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Database: UniProt
Entry: A0A0V1KL94_9BILA
LinkDB: A0A0V1KL94_9BILA
Original site: A0A0V1KL94_9BILA 
ID   A0A0V1KL94_9BILA        Unreviewed;       810 AA.
AC   A0A0V1KL94;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE            EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN   Name=pi4k2b {ECO:0000313|EMBL:KRZ48004.1};
GN   ORFNames=T02_10714 {ECO:0000313|EMBL:KRZ48004.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ48004.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ48004.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ48004.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-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 CBF/MAK21 family.
CC       {ECO:0000256|ARBA:ARBA00007797}.
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:KRZ48004.1}.
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DR   EMBL; JYDW01000493; KRZ48004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1KL94; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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; IPR005612; CCAAT-binding_factor.
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; PF03914; CBF; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW   Transferase {ECO:0000256|RuleBase:RU367084}.
FT   DOMAIN          474..784
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   810 AA;  94533 MW;  01205600354545F4 CRC64;
     MATVHFSLLG QKEMQGLVEL DNLKFVKLIV HADGDVCFNE AVCFDDFNDF VFILKKMEKA
     LSKLRDLLNS ELNDKRNVSR TIVNVVNTTV RCKKGVSESF MSVFSRISCY EDAMSLHNEM
     CYSATLHIFS QCWVNFIRNK LPPSLHCECL LWIDMHILAV VDCPLYFTDF VISSFAMGFP
     LNAAALGSLK HLILICNISY PKLYTAMYNL LQPEIFKLSF RLHFYSVLDT FMHSTHLPTY
     LVAAFIKKLS RLSLRAPLDS CIILLGLIRN WLIRHPACQF LVNRQDEQLQ IKNDPYNMDE
     LNPQLSNAME SFLWEIKTLK NHYNEEVANM ANFVDQLLPS KEVPLKMESA VERVFNKSLL
     RFDGDLAAVC DPPEELFILL FFRNMDQENE FIKKGEMPNF AQNSADVDEA ELFTSGDTVH
     ILYNSEDEEV SESTWKTLHG QIDSLPFLEQ QSWQKNDFEF SCMKQSIEQA VSNGFFPVRL
     PGRSFGSYLV LDEEKNHVGI FKPKDEEEYA TRNPSWMGYF QKMFRLRCPR RGCILANQAY
     LSEVGASIVD EYLDLKIVPK TKVAYLASPT FNYSSAEKRK AEQQRERISG VNLPDKVGSL
     QCVVEGFQPC TFWLKEFASK KLLDNKLQYE LQLLFERVII LDYIIRNTNR TAENLLISYN
     DTRRGNENYA INMAAVDNRY AFPYRHPRRR RPYTYYWATL PLAKKPFSNE TRSFILRKLN
     DMNYMSSLFL QLKRLFELDE NFDKNYFMLQ IMLMHGQIFN LKMALENRET PYELVKRHPV
     YIVPHPDDFT LPAGFLTDKL LQWLKRKYRK
//
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