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Conserved domains on  [gi|568912237|ref|XP_006497457|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 alpha isoform X1 [Mus musculus]

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 ...
27-354 9.59e-179

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 cd17309:

Pssm-ID: 475131  Cd Length: 309  Bit Score: 497.96  E-value: 9.59e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ---------------------- 164
Cdd:cd17309   81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQyivechgntllpqflgmyrltv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 ---------------------------GSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFL 217
Cdd:cd17309  161 dgvetymivtrnvfshrlsvyrkydlkGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 218 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchen 297
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568912237 298 aprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 354
Cdd:cd17309  258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-354 9.59e-179

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: 497.96  E-value: 9.59e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ---------------------- 164
Cdd:cd17309   81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQyivechgntllpqflgmyrltv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 ---------------------------GSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFL 217
Cdd:cd17309  161 dgvetymivtrnvfshrlsvyrkydlkGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 218 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchen 297
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568912237 298 aprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 354
Cdd:cd17309  258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
62-356 1.27e-99

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 298.14  E-value: 1.27e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237    62 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTS 137
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   138 YDKRYVIKTITSEDVAEMHNILKKYHQ---------------------------------------------------GS 166
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEhivqnpntllpkffglyrvkvkggtekkiyflvmenlfysdlkvhrkydlkGS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   167 TVAREAsDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECE 245
Cdd:smart00330 160 TRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   246 ENDGEEEGESDSTHPIGTPPDSPGNTLNSSPPLAPGEFDPnIDVYAIKCHEnaprkEVYFMAIIDILTHYDAKKKAAHAA 325
Cdd:smart00330 239 PVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHWV 312
                          330       340       350
                   ....*....|....*....|....*....|.
gi 568912237   326 KTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 356
Cdd:smart00330 313 KSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
126-355 4.38e-45

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: 154.16  E-value: 4.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  126 SQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ----------------------------------------- 164
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEhvkqnpntllprfyglhrvkpggkkiyfvvmnnlfptdldi 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  165 -------GSTVAREASDKEKAKELPT-LKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVER 236
Cdd:pfam01504  92 herydlkGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLDE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  237 aeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaPRKEVYFMAIIDILTHYD 316
Cdd:pfam01504 172 --------------------------------------------------------------DGKEIYYLGIIDILTEYN 189
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568912237  317 AKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIGHI 355
Cdd:pfam01504 190 LKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1-352 3.72e-26

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 109.92  E-value: 3.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   1 MATPGNLGSSVLASKTKTKKKHFVAQK-----VKLFRASDPLLSvLMWGVNHSINELSHVQiPVMLMPDDFKAYSKIKVD 75
Cdd:PLN03185 310 LVLNNSFSSTSRRAKRRQKKLVKEIKRpgetiIKGHRSYDLMLS-LQLGIRYTVGKITPIQ-RREVRPSDFGPRASFWMN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  76 nhlFNKEN---MPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYVIKTI 147
Cdd:PLN03185 388 ---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRElSSPGKSGSVFFLSQDDRFMIKTL 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 148 TSEDVAEMHNILKKYH-------------------------------------------------QGSTVAREAsDKEKA 178
Cdd:PLN03185 465 RKSEVKVLLRMLPDYHhhvktyentlitkffglhrikpssgqkfrfvvmgnmfctelrihrrfdlKGSSLGRSA-DKVEI 543
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 179 KELPTLKDNDFINEgqkIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEENDG 249
Cdd:PLN03185 544 DENTTLKDLDLNYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVVA 620
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 250 EEEGESDSTH---------PIGTPPDS--PGNTLNSSPPLAPGEFDPNIDV-------YAIKCHENAP-RKE-------- 302
Cdd:PLN03185 621 EEDTIEDEELsypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDLllpgtarLQIQLGVNMPaRAEripgredk 700
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912237 303 -----------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 352
Cdd:PLN03185 701 ekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
73-235 9.13e-19

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 87.31  E-value: 9.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  73 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDdQDFQNSLTRSApLPNDSQARSGARFHTSYDKRYVIKTIT- 148
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-EALVSLLSRYI-LWESNGGKSGSFFLFTRDYKFIIKTISh 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 149 ----------------------------------------------SEDVAEMHNIL--KKYHQ-----GSTVAREASDK 175
Cdd:COG5253  396 sehicfrpmifeyyvhvlfnpltllckifgfyrvksrssisssksrKIYFIVMENLFypHGIHRifdlkGSMRNRHVERT 475
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912237 176 EKAKE-LPTLKDNDFINEGQKIyIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 235
Cdd:COG5253  476 GKSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-354 9.59e-179

