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Conserved domains on  [gi|767996107|ref|XP_011523632|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 beta isoform X4 [Homo sapiens]

Protein Classification

phosphatidylinositol phosphate kinase family protein( domain architecture ID 1000257)

phosphatidylinositol phosphate kinase (PIPK) family protein may catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIPKc super family cl28923
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 1-281 3.97e-125

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family includes phosphatidylinositol 5-phosphate 4-kinases (PIP5Ks) and similar proteins. PIP5Ks catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. The family includes type I and II PIP5Ks (-alpha, -beta, and -gamma) kinases. Signalling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling.


The actual alignment was detected with superfamily member cd17310:

Pssm-ID: 475131  Cd Length: 311  Bit Score: 358.98  E-value: 3.97e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   1 MHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 80
Cdd:cd17310  131 MHNILKKYHQ---------------------------FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  81 RKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdrae 160
Cdd:cd17310  184 RKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---- 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 161 qeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILT 240
Cdd:cd17310  260 ---------------------------------------------------------------------VYFMAIIDILT 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767996107 241 PYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 281
Cdd:cd17310  271 PYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-281 3.97e-125

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 beta (PIP5K2B) and similar proteins; PIP5K2B (EC 2.7.1.149), also known as 1-phosphatidylinositol 5-phosphate 4-kinase 2-beta, or diphosphoinositide kinase 2-beta, or phosphatidylinositol 5-phosphate 4-kinase type II beta, or PI(5)P 4-kinase type II beta, or PIP4KII-beta, or PtdIns(5)P-4-kinase isoform 2-beta, or PIP5KIIbeta, or PIP4K2B, participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. It directly regulates the levels of two important phosphoinositide second messengers, PtdIns5P and phosphatidylinositol-(4,5)-bisphosphate (PtdIns(4,5)P2), one of the key metabolic crossroads in phosphoinositide signaling. It regulates the levels of nuclear PtdIns5P, which in turn modulates the acetylation of the tumour suppressor p53. It also interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha. Moreover, PIP5K2B is a molecular sensor that transduces changes in GTP into changes in the levels of the phosphoinositide PtdIns5P to modulate tumour cell growth.


Pssm-ID: 340447  Cd Length: 311  Bit Score: 358.98  E-value: 3.97e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   1 MHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 80
Cdd:cd17310  131 MHNILKKYHQ---------------------------FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  81 RKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdrae 160
Cdd:cd17310  184 RKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---- 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 161 qeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILT 240
Cdd:cd17310  260 ---------------------------------------------------------------------VYFMAIIDILT 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767996107 241 PYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 281
Cdd:cd17310  271 PYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
39-283 6.42e-77

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 237.28  E-value: 6.42e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107    39 IVECHgNTLLPQFLGMYRLTVDG---VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDFLNE- 114
Cdd:smart00330 108 IVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREA-DKKKVKELPVLKDLDLVEMw 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   115 GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGgnllcSYGTPPDS 194
Cdd:smart00330 186 NQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPPVYGSDESPSSESS-----NGGKAPDI 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   195 PGNLLSFPRFFGPGEFDpSVDVYAMKSHEsspkkEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKR 274
Cdd:smart00330 261 TGNLLVSNSPDGDGPFG-GIPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHWVKSIGHD-GKTISVVHPEQYAKR 333


                   ....*....
gi 767996107   275 FNEFMSNIL 283
Cdd:smart00330 334 FRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 43-282 2.29e-64

Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common kinase core found in the type I phosphatidylinositol-4-phosphate 5-kinase (PIP5K) family as described in. The family consists of various type I, II and III PIP5K enzymes. PIP5K catalyzes the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signaling pathway.


Pssm-ID: 460234  Cd Length: 227  Bit Score: 201.54  E-value: 2.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   43 HGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVG 121
Cdd:pfam01504  55 NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  122 EESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvggnllcsygtppdspgnllsf 201
Cdd:pfam01504 135 PEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD-------------------------------------------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  202 prffgpgefdpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 281
Cdd:pfam01504 171 -----------------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEK 226


                  .
gi 767996107  282 I 282
Cdd:pfam01504 227 I 227
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
43-155 1.36e-23

Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 100.02  E-value: 1.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  43 HGNTLLPQFLGMYRL-------TVDGVETYMVVTRNVFSHRLtVHRKYDLKGSTVAREASDKEKAKD-LPTFKDNDFLNE 114
Cdd:COG5253  415 NPLTLLCKIFGFYRVksrssisSSKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWIRE 493

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767996107 115 GQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHD 155
Cdd:COG5253  494 SPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD 533
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 40-282 1.46e-17

