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Conserved domains on  [gi|767996099|ref|XP_011523628|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 beta isoform X1 [Homo sapiens]

Protein Classification

phosphatidylinositol 5-phosphate 4-kinase type-2 beta( domain architecture ID 13022740)

phosphatidylinositol 5-phosphate 4-kinase type-2 beta (PIP5K2B or PIP4K2B) participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate, and preferentially utilizes GTP, rather than ATP, for PI(5)P phosphorylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
30-440 0e+00

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: 652.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  30 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 109
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 110 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipis 189
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ-------------------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 190 gwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDND 269
Cdd:cd17310  141 -------FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDND 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 270 FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygt 349
Cdd:cd17310  214 FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---------------------------------- 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 350 ppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQ 429
Cdd:cd17310  260 ---------------------------------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQ 300
                        410
                 ....*....|.
gi 767996099 430 YSKRFNEFMSN 440
Cdd:cd17310  301 YSKRFNEFMSN 311
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
30-440 0e+00

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: 652.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  30 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 109
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 110 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipis 189
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ-------------------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 190 gwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDND 269
Cdd:cd17310  141 -------FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDND 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 270 FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygt 349
Cdd:cd17310  214 FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---------------------------------- 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 350 ppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQ 429
Cdd:cd17310  260 ---------------------------------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQ 300
                        410
                 ....*....|.
gi 767996099 430 YSKRFNEFMSN 440
Cdd:cd17310  301 YSKRFNEFMSN 311
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
67-442 7.34e-121

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 355.54  E-value: 7.34e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099    67 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 142
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099   143 YDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHgNTLLPQFLGMYRLTVDG-- 220
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYE---------------------------HIVQNP-NTLLPKFFGLYRVKVKGgt 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099   221 -VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFL 298
Cdd:smart00330 132 eKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099   299 AQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAM 378
Cdd:smart00330 211 ESLKIMDYSLLVGIHDIERGQREEIELPPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAI 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996099   379 KSHEsspkkEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 442
Cdd:smart00330 285 RARR-----VVLYLGIIDILQTYTWDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
131-441 8.49e-74

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: 230.82  E-value: 8.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  131 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVEcHGNTLLPQF 210
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYE---------------------------HVKQ-NPNTLLPRF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  211 LGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLE 289
Cdd:pfam01504  64 YGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  290 KLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgef 369
Cdd:pfam01504 144 QLERDCEFLESLNIMDYSLLLGIHDLD----------------------------------------------------- 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996099  370 dpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 441
Cdd:pfam01504 171 --------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
33-441 1.67e-36

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 142.28  E-value: 1.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  33 VKLFRASEPILSvLMWGVNHTINELSnvPVPVM-LMPDDFKAYSKIKVDnhlFNKENLP-------SRFKFKEYCPMVFR 104
Cdd:PLN03185 342 IKGHRSYDLMLS-LQLGIRYTVGKIT--PIQRReVRPSDFGPRASFWMN---FPKAGSQltpshqsEDFKWKDYCPMVFR 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 105 NLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslp 183
Cdd:PLN03185 416 NLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH------------- 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 184 cgipisgwqkrckfiVECHGNTLLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDL 262
Cdd:PLN03185 483 ---------------VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDEN 546
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 263 PTFKDNDfLNegQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG-- 340
Cdd:PLN03185 547 TTLKDLD-LN--YSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvv 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 341 ---------------GNLLCSYGTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE- 388
Cdd:PLN03185 620 aeedtiedeelsypeGLVLVPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREd 699
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767996099 389 ------------VYFMAIIDILTPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 441
Cdd:PLN03185 700 kekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
78-314 1.73e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 130.07  E-value: 1.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  78 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSs 154
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTIS- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 155 edvaemHNILKKYHQMagslaclcilslpcgipISGWQKRCKFivecHGNTLLPQFLGMYRL-------TVDGVETYMVV 227
Cdd:COG5253  395 ------HSEHICFRPM-----------------IFEYYVHVLF----NPLTLLCKIFGFYRVksrssisSSKSRKIYFIV 447
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 228 TRNVFSHRLtVHRKYDLKGSTVAREASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDY 306
Cdd:COG5253  448 MENLFYPHG-IHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDY 525

                 ....*...
gi 767996099 307 SLLVGIHD 314
Cdd:COG5253  526 SLLVGIDD 533
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
30-440 0e+00

