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Conserved domains on  [gi|1052292374|ref|NP_001316991|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 alpha isoform 2 [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 ...
 1-344 0e+00

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: 531.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   1 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYD 80
Cdd:cd17309    34 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAR 160
Cdd:cd17309   114 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAR 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 161 EASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendge 240
Cdd:cd17309   194 EASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV---------------- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 241 eegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKH 320
Cdd:cd17309   258 ----------------------------------------------------VYFMAIIDILTHYDAKKKAAHAAKTVKH 285

                         330       340
                  ....*....|....*....|....
gi 1052292374 321 GAGAEISTVNPEQYSKRFLDFIGH 344
Cdd:cd17309   286 GAGAEISTVNPEQYSKRFLDFITS 309
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-344 0e+00

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: 531.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   1 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYD 80
Cdd:cd17309    34 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAR 160
Cdd:cd17309   114 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAR 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 161 EASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendge 240
Cdd:cd17309   194 EASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV---------------- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 241 eegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKH 320
Cdd:cd17309   258 ----------------------------------------------------VYFMAIIDILTHYDAKKKAAHAAKTVKH 285

                         330       340
                  ....*....|....*....|....
gi 1052292374 321 GAGAEISTVNPEQYSKRFLDFIGH 344
Cdd:cd17309   286 GAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
3-346 2.01e-132

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 381.34  E-value: 2.01e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374    3 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTS 78
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   79 YDKRYIIKTITSEDVAEMHNILKKYHQYIVECHgITLLPQFLGMYRLNVDG---VEIYVIVTRNVFSHRLSVYRKYDLKG 155
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  156 STVAREAsDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVEC 234
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  235 EENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPnIDVYGIKCHEnsprkEVYFMAIIDILTHYDAKKKAAHA 314
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHW 311

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1052292374  315 AKTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 346
Cdd:smart00330 312 VKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 67-345 3.17e-73

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: 226.19  E-value: 3.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  67 SQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLS 146
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 147 VYRKYDLKGSTVAREASDKEKAKELPT-LKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVe 225
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDL- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 226 raeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikcheNSPRKEVYFMAIIDILTHY 305
Cdd:pfam01504 170 -------------------------------------------------------------DEDGKEIYYLGIIDILTEY 188

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1052292374 306 DAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIGHI 345
Cdd:pfam01504 189 NLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 26-342 6.80e-42

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 155.38  E-value: 6.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  26 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYIIKTITSEDVAEMHNIL 100
Cdd:PLN03185  397 PSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRElSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRML 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 101 KKYHQYiVECHGITLLPQFLGMYRLN-VDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAsDKEKAKELPTLKDNDF 179
Cdd:PLN03185  477 PDYHHH-VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLDL 554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 180 INEgqkIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEENDGEEEGESDGTH- 249
Cdd:PLN03185  555 NYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVVAEEDTIEDEELs 631

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 250 --------PVGTPPDS--PGNTLNSSPPLAPGEFDPNID-----------------------VYGIKCHENSPRKEVY-- 294
Cdd:PLN03185  632 ypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgvnmparaerIPGREDKEKQSFHEVYdv 711

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052292374 295 --FMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 342
Cdd:PLN03185  712 vlYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
14-225 4.49e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 137.77  E-value: 4.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  14 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDdQDFQNSLTRSApLPNDSQARSGARFHTSYDKRYIIKTITS 90
Cdd:COG5253   320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-EALVSLLSRYI-LWESNGGKSGSFFLFTRDYKFIIKTISH 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  91 edvAEMHNILKKYHQYIVEC--HGITLLPQFLGMYRLNV-------DGVEIYVIVTRNVFSHRLsVYRKYDLKGSTVARE 161
Cdd:COG5253   396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVKSrssisssKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRH 471

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052292374 162 ASDKEKAKE-LPTLKDNDFINEGQKIyIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 225
Cdd:COG5253   472 VERTGKSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-344 0e+00