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 82.57  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  40 VECHGNTLLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDfLNegQKL 118
Cdd:PLN03185 483 VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLD-LN--YSF 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 119 HVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG----------------- 181
Cdd:PLN03185 559 YLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvvaeedtiedeelsype 634

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 182 GNLLCSYGTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE-------------VYF 232
Cdd:PLN03185 635 GLVLVPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREdkekqsfhevydvVLY 714

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767996107 233 MAIIDILTPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 282
Cdd:PLN03185 715 LGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-281 3.97e-125

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 beta (PIP5K2B) and similar proteins; PIP5K2B (EC 2.7.1.149), also known as 1-phosphatidylinositol 5-phosphate 4-kinase 2-beta, or diphosphoinositide kinase 2-beta, or phosphatidylinositol 5-phosphate 4-kinase type II beta, or PI(5)P 4-kinase type II beta, or PIP4KII-beta, or PtdIns(5)P-4-kinase isoform 2-beta, or PIP5KIIbeta, or PIP4K2B, participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. It directly regulates the levels of two important phosphoinositide second messengers, PtdIns5P and phosphatidylinositol-(4,5)-bisphosphate (PtdIns(4,5)P2), one of the key metabolic crossroads in phosphoinositide signaling. It regulates the levels of nuclear PtdIns5P, which in turn modulates the acetylation of the tumour suppressor p53. It also interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha. Moreover, PIP5K2B is a molecular sensor that transduces changes in GTP into changes in the levels of the phosphoinositide PtdIns5P to modulate tumour cell growth.


Pssm-ID: 340447  Cd Length: 311  Bit Score: 358.98  E-value: 3.97e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   1 MHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 80
Cdd:cd17310  131 MHNILKKYHQ---------------------------FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  81 RKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdrae 160
Cdd:cd17310  184 RKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---- 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 161 qeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILT 240
Cdd:cd17310  260 ---------------------------------------------------------------------VYFMAIIDILT 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767996107 241 PYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 281
Cdd:cd17310  271 PYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
 1-281 5.25e-109

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II phosphatidylinositol 5-phosphate 4-kinase (PIP5KII) and similar proteins; PIP5KIIs, also known as PIPKIIs, or PI4P5KIIs, are responsible for the synthesis of phosphatidylinositol-4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes, from phosphatidylinositol-5-phosphate (PtdIns5P). Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K2A, PIP5K2B, and PIP5K2C isoforms.


Pssm-ID: 340442  Cd Length: 300  Bit Score: 317.68  E-value: 5.25e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   1 MHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 80
Cdd:cd17305  120 MHHILKQYHQ---------------------------YIVERHGKTLLPQYLGMYRITVNGVETYLVVMRNVFSPRLPIH 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  81 RKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdrae 160
Cdd:cd17305  173 KKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDC---- 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 161 qeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILT 240
Cdd:cd17305  249 ---------------------------------------------------------------------IYFMAIIDILT 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767996107 241 PYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 281
Cdd:cd17305  260 HYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-281 7.78e-102

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (PIP5K2A) and similar proteins; PIP5K2A (EC 2.7.1.149), also known as PIP4K2A, or 1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha, or diphosphoinositide kinase 2-alpha, or PIP5KIII, or phosphatidylinositol 5-phosphate 4-kinase type II alpha, or PI(5)P 4-kinase type II alpha, or PIP4KII-alpha, or PtdIns(4)P-5-kinase C isoform, or PtdIns(5)P-4-kinase isoform 2-alpha, catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), one of the key metabolic crossroads in phosphoinositide signaling. It is possibly involved in a mechanism protecting against tardive dyskinesia-inducing neurotoxicity. PIP5K2A is associated with schizophrenia. It controls the function of KCNQ channels via phosphatidylinositol-4,5-bisphosphate (PIP2) synthesis, and plays a potential role in the regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors.


Pssm-ID: 340446  Cd Length: 309  Bit Score: 299.97  E-value: 7.78e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   1 MHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 80
Cdd:cd17309  129 MHNILKKYHQ---------------------------YIVECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVY 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  81 RKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdrae 160
Cdd:cd17309  182 RKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV---- 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 161 qeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILT 240
Cdd:cd17309  258 ---------------------------------------------------------------------VYFMAIIDILT 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767996107 241 PYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 281
Cdd:cd17309  269 HYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-281 5.69e-89

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (PIP5K2C) and similar proteins; PIP5K2C (EC 2.7.1.149), also known as 1-phosphatidylinositol 5-phosphate 4-kinase 2-gamma, or PI5P4Kgamma, or diphosphoinositide kinase 2-gamma, or phosphatidylinositol 5-phosphate 4-kinase type II gamma, or PI(5)P 4-kinase type II gamma, or PIP4KII-gamma, or PIP4K2C, may play an important role in the production of phosphatidylinositol bisphosphate (PIP2) in the endoplasmic reticulum. It contributes to the development and maintenance of epithelial cell functional polarity. It also plays a role in the regulation of the immune system via mTORC1 signaling. Moreover, PIP5K2C is involved in arsenic trioxide (ATO) cytotoxicity. It mediates PIP2 generation required for positioning and assembly of bipolar spindles and alteration of PIP5K2C function by ATO may thus lead to spindle abnormalities.


