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Conserved domains on  [gi|1788935069|ref|XP_031796947|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 gamma isoform X2 [Sarcophilus harrisii]

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 ...
 1-349 1.48e-178

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 cd17311:

Pssm-ID: 475131  Cd Length: 298  Bit Score: 496.70  E-value: 1.48e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   1 MLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP-SESEGSDGRFLVSYDRT 79
Cdd:cd17311    25 MLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSPPySESEGSDGRFLLSYDRT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  80 LVIKEVSSEDIADMHSNLSNYHQYIVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREA 159
Cdd:cd17311   105 LVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 160 SDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeeeqe 239
Cdd:cd17311   185 SDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV------------------ 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 240 gegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAAHA 319
Cdd:cd17311   247 ----------------------------------------------------------VYFMGLIDILTQYDAKKKAAHA 268

                         330       340       350
                  ....*....|....*....|....*....|
gi 1788935069 320 AKTVKHGAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17311   269 AKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
 
Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-349 1.48e-178

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: 496.70  E-value: 1.48e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   1 MLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP-SESEGSDGRFLVSYDRT 79
Cdd:cd17311    25 MLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSPPySESEGSDGRFLLSYDRT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  80 LVIKEVSSEDIADMHSNLSNYHQYIVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREA 159
Cdd:cd17311   105 LVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 160 SDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeeeqe 239
Cdd:cd17311   185 SDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV------------------ 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 240 gegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAAHA 319
Cdd:cd17311   247 ----------------------------------------------------------VYFMGLIDILTQYDAKKKAAHA 268

                         330       340       350
                  ....*....|....*....|....*....|
gi 1788935069 320 AKTVKHGAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17311   269 AKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
3-351 1.10e-133

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 384.81  E-value: 1.10e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069    3 LPDDFKASSKIKVNNHLfHRENLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSE---SEGSDGRFLVS 75
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLElssGGKSGSFFYLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   76 YDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHgSTLLPQFLGMYRVSVDNE---DSYMLVMRNMFSHRLPVHRKYDLKG 152
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  153 SLVSREAsDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIVRGTESEEEG 231
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  232 PGKEEEQEGEGDCGMAGPPglvgscgtSPEGIGGYIHAHRPLGPGEFESfIDVYAIRSAEgapqkEVYFMGLIDILTQYD 311
Cdd:smart00330 238 PPVYGSDESPSSESSNGGK--------APDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYT 303

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1788935069  312 AKKKAAHAAKTVKHGaGAEISTVHPDQYAKRFLDFITNIF 351
Cdd:smart00330 304 WDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 56-350 7.93e-66

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: 207.32  E-value: 7.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  56 SLTRSPPSE--SEG-SDGRFLVSYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGSTLLPQFLGMYRVSVDNEDSYML 132
Cdd:pfam01504   1 LTGKSILSElsSPGkSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 133 VMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMD 211
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 212 YSLLLGIHDIVRgteseeegpgkeeeqegegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsae 291
Cdd:pfam01504 160 YSLLLGIHDLDE-------------------------------------------------------------------- 171

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1788935069 292 gaPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPDQYAKRFLDFITNI 350
Cdd:pfam01504 172 --DGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 4-351 6.60e-40

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 149.60  E-value: 6.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   4 PDDFKASSKIKVNnhlFHREN---LPSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSESEGSDGR----F 72
Cdd:PLN03185  375 PSDFGPRASFWMN---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKsgsvF 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  73 LVSYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGSTLLPQFLGMYRVSVDNEDSY-MLVMRNMFSHRLPVHRKYDLK 151
Cdd:PLN03185  452 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLK 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 152 GSLVSREAsDKEKVKELPTLKDMDFlnkNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIH---------DIV 222
Cdd:PLN03185  531 GSSLGRSA-DKVEIDENTTLKDLDL---NYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLP 606

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 223 RGTESEEEGPGKEEEQEGEGDCGMAGPPGLV--------GSCGTSPEGIGGYIHAHRP-------LGPGEFESFID--VY 285
Cdd:PLN03185  607 YSRSITADGLEVVAEEDTIEDEELSYPEGLVlvprgaddGSTVPGPHIRGSRLRASAAgdeevdlLLPGTARLQIQlgVN 686

