ID A0A0N0BGV1_9HYME Unreviewed; 1114 AA.
AC A0A0N0BGV1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=WN51_13405 {ECO:0000313|EMBL:KOX75098.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX75098.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX75098.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX75098.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX75098.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
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; KQ435774; KOX75098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0BGV1; -.
DR STRING; 166423.A0A0N0BGV1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000053105; 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:KOX75098.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 260..455
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 804..1069
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 99..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 123503 MW; 9B44EC85EB732C19 CRC64;
MSEVVAVTPS GGSTRQENVA HIKRHKLANC NVPLVHGRSN PPINTRSRLT THQRNHSLDF
RSMGILLPPV PQASATTLTH HHRNRSLDSA LQRIPEVDVT PSPECETTPA PAAAKAVAVP
ACKTRSRERD DLASLGSDDS GILCGSDSGS SDATNAATRE SSVDHLHSRE SLDSSLSQPG
DMDSVDVVDS EVTSAPVSVS VSMPVSPVEL VHLSEPSTKK DSDCSSTTSE PHKHENTSSG
DHSSQEPRSN NVCTIKELDG HEYAHDEQRR TADVGVTLDT RDFQNSMEVS PANDKQSELT
GAAMTLCCGT AVQSETSEAA VKKQTGIVCR RQETVQPKPS EGCLLRLFES QIFDMSMAIS
YLFNSKEPGV QSYLGNKMFS FPDNEVDFYL PQLVVMYIQL HDVTEVLYPY LVHRCRQSAD
FSLKCAWLLD AYSSDAHLPS KKKSHGTKLK NLILSDELRP KGNENKKRVT GLQTPALSSL
TPMQSITSPN KKTHQRSQSD ATGLFQTLRR SHSGTINKVS LGDLSSGRAF DNGCTCFYSC
QGVVNDLRGQ KTDCFCNAPR LAPELEFIQA LISIGKLLGT IPTKESKTVQ LIAELNTLNL
NLPARVWLPL HSSIPHHIVR VPPQYAAVLN SKDKAPYIIY VEVLEVEDIY TSPVPTKIVG
CSLRHTKSEE NLTGGEQSNV MGSSNISTSE TQQNMPPVRQ TPVKNISPYS VRSTEVAFNF
PDDDPNDCWS QEDDEITQQY LQLRKPKDRD TISQLSQDSS DSKEPIFVPG DIKRRLSEMA
AAPSATFNHD PEDPSAAVLK EPWELKQRRI RSSSPYGHLA SWRLLAVIVK CGDDLRQELL
ASQLLSMLQK IWQDEQVPLW VRPYKILCLS NDSGLIEPIL NTVSLHQVKK QCQLTLYQYF
EREFGPSTSE AFIIAQRNFI QSCAAYCLVC YLIQVKDRHN GNILLHSDGH LIHIDFGFIL
STSPRNLGFE TSPFKLTPEF VEVMGGSQSK QFQEFKTLIL QGLIAARKHM EKIVNLVEIM
LSGSQLPCFR SGGAATVQGL KNRFHLTLTE DQLRRHVEDL VEASIHSWST KLYDRFLSSL
QTINHFMKPA QRMTKIQNST CVVSAEKPSA VIQL
//