Pssm-ID: 340448  Cd Length: 298  Bit Score: 266.73  E-value: 5.69e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   1 MHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVH 80
Cdd:cd17311  118 MHSILSHYHQ---------------------------YIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVH 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  81 RKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdrae 160
Cdd:cd17311  171 RKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV---- 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 161 qeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILT 240
Cdd:cd17311  247 ---------------------------------------------------------------------VYFMGLIDILT 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767996107 241 PYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 281
Cdd:cd17311  258 QYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
39-283 6.42e-77

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 237.28  E-value: 6.42e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107    39 IVECHgNTLLPQFLGMYRLTVDG---VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDFLNE- 114
Cdd:smart00330 108 IVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREA-DKKKVKELPVLKDLDLVEMw 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   115 GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGgnllcSYGTPPDS 194
Cdd:smart00330 186 NQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPPVYGSDESPSSESS-----NGGKAPDI 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   195 PGNLLSFPRFFGPGEFDpSVDVYAMKSHEsspkkEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKR 274
Cdd:smart00330 261 TGNLLVSNSPDGDGPFG-GIPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHWVKSIGHD-GKTISVVHPEQYAKR 333


                   ....*....
gi 767996107   275 FNEFMSNIL 283
Cdd:smart00330 334 FRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 43-282 2.29e-64

Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common kinase core found in the type I phosphatidylinositol-4-phosphate 5-kinase (PIP5K) family as described in. The family consists of various type I, II and III PIP5K enzymes. PIP5K catalyzes the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signaling pathway.


Pssm-ID: 460234  Cd Length: 227  Bit Score: 201.54  E-value: 2.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107   43 HGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVG 121
Cdd:pfam01504  55 NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  122 EESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvggnllcsygtppdspgnllsf 201
Cdd:pfam01504 135 PEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD-------------------------------------------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  202 prffgpgefdpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 281
Cdd:pfam01504 171 -----------------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEK 226


                  .
gi 767996107  282 I 282
Cdd:pfam01504 227 I 227
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 43-281 2.93e-55

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family includes phosphatidylinositol 5-phosphate 4-kinases (PIP5Ks) and similar proteins. PIP5Ks catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. The family includes type I and II PIP5Ks (-alpha, -beta, and -gamma) kinases. Signalling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling.


Pssm-ID: 340436  Cd Length: 253  Bit Score: 178.92  E-value: 2.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  43 HGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAS-DKEKAKDLPTFKDNDFLNEGQKLHV 120
Cdd:cd00139   86 NPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKGEKIIL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 121 GEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnlls 200
Cdd:cd00139  166 GPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL-------------------------------------------- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 201 fprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMS 280
Cdd:cd00139  202 -----------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERFLKFME 252


                 .
gi 767996107 281 N 281
Cdd:cd00139  253 S 253
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
 40-281 1.74e-47

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) and similar proteins; PIP5K (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase, or diphosphoinositide kinase, phosphorylates phosphatidylinositol-4-phosphate to produce phosphatidylinositol-4,5-bisphosphate as a precursor of two second messengers, inositol-1,4,5-triphosphate and diacylglycerol, and as a regulator of many cellular proteins involved in signal transduction and cytoskeletal organization. The family includes Saccharomyces cerevisiae PIP5K MSS4, Schizosaccharomyces pombe PIP5K Its3. MSS4 is required for organization of the actin cytoskeleton in budding yeast. Its3 is involved, together with the calcineurin ppb1, in cytokinesis of fission yeast.


Pssm-ID: 340440  Cd Length: 318  Bit Score: 160.92  E-value: 1.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  40 VECHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAS-DKEKAKDLPTFKDNDFLNEGQK 117
Cdd:cd17303  133 VKENPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPeDKLAKGPRATLKDLNWLRRKRK 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 118 LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvGGnllcsygtppdspgn 197
Cdd:cd17303  213 LALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD-----------------------GG--------------- 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 198 llsfprFFGPGEFDpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNE 277
Cdd:cd17303  255 ------FQATDENN-------------EPGDEIYYLGIIDILTPYNAKKKLEHFFKSLRH-DRHTISAVPPKEYARRFLK 314


                 ....
gi 767996107 278 FMSN 281
Cdd:cd17303  315 FIED 318
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
 43-281 4.53e-35

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinases (PIP5KI) and similar proteins; PIP5KIs, also known as PIPKIs, or PI4P5KIs, phosphorylate the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes. Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K1alpha, PIP5K1beta, and PIP5K1gamma isoforms.


