ID A0A0V1I1A8_9BILA Unreviewed; 524 AA.
AC A0A0V1I1A8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN Name=Tmem11 {ECO:0000313|EMBL:KRZ16696.1};
GN ORFNames=T11_1022 {ECO:0000313|EMBL:KRZ16696.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ16696.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ16696.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ16696.1};
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:KRZ16696.1}.
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DR EMBL; JYDP01000010; KRZ16696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I1A8; -.
DR Proteomes; UP000055024; 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:KRZ16696.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transferase {ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 139..490
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 60001 MW; 2EFC630D8949F581 CRC64;
MDKSNTSNNA SDDDKVENEE ERIVEDVAKQ CFPPLPDVTY SYSNPTPKLS SSCGGSDTAN
IRVVSDLNLR NLSLFKYKSR SRSADGDETI QSTPSLSSRR EKVPLLARMS DSCITHCSFP
GDTVYNDMLQ QAEEAIEAGV YPKRIAQGSS ACGLAKFEFS KNCGIHLFFI PSNLSIVITE
IIGVFKPKNE EPYGHLNPKW LKWMQRVCCP CCFGRSCLPL NQGYLSEAAA SLVDEKLQLH
VVPKTKVVRL AAPTFNYSRI DHAKAQTKQH IMEKYPNIGR HFHRLGLPRK IGSLQTFVSG
YKDANYWLAH FEQEPLSEAA KVQFQRQFER LVILDYIIRN TDRGSDNWLI KYVHEDQVNG
EQMVDVECDD KESSALIKIA AIDNGLAFPL KHPDEWRAYP FHWAWLKQAR EPFSDETRRL
MLPRIEDLDF VMELCDDLKK LFETDQGFDP QIFEKQMSVL RGQILNLCQA LKECKSPLQL
VQMPPMIIEK TKEHVRSKTR ARWDSFKQSF QKRAPFFSCY SSIL
//