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788935069 286 AIRSAEGAPQKE-------------VYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHPDQYAKRFLDFITNIF 351
Cdd:PLN03185  687 MPARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
22-221 1.38e-33

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 130.84  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  22 RENLPS---HFKFKEYCPQVFRNLRDRFGIDDQDYQvSLTRSPPSESEG--SDGRFLVSYDRTLVIKEVSSEDIADMHSN 96
Cdd:COG5253   326 NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALVS-LLSRYILWESNGgkSGSFFLFTRDYKFIIKTISHSEHICFRPM 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  97 LSNYHQYiVKCHGSTLLPQFLGMYRVSVDNEDS-------YMLVMRNMFSHRLPvHRKYDLKGSLVSREASDKEKVKE-L 168
Cdd:COG5253   405 IFEYYVH-VLFNPLTLLCKIFGFYRVKSRSSISssksrkiYFIVMENLFYPHGI-HRIFDLKGSMRNRHVERTGKSMSvL 482

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1788935069 169 PTLKDMDFLNKNQKVYIGEEeKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDI 221
Cdd:COG5253   483 LDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
 
Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-349 1.48e-178

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: 496.70  E-value: 1.48e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   1 MLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP-SESEGSDGRFLVSYDRT 79
Cdd:cd17311    25 MLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSPPySESEGSDGRFLLSYDRT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  80 LVIKEVSSEDIADMHSNLSNYHQYIVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREA 159
Cdd:cd17311   105 LVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 160 SDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeeeqe 239
Cdd:cd17311   185 SDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV------------------ 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 240 gegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAAHA 319
Cdd:cd17311   247 ----------------------------------------------------------VYFMGLIDILTQYDAKKKAAHA 268

                         330       340       350
                  ....*....|....*....|....*....|
gi 1788935069 320 AKTVKHGAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17311   269 AKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
 1-349 1.83e-166

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: 465.98  E-value: 1.83e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   1 MLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSESEG---SDGRFLVSYD 77
Cdd:cd17305    25 MLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNSLTRSQPLASDSpgrSGSRFLVSYD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  78 RTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSR 157
Cdd:cd17305   105 KKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVVMRNVFSPRLPIHKKYDLKGSTVDR 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 158 EASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeee 237
Cdd:cd17305   185 QASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDC---------------- 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 238 qegegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAA 317
Cdd:cd17305   249 ------------------------------------------------------------IYFMAIIDILTHYGAKKRAA 268

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1788935069 318 HAAKTVKHGAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17305   269 HAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-349 1.22e-149

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: 424.08  E-value: 1.22e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   1 MLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP--SESEGSDG-RFLVSYD 77
Cdd:cd17310    36 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPinSDSQGRCGtRFLTTYD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  78 RTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSR 157
Cdd:cd17310   116 RRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSR 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 158 EASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeee 237
Cdd:cd17310   196 EASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---------------- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 238 qegegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAA 317
Cdd:cd17310   260 ------------------------------------------------------------VYFMAIIDILTPYDAKKKAA 279

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1788935069 318 HAAKTVKHGAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17310   280 HAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-349 5.77e-142

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: 404.36  E-value: 5.77e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   1 MLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP--SESEGSDG-RFLVSYD 77
Cdd:cd17309    34 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPlaNDSQARSGaRFHTSYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  78 RTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSR 157
Cdd:cd17309   114 KRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAR 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 158 EASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeee 237
Cdd:cd17309   194 EASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV---------------- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 238 qegegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAA 317
Cdd:cd17309   258 ------------------------------------------------------------VYFMAIIDILTHYDAKKKAA 277

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1788935069 318 HAAKTVKHGAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17309   278 HAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
3-351 1.10e-133

