ID A0A154P0B6_DUFNO Unreviewed; 1048 AA.
AC A0A154P0B6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=WN55_05801 {ECO:0000313|EMBL:KZC05283.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC05283.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC05283.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC05283.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC05283.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-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|ARBA:ARBA00036767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000256|ARBA:ARBA00036767};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004308}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037860}.
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DR EMBL; KQ434787; KZC05283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A154P0B6; -.
DR STRING; 178035.A0A154P0B6; -.
DR Proteomes; UP000076502; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZC05283.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 267..457
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 768..1033
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 116135 MW; 65141A517E391EC3 CRC64;
MSEVVAVTPS GGSTHQESVA HVKRHKLANC NVPLVHGRTN PPINNRNRLT THQRNHSLDF
RSMGILLPPV PQTSATTLTH HHRNRSLDSA LQRIPEVDVT PSPECETTPA PVAKAAVPPC
KVRSREREDL ASLGSDDSGI LCGSDSGSSS DATNAATRES SVDHLHSRES LDSSLSQPGD
MDGVDAVDGE VNSSVRVLST VSVSMPVSPV EIVCLSEPPS KKGEYGDGGS ERGKQPCERE
NTNIGGGETS TQELRSGSAV KELEAHEYRL DELCAEMAVT VDARDFQNPL DVSPVNDKSE
LAGAAMTLCC GTTVQSEANE STVKKPTGVV CRRQETVQPK PSEGCLLRLF ESQIFDMSMA
ISYLFNSKEP GVQSYLGNKM FSFPNTDVDF YLPQLVVMYI QLHDVTEVLY PYLVHRCRQS
ADFSVKCAWL LDAYSSDAHL PSKKKSHGTK LKNLILSDEL RPKGNESKKH RVVGLQTPAP
PLLTTMQSIT SPNKKTHQRS QSDATGLFQT LRRSHSGTIN KAPRLAPELE FIQALISIGK
LLGTIPTKES KTVQLIAELS TLNLNLPARV WLPLHSSVPH HIVRVPPQYA AVLNSKDKAP
YIIYVEVLEV EDIYTSPVPT KIIGHSLRHT KSEENLTGGE QSTVIDSSNI SASETQQNMP
PIRQTPVKNI SPYSVRSTEV AFTFPDDDPI DCWSQEDDEI TQQYLQLRKP KDRDTISQLS
QESSDSKEPI FVPGDIKRRL SEMAAAPSAT FNHDPEDPSA AVLKEPWELK QRRIRASSPY
GHLASWKLLA VIVKCGDDLR QELLASQLLS MLQKIWQDEQ VPLWVQPYKI LCLSNDSGLI
EPILNTVSLH QVKKQCQLTL VQYFEREFGP STSETFITAQ RNFIQSCAAY CLVCYLIQVK
DRHNGNILLH SDGHLIHIDF GFILSTSPRN LGFETSPFKL TPEFVEVMGG SQSKQFQEFK
TLILQGLIAA RKHMEKIVNL VEIMLSGSQL PCFRSGGAAT VQGLKNRFHL TLTEDQLRRH
VEDLVEASIH SWSTKLYDRY QYFANGTL
//