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: 652.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  30 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 109
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 110 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipis 189
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ-------------------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 190 gwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDND 269
Cdd:cd17310  141 -------FIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDND 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 270 FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygt 349
Cdd:cd17310  214 FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV---------------------------------- 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 350 ppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQ 429
Cdd:cd17310  260 ---------------------------------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQ 300
                        410
                 ....*....|.
gi 767996099 430 YSKRFNEFMSN 440
Cdd:cd17310  301 YSKRFNEFMSN 311
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
41-440 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: 578.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  41 PILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 120
Cdd:cd17305    1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 121 VTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVE 200
Cdd:cd17305   81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQ---------------------------YIVE 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 201 CHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVG 280
Cdd:cd17305  134 RHGKTLLPQYLGMYRITVNGVETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIG 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 281 EESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsf 360
Cdd:cd17305  214 DEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDC--------------------------------------------- 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 361 prffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 440
Cdd:cd17305  249 ----------------------------IYFMAIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
32-440 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: 544.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  32 KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG 111
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 112 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgw 191
Cdd:cd17309   81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQ---------------------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 192 qkrckFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFL 271
Cdd:cd17309  139 -----YIVECHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFI 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 272 NEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtpp 351
Cdd:cd17309  214 NDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV------------------------------------ 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 352 dspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYS 431
Cdd:cd17309  258 -------------------------------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYS 300

                 ....*....
gi 767996099 432 KRFNEFMSN 440
Cdd:cd17309  301 KRFLDFITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
41-440 8.33e-165

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: 465.49  E-value: 8.33e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  41 PILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 120
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 121 VTRSAPINSDSQGrcGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVE 200
Cdd:cd17311   81 LTRSPPYSESEGS--DGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQ---------------------------YIVK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 201 CHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVG 280
Cdd:cd17311  132 CHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 281 EESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsf 360
Cdd:cd17311  212 EEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV--------------------------------------------- 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 361 prffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 440
Cdd:cd17311  247 ----------------------------VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
67-442 7.34e-121

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 355.54  E-value: 7.34e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099    67 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 142
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099   143 YDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHgNTLLPQFLGMYRLTVDG-- 220
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYE---------------------------HIVQNP-NTLLPKFFGLYRVKVKGgt 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099   221 -VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFL 298
Cdd:smart00330 132 eKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099   299 AQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAM 378
Cdd:smart00330 211 ESLKIMDYSLLVGIHDIERGQREEIELPPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAI 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996099   379 KSHEsspkkEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 442
Cdd:smart00330 285 RARR-----VVLYLGIIDILQTYTWDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
92-440 2.02e-84

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: 259.04  E-value: 2.02e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  92 RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSD--SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ 169
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 170 magslaclcilslpcgipisgwqkrckFIVEcHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGST 248
Cdd:cd00139   82 ---------------------------HIKK-NPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGST 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 249 VAREAS-DKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemevee 327
Cdd:cd00139  134 VGRRVSkEKEKKKGLKVLKDLDFLEKGEKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL------------ 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 328 raedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKA 407
Cdd:cd00139  202 -------------------------------------------------------------VYYLGIIDILQEYNLRKKL 220
                        330       340       350
                 ....*....|....*....|....*....|...
gi 767996099 408 AHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 440
Cdd:cd00139  221 ERFLKSLLYGKDSGISCVPPDEYAERFLKFMES 253
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
131-441 8.49e-74

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: 230.82  E-value: 8.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  131 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVEcHGNTLLPQF 210
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYE---------------------------HVKQ-NPNTLLPRF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  211 LGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLE 289
Cdd:pfam01504  64 YGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  290 KLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgef 369
Cdd:pfam01504 144 QLERDCEFLESLNIMDYSLLLGIHDLD----------------------------------------------------- 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996099  370 dpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 441
Cdd:pfam01504 171 --------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
66-440 4.17e-69

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: 222.17  E-value: 4.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  66 LMPDDFKAYSKIKVDnHLFNKENLPSR--FKFKEYCPMVFRNLRERFGIDDQDYQNSVTrSAPINS--DSQGRCGTRFLT 141
Cdd:cd17303   26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLT-GKYILSelGSPGKSGSFFYF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 142 TYDRRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLTV-DG 220
Cdd:cd17303  104 SRDYRFIIKTIHHSEHKFLRKILPDYYNH----------------------------VKENPNTLLSQFYGLHRVKMpRG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 221 VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAS-DKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLA 299
Cdd:cd17303  156 RKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 300 QLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvGGnllcsygtppdspgnllsfprFFGPGEFDpsvdvyamk 379
Cdd:cd17303  236 SLNIMDYSLLVGIHDLD-----------------------GG---------------------FQATDENN--------- 262
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996099 380 shesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 440
Cdd:cd17303  263 ----EPGDEIYYLGIIDILTPYNAKKKLEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
93-441 1.93e-51