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 384.81  E-value: 1.10e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069    3 LPDDFKASSKIKVNNHLfHRENLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSE---SEGSDGRFLVS 75
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLElssGGKSGSFFYLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   76 YDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHgSTLLPQFLGMYRVSVDNE---DSYMLVMRNMFSHRLPVHRKYDLKG 152
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  153 SLVSREAsDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIVRGTESEEEG 231
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  232 PGKEEEQEGEGDCGMAGPPglvgscgtSPEGIGGYIHAHRPLGPGEFESfIDVYAIRSAEgapqkEVYFMGLIDILTQYD 311
Cdd:smart00330 238 PPVYGSDESPSSESSNGGK--------APDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYT 303

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1788935069  312 AKKKAAHAAKTVKHGaGAEISTVHPDQYAKRFLDFITNIF 351
Cdd:smart00330 304 WDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 28-349 1.19e-76

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: 236.32  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  28 HFKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP----SESEG-SDGRFLVSYDRTLVIKEVSSEDIADMHSNLSNYHQ 102
Cdd:cd00139     2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENlrelKESEGkSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 103 YIVKcHGSTLLPQFLGMYRVSVDNEDS-YMLVMRNMFSHRLPVHRKYDLKGSLVSREAS-DKEKVKELPTLKDMDFLNKN 180
Cdd:cd00139    82 HIKK-NPNSLLTRFYGLYSIKLQKGKKvYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 181 QKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIvrgteseeegpgkeeeqegegdcgmagppglvgscgtsp 260
Cdd:cd00139   161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 261 egiggyihahrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPDQYA 340
Cdd:cd00139   202 -------------------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYA 244


                  ....*....
gi 1788935069 341 KRFLDFITN 349
Cdd:cd00139   245 ERFLKFMES 253
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
 2-349 1.99e-66

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: 212.16  E-value: 1.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   2 LLPDDFKASSKIKVNNHlfHRENLPSH---FKFKEYCPQVFRNLRDRFGIDDQDYQVSLT-RSPPSE--SEGSDGRFL-V 74
Cdd:cd17303    26 LTDADFKAVHKFSFDIT--GNELTPSSkydFKFKDYAPWVFRFLRELFGIDPADYLMSLTgKYILSElgSPGKSGSFFyF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  75 SYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGSTLLPQFLGMYRVSV-DNEDSYMLVMRNMFSHRLPVHRKYDLKGS 153
Cdd:cd17303   104 SRDYRFIIKTIHHSEHKFLRKILPDYYNH-VKENPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 154 LVSREAS-DKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDivrgteseeegp 232
Cdd:cd17303   183 TVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHD------------ 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 233 gkeeeqegegdcgmagppglvgscgtspegIGGYIHAhrplgpgefesfidvyaiRSAEGAPQKEVYFMGLIDILTQYDA 312
Cdd:cd17303   251 ------------------------------LDGGFQA------------------TDENNEPGDEIYYLGIIDILTPYNA 282

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1788935069 313 KKKAAHAAKTVKHgAGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17303   283 KKKLEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 56-350 7.93e-66

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: 207.32  E-value: 7.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  56 SLTRSPPSE--SEG-SDGRFLVSYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGSTLLPQFLGMYRVSVDNEDSYML 132
Cdd:pfam01504   1 LTGKSILSElsSPGkSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 133 VMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMD 211
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 212 YSLLLGIHDIVRgteseeegpgkeeeqegegdcgmagppglvgscgtspegiggyihahrplgpgefesfidvyairsae 291
Cdd:pfam01504 160 YSLLLGIHDLDE-------------------------------------------------------------------- 171

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1788935069 292 gaPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPDQYAKRFLDFITNI 350
Cdd:pfam01504 172 --DGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
 2-349 4.04e-49

