanoid; A0A177C2T9; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000077069; 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 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; 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}; Kinase {ECO:0000256|RuleBase:RU367084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transferase {ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 163..572
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 88600 MW; 027FEF540C7317CD CRC64;
MPRSRRPPNS GYARIAQAEE EEDSHDDSEE EFHERTLASS YAPIQPRKER MRMPQSGDSS
PKLRRTTSGR RQRTNSGVDI KAINARLERW ADEIAQKFKI KKQKDTPEDE ALEIHHSVFQ
APDWVRPATA ETLTFDYEGS SDRMTKLQFD EIVESVQVAI EQGMHPKLIT QGSSGSYFAR
NSQGKVVGVF KPKDEEPYAS RNPKWTKWIH RNLFPFFFGR ACLIPNLSYI SEAAAYVLDC
QLRTNLVPYT EVVSLSSKSF HYDFWDRRAY YRKRKPFPEK AGSFQVFLKG FKDANIFLKE
HPWPDQNNVN LNNARRKKKR RWAEECRPSG PQSDDEDEEE ARSNTPELQH RRGFWTEGLQ
QSFREQLEKL VILDYIMRNT DRGLDNWMIR IDQKTQEASI VAEPPRTDGH LEEDEEVVPS
NYTRQSMSEA DPYGRREPMK ATSRSTTPMA SGPTPAITIG AIDNSLSWPW KHPDAWRSYP
FGWLFLPVSL IGKPFSEATR RHFLPLLTSK LWWAETQAAL RKCFTQDDDF KERMYAKQIA
VMKGQAWNVV ETLKEPDHGP LELTRRARVC VWDDLVEIPI AVPLREPSAE MRRKTQPNRQ
RVAEQEEMDI TALSTPPQKP QPDLLMNSPP MELASENRFN LSRESSSMDV RRQQPDDSGV
ADSQAQAVTW NSRLESGSPS LQTNGRPSHR SRMSYDAPRR RDQDLRRHHR RLSLSSRRGN
GGLFAGDEDD EGDLGYAANE DLDGNRKRVI VERLEMVKAK NPVFTWC
//