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: 531.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   1 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYD 80
Cdd:cd17309    34 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAR 160
Cdd:cd17309   114 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAR 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 161 EASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendge 240
Cdd:cd17309   194 EASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV---------------- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 241 eegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKH 320
Cdd:cd17309   258 ----------------------------------------------------VYFMAIIDILTHYDAKKKAAHAAKTVKH 285

                         330       340
                  ....*....|....*....|....
gi 1052292374 321 GAGAEISTVNPEQYSKRFLDFIGH 344
Cdd:cd17309   286 GAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
 1-344 0e+00

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: 509.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   1 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYD 80
Cdd:cd17305    25 MLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNSLTRSQPLASDSPGRSGSRFLVSYD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAR 160
Cdd:cd17305   105 KKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVVMRNVFSPRLPIHKKYDLKGSTVDR 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 161 EASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendge 240
Cdd:cd17305   185 QASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDC---------------- 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 241 eegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKH 320
Cdd:cd17305   249 ----------------------------------------------------IYFMAIIDILTHYGAKKRAAHAAKTVKH 276

                         330       340
                  ....*....|....*....|....
gi 1052292374 321 GAGAEISTVNPEQYSKRFLDFIGH 344
Cdd:cd17305   277 GAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-342 7.83e-176

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: 490.33  E-value: 7.83e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   1 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYD 80
Cdd:cd17310    36 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAR 160
Cdd:cd17310   116 RRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSR 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 161 EASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendge 240
Cdd:cd17310   196 EASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---------------- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 241 eegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKH 320
Cdd:cd17310   260 ----------------------------------------------------VYFMAIIDILTPYDAKKKAAHAAKTVKH 287

                         330       340
                  ....*....|....*....|..
gi 1052292374 321 GAGAEISTVNPEQYSKRFLDFI 342
Cdd:cd17310   288 GAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-342 3.63e-142

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: 404.25  E-value: 3.63e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   1 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQarSGARFHTSYD 80
Cdd:cd17311    25 MLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSPPYSESEG--SDGRFLLSYD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAR 160
Cdd:cd17311   103 RTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 161 EASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendge 240
Cdd:cd17311   183 EASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV---------------- 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 241 eegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKH 320
Cdd:cd17311   247 ----------------------------------------------------VYFMGLIDILTQYDAKKKAAHAAKTVKH 274

                         330       340
                  ....*....|....*....|..
gi 1052292374 321 GAGAEISTVNPEQYSKRFLDFI 342
Cdd:cd17311   275 GAGAEISTVHPEQYAKRFLDFI 296
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
3-346 2.01e-132

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 381.34  E-value: 2.01e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374    3 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTS 78
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   79 YDKRYIIKTITSEDVAEMHNILKKYHQYIVECHgITLLPQFLGMYRLNVDG---VEIYVIVTRNVFSHRLSVYRKYDLKG 155
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  156 STVAREAsDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVEC 234
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  235 EENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPnIDVYGIKCHEnsprkEVYFMAIIDILTHYDAKKKAAHA 314
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHW 311

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1052292374  315 AKTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 346
Cdd:smart00330 312 VKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 28-342 9.85e-85

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: 256.73  E-value: 9.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  28 HFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPND--SQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQ 105
Cdd:cd00139     2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 106 YIVECHGiTLLPQFLGMYRLNV-DGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAS-DKEKAKELPTLKDNDFINEG 183
Cdd:cd00139    82 HIKKNPN-SLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 184 QKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntln 263
Cdd:cd00139   161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052292374 264 sspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 342
Cdd:cd00139   202 -----------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERFLKFM 251
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 67-345 3.17e-73

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: 226.19  E-value: 3.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  67 SQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLS 146
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 147 VYRKYDLKGSTVAREASDKEKAKELPT-LKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVe 225
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDL- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 226 raeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikcheNSPRKEVYFMAIIDILTHY 305
Cdd:pfam01504 170 -------------------------------------------------------------DEDGKEIYYLGIIDILTEY 188

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1052292374 306 DAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIGHI 345
Cdd:pfam01504 189 NLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
 2-343 5.77e-71