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: 497.96  E-value: 9.59e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ---------------------- 164
Cdd:cd17309   81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQyivechgntllpqflgmyrltv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 ---------------------------GSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFL 217
Cdd:cd17309  161 dgvetymivtrnvfshrlsvyrkydlkGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 218 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchen 297
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568912237 298 aprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 354
Cdd:cd17309  258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
36-354 3.13e-160

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: 450.57  E-value: 3.13e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNS 115
Cdd:cd17305    1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 116 LTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ------------------------------- 164
Cdd:cd17305   81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQyiverhgktllpqylgmyritvngvetylvv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 ------------------GSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYS 226
Cdd:cd17305  161 mrnvfsprlpihkkydlkGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 227 LLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaprkeVYFM 306
Cdd:cd17305  241 LLVGIHDC--------------------------------------------------------------------IYFM 252
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 568912237 307 AIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 354
Cdd:cd17305  253 AIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
25-352 3.74e-156

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: 440.64  E-value: 3.74e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  25 AQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRER 104
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 105 FGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ-------------------- 164
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQfivechgntllpqflgmyrl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 -----------------------------GSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVE 215
Cdd:cd17310  161 tvdgvetymvvtrnvfshrltvhrkydlkGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 216 FLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikch 295
Cdd:cd17310  241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568912237 296 enaprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 352
Cdd:cd17310  260 -------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
36-352 1.99e-117

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: 341.85  E-value: 1.99e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNS 115
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 116 LTRSAPLPNDSQarSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ------------------------------- 164
Cdd:cd17311   81 LTRSPPYSESEG--SDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQyivkchgntllpqflgmyrlsvdnedsymlv 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 ------------------GSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYS 226
Cdd:cd17311  159 mrnmfshrlpvhrkydlkGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 227 LLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaprkeVYFM 306
Cdd:cd17311  239 LLLGIHDV--------------------------------------------------------------------VYFM 250
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 568912237 307 AIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 352
Cdd:cd17311  251 GLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFI 296
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
62-356 1.27e-99

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 298.14  E-value: 1.27e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237    62 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTS 137
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   138 YDKRYVIKTITSEDVAEMHNILKKYHQ---------------------------------------------------GS 166
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEhivqnpntllpkffglyrvkvkggtekkiyflvmenlfysdlkvhrkydlkGS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   167 TVAREAsDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECE 245
Cdd:smart00330 160 TRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   246 ENDGEEEGESDSTHPIGTPPDSPGNTLNSSPPLAPGEFDPnIDVYAIKCHEnaprkEVYFMAIIDILTHYDAKKKAAHAA 325
Cdd:smart00330 239 PVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHWV 312
                          330       340       350
                   ....*....|....*....|....*....|.
gi 568912237   326 KTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 356
Cdd:smart00330 313 KSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
87-352 1.14e-57

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: 187.39  E-value: 1.14e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  87 HFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPND--SQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ 164
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 -------------------------------------------------GSTVAREAS-DKEKAKELPTLKDNDFINEGQ 194
Cdd:cd00139   82 hikknpnslltrfyglysiklqkgkkvyfvvmenvfptdlkiherydlkGSTVGRRVSkEKEKKKGLKVLKDLDFLEKGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 195 KIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlns 274
Cdd:cd00139  162 KIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL---------------------------------------- 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912237 275 spplapgefdpnidvyaikchenaprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 352
Cdd:cd00139  202 ----------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERFLKFM 251
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
61-353 1.87e-50

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: 170.94  E-value: 1.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  61 LMPDDFKAYSKIKVDnHLFNKENMPSH--FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTS 137
Cdd:cd17303   26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKYILSElGSPGKSGSFFYFS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 138 YDKRYVIKTITSEDVAEMHNILKKYHQ-------------------------------------------------GSTV 168
Cdd:cd17303  105 RDYRFIIKTIHHSEHKFLRKILPDYYNhvkenpntllsqfyglhrvkmprgrkihfvvmnnlfpphrdihqtfdlkGSTV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 169 AREAS-DKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVEraeqeeveceen 247
Cdd:cd17303  185 GRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD------------ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 248 dgeeegesdsthpigtppdspgntlnsspplapGEFDPnIDVyaikchENAPRKEVYFMAIIDILTHYDAKKKAAHAAKT 327
Cdd:cd17303  253 ---------------------------------GGFQA-TDE------NNEPGDEIYYLGIIDILTPYNAKKKLEHFFKS 292
                        330       340
                 ....*....|....*....|....*.
gi 568912237 328 VKHgAGAEISTVNPEQYSKRFLDFIG 353
Cdd:cd17303  293 LRH-DRHTISAVPPKEYARRFLKFIE 317
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
126-355 4.38e-45

