ID A0A0V1PCG7_9BILA Unreviewed; 424 AA.
AC A0A0V1PCG7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN Name=pi4k2a {ECO:0000313|EMBL:KRZ93930.1};
GN ORFNames=T08_12999 {ECO:0000313|EMBL:KRZ93930.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ93930.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ93930.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ93930.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367084};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00008941,
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:KRZ93930.1}.
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DR EMBL; JYDM01000022; KRZ93930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PCG7; -.
DR STRING; 92180.A0A0V1PCG7; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 Kinase {ECO:0000256|RuleBase:RU367084, ECO:0000313|EMBL:KRZ93930.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transferase {ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 90..400
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 49762 MW; F55F64ECD9680DC9 CRC64;
MDQENEFINN EEMPSYEHNS TDVQKAELLT SGDTVHIVYN GEKYDDREST WETLHGQDGS
LLFLEQQSWQ KNDFQFSCMK KSIEQAVKNG FLPSRIEGSS FGSYLVLDEE KNRVGIFNPK
DEEEYATRNP SRIGWFQKMF RLCCPRRGCI LANQAYLSEV GASIVDECLD LKIVPKTKVA
YLASPTFNYS SAEKRKAEQQ REHIFGVNLP NKVGSLQCVV EGFQPCTFWL KVFASKKLLD
DELKYELQLL FERVIILDYI IRNTNRTAEN LLICYNDTRK GDENYSVNMA AVDNRYAFPY
RHPRRRRPYT YYWATLPLAK RPFSNETRSF ILRRLNDAKR MSSLFEHLKK LFELDENFDQ
DYFKLQMMLM QGQIFNLKMA LENNESPYEL VERCPIYVHT HPDDITLPLN IVTDKTLHLM
KGKY
//