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: 223.71  E-value: 5.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   2 LMPDDFKAYSKIKVDnHLFNKENMPSH--FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTS 78
Cdd:cd17303    26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKYILSElGSPGKSGSFFYFS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  79 YDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGITLLPQFLGMYRLNV-DGVEIYVIVTRNVFSHRLSVYRKYDLKGST 157
Cdd:cd17303   105 RDYRFIIKTIHHSEHKFLRKILPDYYNHVKE-NPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGST 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 158 VAREAS-DKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVEraeqeevecee 236
Cdd:cd17303   184 VGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD----------- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 237 ndgeeegesDGTHPVGTppdspgntlnsspplapgefdpnidvygikchENSPRKEVYFMAIIDILTHYDAKKKAAHAAK 316
Cdd:cd17303   253 ---------GGFQATDE--------------------------------NNEPGDEIYYLGIIDILTPYNAKKKLEHFFK 291

                         330       340
                  ....*....|....*....|....*..
gi 1052292374 317 TVKHgAGAEISTVNPEQYSKRFLDFIG 343
Cdd:cd17303   292 SLRH-DRHTISAVPPKEYARRFLKFIE 317
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
 24-345 2.05e-53

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: 178.25  E-value: 2.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  24 NMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYIIKTITSEDVAEMHN 98
Cdd:cd17302    48 TPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLR 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  99 ILKKYHQYiVECHGITLLPQFLGMYRLN-VDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAS-DKEKAKELPTLKD 176
Cdd:cd17302   128 MLPAYYKH-VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNTTLKD 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 177 NDFineGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDveraeqeeveceendgeeegesdgthpvgTPPD 256
Cdd:cd17302   207 LDL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVHF-----------------------------RAGD 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 257 SPGntlnsspplapgefdpnidvygikchenSPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSK 336
Cdd:cd17302   255 STG----------------------------EPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSR 305


                  ....*....
gi 1052292374 337 RFLDFIGHI 345
Cdd:cd17302   306 RFRDFIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
 2-343 4.07e-50

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: 169.73  E-value: 4.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   2 LMPDDFKayskiKVDNHLFNKE---NMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSaPLPNDSQ-ARSGA 73
Cdd:cd17301    26 VLMQDFE-----VVESVFFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNE-PLRELSNpGASGS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  74 RFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDL 153
Cdd:cd17301   100 LFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 154 KGSTVAREASDKEKAKELPTLKDNDFINEGQK-IYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDveraeqeev 232
Cdd:cd17301   179 KGSTYKRKASKKERQKKSPTLKDLDFMEDHPEgILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGVHN--------- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 233 eceendgeeegesdgthPVGTPpdspgnTLNSSpplapgefdpnidvyGIKChensprkeVYFMAIIDILTHYDAKKKAA 312
Cdd:cd17301   250 -----------------LGGIP------ARNSK---------------GERL--------LLFIGIIDILQSYRLKKKLE 283

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1052292374 313 HAAKTVKHGaGAEISTVNPEQYSKRFLDFIG 343
Cdd:cd17301   284 HTWKSVVHD-GDTVSVHRPSFYAERFQNFMA 313
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 26-342 6.80e-42

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 155.38  E-value: 6.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  26 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYIIKTITSEDVAEMHNIL 100
Cdd:PLN03185  397 PSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRElSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRML 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 101 KKYHQYiVECHGITLLPQFLGMYRLN-VDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAsDKEKAKELPTLKDNDF 179
Cdd:PLN03185  477 PDYHHH-VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLDL 554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 180 INEgqkIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEENDGEEEGESDGTH- 249
Cdd:PLN03185  555 NYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVVAEEDTIEDEELs 631

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 250 --------PVGTPPDS--PGNTLNSSPPLAPGEFDPNID-----------------------VYGIKCHENSPRKEVY-- 294
Cdd:PLN03185  632 ypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgvnmparaerIPGREDKEKQSFHEVYdv 711

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1052292374 295 --FMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 342
Cdd:PLN03185  712 vlYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 26-222 4.65e-41