Pssm-ID: 340438  Cd Length: 320  Bit Score: 128.52  E-value: 4.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  43 HGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLN---EGQKLh 119
Cdd:cd17301  136 NPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEdhpEGILL- 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 120 vgEESKKNFLEK-LKRDVEFLAQLKIMDYSLLVGIHDvdraeqeemeveeraedeecendgVGGnllcsygtppdspgnl 198
Cdd:cd17301  215 --EPDTYDALLKtIQRDCRVLESFKIMDYSLLLGVHN------------------------LGG---------------- 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 199 lsfprffgpgefdpsvdvyaMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEF 278
Cdd:cd17301  253 --------------------IPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNF 311


                 ...
gi 767996107 279 MSN 281
Cdd:cd17301  312 MAN 314
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
 40-282 2.31e-31

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) and similar proteins; PIP5K (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase, or diphosphoinositide kinase, phosphorylates phosphatidylinositol-4-phosphate to produce phosphatidylinositol-4,5-bisphosphate as a precursor of two second messengers, inositol-1,4,5-triphosphate and diacylglycerol, and as a regulator of many cellular proteins involved in signal transduction and cytoskeletal organization. The family includes several PIP5Ks from Arabidopsis thaliana. AtPIP5K1 is involved in water-stress signal transduction. AtPIP5K2 acts as an interactor of all five Arabidopsis RAB-E proteins but not with other Rab subclasses residing at the Golgi or trans-Golgi network. AtPIP5K3 is a key regulator of root hair tip growth. AtPIP5K4 and AtPIP5K5 are type B PI4P 5-kinases expressed in pollen and have important functions in pollen germination and in pollen tube growth. AtPIP5K6 regulates clathrin-dependent endocytosis in pollen tubes. AtPIP5K9 interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth.


Pssm-ID: 340439  Cd Length: 314  Bit Score: 118.55  E-value: 2.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  40 VECHGNTLLPQFLGMYRLT-VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFlneGQK 117
Cdd:cd17302  136 VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTtLKDLDL---DFK 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 118 LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgn 197
Cdd:cd17302  213 FRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH------------------------------------------- 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 198 llsfprFFGPGEFDPSVDVyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFNE 277
Cdd:cd17302  250 ------FRAGDSTGEPYDV-------------VLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRRFRD 309


                 ....*
gi 767996107 278 FMSNI 282
Cdd:cd17302  310 FIRKV 314
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 46-154 3.10e-27

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 beta (PIP5K1beta) and similar proteins; PIP5K1beta (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase 1 beta, or protein STM-7, or PIP5K1B, is encoded by the Friedreich's ataxia (FRDA) gene, STM7. FRDA is a progressive neurodegenerative disease characterized by ataxia, variously associating heart disease, diabetes mellitus, and/or glucose intolerance. PIP5K1beta is an enzyme functionally linked to actin cytoskeleton dynamics and it phosphorylates phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2).


Pssm-ID: 340444  Cd Length: 321  Bit Score: 107.77  E-value: 3.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  46 TLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQK-LHVGEES 124
Cdd:cd17307  139 TLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDgLYFDPET 218

                         90       100       110
                 ....*....|....*....|....*....|
gi 767996107 125 KKNFLEKLKRDVEFLAQLKIMDYSLLVGIH 154
Cdd:cd17307  219 YNALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 46-283 1.57e-25

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1gamma) and similar proteins; PIP5K1gamma(EC 2.7.1.68), also known as PtdIns(4)P-5-kinase 1 gamma, or PIP5K1gamma, or PIPKIgamma, or PtdInsPKI gamma, is a phosphatidylinositol-4-phosphate 5-kinase that catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), which is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. PIP5K1gamma is required for epidermal growth factor (EGF)-stimulated directional cell migration. It also modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin.