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: 154.16  E-value: 4.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  126 SQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ----------------------------------------- 164
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEhvkqnpntllprfyglhrvkpggkkiyfvvmnnlfptdldi 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  165 -------GSTVAREASDKEKAKELPT-LKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVER 236
Cdd:pfam01504  92 herydlkGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLDE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  237 aeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaPRKEVYFMAIIDILTHYD 316
Cdd:pfam01504 172 --------------------------------------------------------------DGKEIYYLGIIDILTEYN 189
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568912237  317 AKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIGHI 355
Cdd:pfam01504 190 LKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
83-355 2.34e-33

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: 125.87  E-value: 2.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  83 NMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYVIKTITSEDVAEMHN 157
Cdd:cd17302   48 TPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLR 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 158 ILKKYH-------------------------------------------------QGSTVAREAS-DKEKAKELPTLKDN 187
Cdd:cd17302  128 MLPAYYkhvkayentlltkffgvhrvkpvggrkvrfvvmgnlfctelrihrrfdlKGSTHGRTTGkPESEIDPNTTLKDL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 188 DFineGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDveraeqeeveceendgeeegesdsthpigTPPDS 267
Cdd:cd17302  208 DL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVHF-----------------------------RAGDS 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 268 PGntlnsspplapgefdpnidvyaikchenAPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSKR 347
Cdd:cd17302  256 TG----------------------------EPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRR 306

                 ....*...
gi 568912237 348 FLDFIGHI 355
Cdd:cd17302  307 FRDFIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
35-353 6.96e-32

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: 121.97  E-value: 6.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  35 DPLLSVLMWGVNHSINELSHVQIPVMLMpDDFKayskiKVDNHLFNKE---NMPSH----FKFKEYCPMVFRNLRERFGI 107
Cdd:cd17301    1 SELMGAIQLGIGHSVGSLSSKPERDVLM-QDFE-----VVESVFFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 108 DDQDFQNSLTRSaPLPNDSQ-ARSGARFHTSYDKRYVIKTITSEDvAE-------------------------------- 154
Cdd:cd17301   75 KPDDYLLSLCNE-PLRELSNpGASGSLFYLTHDDEFIIKTVQHKE-AEflqkllpgyymnlnqnprtllpkfyglycyqs 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 155 ---------MHNILK---KYHQ-----GSTVAREASDKEKAKELPTLKDNDFINEGQK-IYIDDNNKKIFLEKLKKDVEF 216
Cdd:cd17301  153 ggknirfvvMNNLLPsniKMHEkydlkGSTYKRKASKKERQKKSPTLKDLDFMEDHPEgILLEPDTYDALLKTIQRDCRV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 217 LAQLKLMDYSLLVGIHDveraeqeeveceendgeeegesdsthPIGTPpdspgnTLNSSpplapGEfdpnidvyaikche 296
Cdd:cd17301  233 LESFKIMDYSLLLGVHN--------------------------LGGIP------ARNSK-----GE-------------- 261
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568912237 297 naprKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIG 353
Cdd:cd17301  262 ----RLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMA 313
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1-352 3.72e-26

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 109.92  E-value: 3.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237   1 MATPGNLGSSVLASKTKTKKKHFVAQK-----VKLFRASDPLLSvLMWGVNHSINELSHVQiPVMLMPDDFKAYSKIKVD 75
Cdd:PLN03185 310 LVLNNSFSSTSRRAKRRQKKLVKEIKRpgetiIKGHRSYDLMLS-LQLGIRYTVGKITPIQ-RREVRPSDFGPRASFWMN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  76 nhlFNKEN---MPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYVIKTI 147
Cdd:PLN03185 388 ---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRElSSPGKSGSVFFLSQDDRFMIKTL 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 148 TSEDVAEMHNILKKYH-------------------------------------------------QGSTVAREAsDKEKA 178
Cdd:PLN03185 465 RKSEVKVLLRMLPDYHhhvktyentlitkffglhrikpssgqkfrfvvmgnmfctelrihrrfdlKGSSLGRSA-DKVEI 543
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 179 KELPTLKDNDFINEgqkIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEENDG 249
Cdd:PLN03185 544 DENTTLKDLDLNYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVVA 620
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 250 EEEGESDSTH---------PIGTPPDS--PGNTLNSSPPLAPGEFDPNIDV-------YAIKCHENAP-RKE-------- 302
Cdd:PLN03185 621 EEDTIEDEELsypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDLllpgtarLQIQLGVNMPaRAEripgredk 700
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912237 303 -----------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 352
Cdd:PLN03185 701 ekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
36-352 6.01e-22