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: 146.29  E-value: 4.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  26 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 101
Cdd:cd17307    48 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 102 KYHQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN 181
Cdd:cd17307   128 GYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQ 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1052292374 182 EGQK-IYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIH 222
Cdd:cd17307   207 DMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 26-224 2.12e-38

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: 139.36  E-value: 2.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  26 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 101
Cdd:cd17308    49 PAHhypdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 102 KYHQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN 181
Cdd:cd17308   129 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQ 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1052292374 182 E-GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDV 224
Cdd:cd17308   208 DmPEGLMLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHNI 251
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 26-225 1.01e-37

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: 137.82  E-value: 1.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  26 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 101
Cdd:cd17306    51 PAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 102 KYHQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN 181
Cdd:cd17306   131 GYYMNLNQ-NPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQ 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1052292374 182 E-GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 225
Cdd:cd17306   210 DiPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNID 254
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
14-225 4.49e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 137.77  E-value: 4.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  14 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDdQDFQNSLTRSApLPNDSQARSGARFHTSYDKRYIIKTITS 90
Cdd:COG5253   320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-EALVSLLSRYI-LWESNGGKSGSFFLFTRDYKFIIKTISH 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  91 edvAEMHNILKKYHQYIVEC--HGITLLPQFLGMYRLNV-------DGVEIYVIVTRNVFSHRLsVYRKYDLKGSTVARE 161
Cdd:COG5253   396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVKSrssisssKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRH 471

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052292374 162 ASDKEKAKE-LPTLKDNDFINEGQKIyIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 225
Cdd:COG5253   472 VERTGKSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 2-342 3.93e-35

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: 130.56  E-value: 3.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374   2 LMPDDFKAyskiKVDNHLFNKENmpshFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAP-LPNDSQARSGARFHTSYD 80
Cdd:cd17304    30 LSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyLQFISNSKSGQDFFLTND 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  81 KRYIIKTITSEDVAEMHNILKKYHQYIvECHGITLLPQFLGMYRLNVDG-VEIYVIVTRNVFSHRLSVYRKYDLKGSTVA 159
Cdd:cd17304   102 KRFFLKTQTKREAKFLLSILRKYVQHL-ENYPHSLLVKFLGVHSIKLPGkKKKYFIVMQSVFYPDERINERYDIKGCQVS 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 160 R-EASDKEKAKELPTLKDNDFinEGQKIYIDDNNkKVFLEKLKKDVEFLAQLKLMDYSLLVG---IHDVERAEQEevece 235
Cdd:cd17304   181 RyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQR-SWFLRQVEIDTEFLKGLNVLDYSLLVGfqpLHSDENRRLL----- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 236 endgeeegesdgthpvgtpPDSPgNTLNssppLAPGEfdpnidvygikchensprKEVYFMAIIDILTHYDAKKKAAHAA 315
Cdd:cd17304   253 -------------------PNYK-NALH----VVDGP------------------EYRYFVGIIDIFTVYGLRKRLEHLW 290

                         330       340
                  ....*....|....*....|....*..
gi 1052292374 316 KTVKHgAGAEISTVNPEQYSKRFLDFI 342
Cdd:cd17304   291 KSLRY-PGQSFSTVSPEKYARRFCQWV 316
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
 39-221 1.75e-31

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: 119.15  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374  39 FRNLRERFGIDDQDFQNSLTRSAPLpnDSQ-ARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECH---GIT 114
Cdd:cd17300    13 FHALRSLYCGGEDDFIRSLSRCVKW--DASgGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALfhkRPS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052292374 115 LLPQFLGMYRLNV------DGVEIYVIVTRNVFsHRLSVYRKYDLKGSTVAREASDKEKakELPTLKDNDFINE--GQKI 186
Cdd:cd17300    91 LLAKILGVYRISVknsttnKTSKQDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAED--EDSVLLDENFLEYtkGSPL 167

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1052292374 187 YIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGI 221
Cdd:cd17300   168 YLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 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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