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: 167.42  E-value: 4.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   2 LLPDDFKASSKIkvnnhLFHRE---NLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSE--SEGSDGR- 71
Cdd:cd17301    26 VLMQDFEVVESV-----FFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNEPLRElsNPGASGSl 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  72 FLVSYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLK 151
Cdd:cd17301   101 FYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLK 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 152 GSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEK-LKRDVEFLVQLKIMDYSLLLGIHDIvrgteseee 230
Cdd:cd17301   180 GSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKtIQRDCRVLESFKIMDYSLLLGVHNL--------- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 231 gpgkeeeqegegdcgmagppglvgscgtspegigGYIHAhrplgpgefesfidvyaiRSAEGapQKEVYFMGLIDILTQY 310
Cdd:cd17301   251 ----------------------------------GGIPA------------------RNSKG--ERLLLFIGIIDILQSY 276

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1788935069 311 DAKKKAAHAAKTVKHGaGAEISTVHPDQYAKRFLDFITN 349
Cdd:cd17301   277 RLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMAN 314
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
 24-350 1.14e-47

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: 163.62  E-value: 1.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  24 NLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLT-------RSPPSESeGSdgRFLVSYDRTLVIKEVSSEDIAD 92
Cdd:cd17302    48 TPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSLCgddalreLSSPGKS-GS--VFYLSHDDRFMIKTMRKSEMKV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  93 MHSNLSNYHQYiVKCHGSTLLPQFLGMYRV-SVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREAS-DKEKVKELPT 170
Cdd:cd17302   125 LLRMLPAYYKH-VKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNTT 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 171 LKDMDFlnkNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHdivrgteseeegpgkeeeqegegdcgmagpp 250
Cdd:cd17302   204 LKDLDL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH------------------------------- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 251 glvgscgtspegiggyihaHRPLGPGefesfidvyairsaeGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAe 330
Cdd:cd17302   250 -------------------FRAGDST---------------GEPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPAS- 294

                         330       340
                  ....*....|....*....|
gi 1788935069 331 ISTVHPDQYAKRFLDFITNI 350
Cdd:cd17302   295 ISAVDPKLYSRRFRDFIRKV 314
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 4-351 6.60e-40

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 149.60  E-value: 6.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069   4 PDDFKASSKIKVNnhlFHREN---LPSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSESEGSDGR----F 72
Cdd:PLN03185  375 PSDFGPRASFWMN---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKsgsvF 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  73 LVSYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGSTLLPQFLGMYRVSVDNEDSY-MLVMRNMFSHRLPVHRKYDLK 151
Cdd:PLN03185  452 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLK 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 152 GSLVSREAsDKEKVKELPTLKDMDFlnkNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIH---------DIV 222
Cdd:PLN03185  531 GSSLGRSA-DKVEIDENTTLKDLDL---NYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLP 606

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 223 RGTESEEEGPGKEEEQEGEGDCGMAGPPGLV--------GSCGTSPEGIGGYIHAHRP-------LGPGEFESFID--VY 285
Cdd:PLN03185  607 YSRSITADGLEVVAEEDTIEDEELSYPEGLVlvprgaddGSTVPGPHIRGSRLRASAAgdeevdlLLPGTARLQIQlgVN 686

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788935069 286 AIRSAEGAPQKE-------------VYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHPDQYAKRFLDFITNIF 351
Cdd:PLN03185  687 MPARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKVF 764
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 26-221 5.45e-38

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: 138.20  E-value: 5.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  26 PSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSE--SEGSDGR-FLVSYDRTLVIKEVSSEDIADMHSNLS 98
Cdd:cd17307    48 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIElsNPGASGSlFYVTSDDEFIIKTVQHKEAEFLQKLLP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  99 NYHQYIVKcHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLN 178
Cdd:cd17307   128 GYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQ 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1788935069 179 KNQK-VYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDI 221
Cdd:cd17307   207 DMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIHVL 250
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 26-350 1.27e-35

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: 132.04  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  26 PSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSE--SEGSDGR-FLVSYDRTLVIKEVSSEDIADMHSNLS 98
Cdd:cd17308    49 PAHhypdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIElsNPGASGSlFYVTSDDEFIIKTVMHKEAEFLQKLLP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  99 NYHQYIVKcHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLN 178
Cdd:cd17308   129 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 179 K-NQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDivrgteseeegpgkeeeqegegdcgmagppglvgscg 257
Cdd:cd17308   208 DmPEGLMLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHN------------------------------------- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 258 tspegIGGyihahrplgpgefesfidvyaIRSAEGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPD 337
Cdd:cd17308   251 -----IGG---------------------IPAVNGKGERLLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPS 303