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: 94.73  E-value: 6.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAyskiKVDNHLFNKENmpshFKFKEYCPMVFRNLRERFGIDDQDFQNS 115
Cdd:cd17304    5 SLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 116 LTRSAP-LPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ------------------------------ 164
Cdd:cd17304   77 LSPDEPyLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQhlenyphsllvkflgvhsiklpgkkkkyfi 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 165 -------------------GSTVAR-EASDKEKAKELPTLKDNDFinEGQKIYIDDNNkKIFLEKLKKDVEFLAQLKLMD 224
Cdd:cd17304  157 vmqsvfypderinerydikGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQR-SWFLRQVEIDTEFLKGLNVLD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 225 YSLLVG---IHDVERAEQEeveceendgeeegesdsthpigtpPDSPgNTLNssppLAPGEfdpnidvyaikchenaprK 301
Cdd:cd17304  234 YSLLVGfqpLHSDENRRLL------------------------PNYK-NALH----VVDGP------------------E 266
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568912237 302 EVYFMAIIDILTHYDAKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFLDFI 352
Cdd:cd17304  267 YRYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWV 316
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
85-232 9.38e-22

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: 94.29  E-value: 9.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  85 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILK 160
Cdd:cd17307   48 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLP 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 161 KYH------------------------------------------------QGSTVAREASDKEKAKELPTLKDNDFINE 192
Cdd:cd17307  128 GYYmnlnqnprtllpkfyglycmqsgginirivvmnnvlprsvkmhykydlKGSTYKRRASRKEREKSCPTYKDLDFLQD 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568912237 193 GQK-IYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIH 232
Cdd:cd17307  208 MHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
34-235 1.01e-21

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: 94.29  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  34 SDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFG 106
Cdd:cd17306    3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhyndFRFKTYAPVAFRYFRELFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYH----------------------- 163
Cdd:cd17306   77 IRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYmnlnqnprtllpkfyglycvqag 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 164 -------------------------QGSTVAREASDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEFL 217
Cdd:cd17306  157 gknirivvmnnllprsvkmhlkydlKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLVL 236
                        250
                 ....*....|....*...
gi 568912237 218 AQLKLMDYSLLVGIHDVE 235
Cdd:cd17306  237 QSFKIMDYSLLVGIHNID 254
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
34-234 1.17e-21

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: 93.90  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  34 SDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFG 106
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhypdFRFKTYAPVAFRYFRELFG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSED----------------------------------- 151
Cdd:cd17308   75 IRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEaeflqkllpgyymnlnqnprtllpkfyglycvqsg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 152 -----VAEMHNILK---KYH-----QGSTVAREASDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEFL 217
Cdd:cd17308  155 gknirVVVMNNILPrvvKMHlkfdlKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVL 234
                        250
                 ....*....|....*..
gi 568912237 218 AQLKLMDYSLLVGIHDV 234
Cdd:cd17308  235 ESFKIMDYSLLLGVHNI 251
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
73-235 9.13e-19

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 87.31  E-value: 9.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  73 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDdQDFQNSLTRSApLPNDSQARSGARFHTSYDKRYVIKTIT- 148
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-EALVSLLSRYI-LWESNGGKSGSFFLFTRDYKFIIKTISh 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 149 ----------------------------------------------SEDVAEMHNIL--KKYHQ-----GSTVAREASDK 175
Cdd:COG5253  396 sehicfrpmifeyyvhvlfnpltllckifgfyrvksrssisssksrKIYFIVMENLFypHGIHRifdlkGSMRNRHVERT 475
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912237 176 EKAKE-LPTLKDNDFINEGQKIyIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 235
Cdd:COG5253  476 GKSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
98-231 3.18e-14

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: 71.77  E-value: 3.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237  98 FRNLRERFGIDDQDFQNSLTRSAPLpnDSQ-ARSGARFHTSYDKRYVIKTITS--------------------------- 149
Cdd:cd17300   13 FHALRSLYCGGEDDFIRSLSRCVKW--DASgGKSGASFFKTLDDRFILKQISKaelqsfldfapayfeymakalfhkrps 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912237 150 -----------------------EDVAEMHNIL--KKYHQ-----GSTVAREASDKEKakELPTLKDNDFINE--GQKIY 197
Cdd:cd17300   91 llakilgvyrisvknsttnktskQDLLVMENLFygRNISQvydlkGSLRNRYVNVAED--EDSVLLDENFLEYtkGSPLY 168
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568912237 198 IDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGI 231
Cdd:cd17300  169 LREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
 
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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