Pssm-ID: 340445  Cd Length: 323  Bit Score: 103.15  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  46 TLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEES 124
Cdd:cd17308  140 TLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADT 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 125 KKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgNLLSFPRF 204
Cdd:cd17308  220 FSALVKTLQRDCLVLESFKIMDYSLLLGVH------------------------------------------NIGGIPAV 257

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996107 205 FGPGEfdpsvdvyamkshesspkKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 283
Cdd:cd17308  258 NGKGE------------------RLLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSNTV 317
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 46-157 8.00e-24

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1alpha) and similar proteins; PIP5K1alpha (EC 2.7.1.68), also termed PIP5K1A, or PtdIns(4)P-5-kinase 1 alpha, or 68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha, or PIPKI-alpha, catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). It mediates extracellular calcium-induced keratinocyte differentiation. Unlike other type I phosphatidylinositol-4-phosphate 5-kinase (PIPKI) isoforms, PIP5K1alpha regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation. This function is independent of its catalytic activity, and requires physical interaction of PIP5K1alpha with the Rac1 polybasic domain. The family also includes testis-specific PIP5K1A and PSMD4-like protein, also known as PIP5K1A-PSMD4 or PIPSL. It has negligeable PIP5 kinase activity and binds to ubiquitinated proteins.


Pssm-ID: 340443  Cd Length: 339  Bit Score: 98.53  E-value: 8.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  46 TLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEES 124
Cdd:cd17306  142 TLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDM 221

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767996107 125 KKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 157
Cdd:cd17306  222 YNALCKTLQRDCLVLQSFKIMDYSLLVGIHNID 254
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
43-155 1.36e-23

Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 100.02  E-value: 1.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  43 HGNTLLPQFLGMYRL-------TVDGVETYMVVTRNVFSHRLtVHRKYDLKGSTVAREASDKEKAKD-LPTFKDNDFLNE 114
Cdd:COG5253  415 NPLTLLCKIFGFYRVksrssisSSKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWIRE 493

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767996107 115 GQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHD 155
Cdd:COG5253  494 SPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD 533
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 41-281 1.19e-19

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PIP5KL1) and similar proteins; PIP5KL1 (EC 2.7.1.68), also known as PI(4)P 5-kinase-like protein 1, or PtdIns(4)P-5-kinase-like protein 1, may act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment, and conversion to PI(3,4,5)P3.


Pssm-ID: 340441  Cd Length: 319  Bit Score: 86.64  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  41 ECHGNTLLPQFLGMYRLTVDG-VETYMVVTRNVFSHRLTVHRKYDLKGSTVAR-EASDKEKAKDLPTFKDNDFlnEGQKL 118
Cdd:cd17304  129 ENYPHSLLVKFLGVHSIKLPGkKKKYFIVMQSVFYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 119 HVGEEsKKNFLEKLKRDVEFLAQLKIMDYSLLVGI----HDVDRaeqeemeveeraedeecendgvggNLLcsygtpPDS 194
Cdd:cd17304  207 NLGQQ-RSWFLRQVEIDTEFLKGLNVLDYSLLVGFqplhSDENR------------------------RLL------PNY 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 195 PGNLlsfprffgpgefdpsvdvyamksHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKR 274
Cdd:cd17304  256 KNAL-----------------------HVVDGPEYRYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARR 311


                 ....*..
gi 767996107 275 FNEFMSN 281
Cdd:cd17304  312 FCQWVED 318
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
 46-153 1.64e-18

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in 1-phosphatidylinositol-3-phosphate 5-kinase and similar proteins; 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is also called FYVE finger-containing phosphoinositide kinase, PIKfyve, phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase). It forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] by catalyzing the phosphorylation of phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) on the fifth hydroxyl of the myo-inositol ring. Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. PIKfyve is vital in early embryonic development. It forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, playing a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human Ether-a-go-go-Related Gene (hERG) channels. This family also includes the yeast ortholog of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal catalytic lipid kinase domain related to PtdInsP kinases (or the PIPKc domain).


Pssm-ID: 340437  Cd Length: 262  Bit Score: 82.56  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  46 TLLPQFLGMYRLTVDGVET------YMVVTRNVFsHRLTVHRKYDLKGSTVAREASDKEKakDLPTFKDNDFLNE--GQK 117
Cdd:cd17300   90 SLLAKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAED--EDSVLLDENFLEYtkGSP 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767996107 118 LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 153
Cdd:cd17300  167 LYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 40-282 1.46e-17

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 82.57  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107  40 VECHGNTLLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDfLNegQKL 118
Cdd:PLN03185 483 VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLD-LN--YSF 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 119 HVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG----------------- 181
Cdd:PLN03185 559 YLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvvaeedtiedeelsype 634

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996107 182 GNLLCSYGTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE-------------VYF 232
Cdd:PLN03185 635 GLVLVPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREdkekqsfhevydvVLY 714

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767996107 233 MAIIDILTPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 282
Cdd:PLN03185 715 LGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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