                         330
                  ....*....|...
gi 1788935069 338 QYAKRFLDFITNI 350
Cdd:cd17308   304 FYAERFFKFMSNT 316
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 26-221 8.58e-35

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: 130.12  E-value: 8.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  26 PSH----FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPPSE--SEGSDGR-FLVSYDRTLVIKEVSSEDIADMHSNLS 98
Cdd:cd17306    51 PAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIElsNSGASGSlFYVSSDDEFIIKTVQHKEAEFLQKLLP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  99 NYHQYiVKCHGSTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLN 178
Cdd:cd17306   131 GYYMN-LNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQ 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1788935069 179 K-NQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDI 221
Cdd:cd17306   210 DiPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNI 253
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
22-221 1.38e-33

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 130.84  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  22 RENLPS---HFKFKEYCPQVFRNLRDRFGIDDQDYQvSLTRSPPSESEG--SDGRFLVSYDRTLVIKEVSSEDIADMHSN 96
Cdd:COG5253   326 NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALVS-LLSRYILWESNGgkSGSFFLFTRDYKFIIKTISHSEHICFRPM 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  97 LSNYHQYiVKCHGSTLLPQFLGMYRVSVDNEDS-------YMLVMRNMFSHRLPvHRKYDLKGSLVSREASDKEKVKE-L 168
Cdd:COG5253   405 IFEYYVH-VLFNPLTLLCKIFGFYRVKSRSSISssksrkiYFIVMENLFYPHGI-HRIFDLKGSMRNRHVERTGKSMSvL 482

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1788935069 169 PTLKDMDFLNKNQKVYIGEEeKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDI 221
Cdd:COG5253   483 LDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
 39-218 1.39e-33

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: 124.93  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  39 FRNLRDRFGIDDQDYQVSLTRSPPSESEG--SDGRFLVSYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCH---GSTLL 113
Cdd:cd17300    13 FHALRSLYCGGEDDFIRSLSRCVKWDASGgkSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALfhkRPSLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 114 PQFLGMYRVSVDNEDS------YMLVMRNMFsHRLPVHRKYDLKGSLVSREASDKEKVKElpTLKDMDFLN--KNQKVYI 185
Cdd:cd17300    93 AKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAEDEDS--VLLDENFLEytKGSPLYL 169

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1788935069 186 GEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGI 218
Cdd:cd17300   170 REHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 25-347 1.27e-26

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: 107.44  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  25 LPSH--FKFKEYCPQVFRNLRDRFGIDDQDYQVSLTRSPP-----SESEgSDGRFLVSYDRTLVIKEVSSEDIADMHSNL 97
Cdd:cd17304    43 IPKHkgFEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPylqfiSNSK-SGQDFFLTNDKRFFLKTQTKREAKFLLSIL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069  98 SNYHQYIVKcHGSTLLPQFLGMYRVSVD-NEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSR-EASDKEKVKELPTLKDMD 175
Cdd:cd17304   122 RKYVQHLEN-YPHSLLVKFLGVHSIKLPgKKKKYFIVMQSVFYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLN 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 176 FlnKNQKVYIGEEeKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDivrgteseeegpgkeeeqegegdcgmagppglvgs 255
Cdd:cd17304   201 F--EGNSINLGQQ-RSWFLRQVEIDTEFLKGLNVLDYSLLVGFQP----------------------------------- 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788935069 256 cgtspegiggyIHA--HRPLGPGEFEsfidvyAIRSAEGAPQKevYFMGLIDILTQYDAKKKAAHAAKTVKHgAGAEIST 333
Cdd:cd17304   243 -----------LHSdeNRRLLPNYKN------ALHVVDGPEYR--YFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFST 302

                         330
                  ....*....|....
gi 1788935069 334 VHPDQYAKRFLDFI 347
Cdd:cd17304   303 VSPEKYARRFCQWV 316
 
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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