ID A0A0Q3TZU5_AMAAE Unreviewed; 824 AA.
AC A0A0Q3TZU5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=AAES_22661 {ECO:0000313|EMBL:KQL59294.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL59294.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL59294.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL59294.1};
RA Gilbert D.G.;
RL Submitted (OCT-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}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. 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}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:KQL59294.1}.
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DR EMBL; LMAW01000369; KQL59294.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3TZU5; -.
DR Proteomes; UP000051836; 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; cd22246; PI4KB_NTD; 1.
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 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQL59294.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 73..265
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 543..809
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 12..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 92506 MW; B15F9D144879BC62 CRC64;
MLIRVESFEX CGPTTAMGDS XADPGRRTAL DPVPQGNGGT SLSVITEGVG ELAVIDPEVA
KKACEEVLEK VKLMHGISSD SSAKAAGGRG TERAPRTAMD LVNGELGEGC EIRCLDDPPG
TASKIQEEDE TAANTVKTAR KRQKNNSAKQ SWLLRLFESK LFDISMAISY LYNSKEPGVQ
AYIGNRLFCF RNEEVDFYLP QLLNMYIHMD EDVGDAIKPY IVHRCRQSIN FSLQCALLLG
AYSSDMHIST QRHSRGTKLR KLILSDELKP AYKKRELPSL SPAPDTGLSP SKRTHQRSKS
DATVTISLSS NLKRTASNPK VESEEEPVRL APEREFIKSL IAIGKRLATL PTKEQKTQRL
ISELSLLNHK LPARAWLPTA GFDHHVVRVP HTQAVVLNSK DKAPYLIYVE VLECDNFDTA
NVPARIPENR IRSTRSAENL PECGITHEQR TSSFTTVPNY DNDDEAWSVD DIVELQVELP
EIHTNSCDNI SQFSVDSITS QESREPVFIA AGDIRRRLSE QLAHTPTSFR RDPEDPSAVA
LKEPWQEKVR RIREGSPYGH LPSWRLLSVI VKCGDDLRQE LLAFQVLKQL QSIWEQERVP
LWIKPYKILV ISADSGMIEP VVNAVSIHQI KKQSLLSLLD YFLQEHGSYN TESFLTAQRN
FVQSCAGYCL VCYLLQVKDR HNGNILLDAD GHIIHIDFGF ILSSSPXNLG FETSAFKLTT
EFVDVMGGLD GDMFNYYKML MLQGLIAARK HMDKVVQIVE IMQQGSQLPC FHGSSTIRNL
KERFHMNMTE EQLQLLIDQM VDGSMRSITT KLYDGFQYLT NGIM
//
