ID A0A091F2I6_CORBR Unreviewed; 731 AA.
AC A0A091F2I6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
DE Flags: Fragment;
GN ORFNames=N302_14865 {ECO:0000313|EMBL:KFO63476.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO63476.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO63476.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO63476.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK719448; KFO63476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091F2I6; -.
DR STRING; 85066.A0A091F2I6; -.
DR Proteomes; UP000052976; 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 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO63476.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..199
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 509..731
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO63476.1"
FT NON_TER 731
FT /evidence="ECO:0000313|EMBL:KFO63476.1"
SQ SEQUENCE 731 AA; 81529 MW; 4A5A92A50AB3E6F8 CRC64;
GSSLSVITEG VGELALIDPE VAKKACEEVL EKVKQLHGAD GIPNGESCQI RCLDDPPGSR
IQEEEEESSN TVRTARKRQN QAKQSWLLRL FESKLFDISM AISYLYNSKE PGVQAYIGNR
LFCFRNEEVD FYLPQLLNMY IHMDEDVGDA IKPYIVHRCR QSVDFSLQCA LLLGAYSSDM
HISTQRHSRG TKLRRLILSD ELKPAARKRE LGGAVPAAGP DTGLSPSKRT HQRSKSDATV
SISLSSNLKR TASNPKVESE EEEFSSSTES LDKSLAPPVR LAPEREFIKS LMAIGKRLAT
LPTKEQKTQR LISALSLLNH KLPAPLESPF PPYPREPRIS PQPGEHPGSS VSLAPVPQAP
YLIYVEVLEC DNFDTANVPA RIPENRIRST RSAENLPECG MGPEQRAGSF STVPNYDNDD
EAWSVDDIVE LQVEVGMSGM GSDAGPRPPN IGNGLGRGAT APGMSMATKV FSWSRAVSSR
RRRLSEQLAH TPTSFRRDPE DPSAVALKEP WQEKVRRIRE ASPYGHLPSW RLLSVIVKCG
DDLRQELLAF QVLKQLQSIW EQERVPLWIK PYKILVISAD SGMIEPVLSA VSIHQIKKQS
QLSLLDYFLQ EHGNYNSESF LSAQRNFVRS CAGYSLVCYL LQVKDRHNGN ILLDADGHII
HIDFGFILSS SPRNLGFETS AFKLTTEFVD VMGGLDGDMF NYYKMLMLQG LIAARKHMDR
VVQIVEIMQQ G
//