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: 175.94  E-value: 1.93e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  93 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMa 171
Cdd:cd17302   57 FKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 172 gslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLT-VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVA 250
Cdd:cd17302  136 ---------------------------VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 251 REASDKEKAKDLPT-FKDNDFlneGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveera 329
Cdd:cd17302  189 RTTGKPESEIDPNTtLKDLDL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH---------------- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 330 edeecendgvggnllcsygtppdspgnllsfprFFGPGEFDPSVDVyamkshesspkkeVYFMAIIDILTPYDTKKKAAH 409
Cdd:cd17302  250 ---------------------------------FRAGDSTGEPYDV-------------VLYFGIIDILQEYNISKKLEH 283
                        330       340       350
                 ....*....|....*....|....*....|..
gi 767996099 410 AAKTVKHGAGAeISTVNPEQYSKRFNEFMSNI 441
Cdd:cd17302  284 AYKSLQYDPAS-ISAVDPKLYSRRFRDFIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
42-440 3.27e-51

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: 175.51  E-value: 3.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  42 ILSVLMWGVNHTINELSNVPVPVMLMpDDFKayskiKVDNHLFNKE---NLP----SRFKFKEYCPMVFRNLRERFGIDD 114
Cdd:cd17301    3 LMGAIQLGIGHSVGSLSSKPERDVLM-QDFE-----VVESVFFPSEgstLTPahhySDFRFKTYAPVAFRYFRELFGIKP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 115 QDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKY----HQmagslaclcilslpcgipisg 190
Cdd:cd17301   77 DDYLLSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYymnlNQ--------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 191 wqkrckfivecHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDF 270
Cdd:cd17301  136 -----------NPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDF 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 271 LN---EGQKLhvgEESKKNFLEK-LKRDVEFLAQLKIMDYSLLVGIHDvdraeqeemeveeraedeecendgVGGnllcs 346
Cdd:cd17301  205 MEdhpEGILL---EPDTYDALLKtIQRDCRVLESFKIMDYSLLLGVHN------------------------LGG----- 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 347 ygtppdspgnllsfprffgpgefdpsvdvyaMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVN 426
Cdd:cd17301  253 -------------------------------IPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHR 300
                        410
                 ....*....|....
gi 767996099 427 PEQYSKRFNEFMSN 440
Cdd:cd17301  301 PSFYAERFQNFMAN 314
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
49-313 2.92e-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: 149.37  E-value: 2.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  49 GVNHTINELSNVPVPVMLMPDDFKAYSKI--KVDNHLFNKENLPSrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP 126
Cdd:cd17307   10 GIGYTVGNLTSKPDRDVLMQDFYVVESVFlpSEGSNLTPAHHYPD-FRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 127 INSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMAGSlaclcilslpcgipisgwqkrckfivecHGNTL 206
Cdd:cd17307   89 IELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ----------------------------NPRTL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 207 LPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQK-LHVGEESKK 285
Cdd:cd17307  141 LPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDgLYFDPETYN 220
                        250       260
                 ....*....|....*....|....*...
gi 767996099 286 NFLEKLKRDVEFLAQLKIMDYSLLVGIH 313
Cdd:cd17307  221 ALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
49-442 1.70e-39

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: 144.37  E-value: 1.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  49 GVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NLP-----SRFKFKEYCPMVFRNLRERFGIDDQDYQNSV 121
Cdd:cd17308   11 GIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLTpahhyPDFRFKTYAPVAFRYFRELFGIRPDDYLYSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 122 TRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMAGSlaclcilslpcgipisgwqkrckfivec 201
Cdd:cd17308   85 CNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ---------------------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 202 HGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVG 280
Cdd:cd17308  137 NPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLD 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 281 EESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgNLLSF 360
Cdd:cd17308  217 ADTFSALVKTLQRDCLVLESFKIMDYSLLLGVH------------------------------------------NIGGI 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 361 PRFFGPGEfdpsvdvyamkshesspkKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 440
Cdd:cd17308  255 PAVNGKGE------------------RLLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSN 315

                 ..
gi 767996099 441 IL 442
Cdd:cd17308  316 TV 317
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
39-316 4.17e-39

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: 143.98  E-value: 4.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  39 SEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NLP-----SRFKFKEYCPMVFRNLRERFG 111
Cdd:cd17306    3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLTpahhyNDFRFKTYAPVAFRYFRELFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 112 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslpcgipisgw 191
Cdd:cd17306   77 IRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMN--------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 192 qkrckfiVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFL 271
Cdd:cd17306  136 -------LNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFL 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767996099 272 NE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 316
Cdd:cd17306  209 QDiPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNID 254
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
33-441 1.67e-36

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 142.28  E-value: 1.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  33 VKLFRASEPILSvLMWGVNHTINELSnvPVPVM-LMPDDFKAYSKIKVDnhlFNKENLP-------SRFKFKEYCPMVFR 104
Cdd:PLN03185 342 IKGHRSYDLMLS-LQLGIRYTVGKIT--PIQRReVRPSDFGPRASFWMN---FPKAGSQltpshqsEDFKWKDYCPMVFR 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 105 NLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslp 183
Cdd:PLN03185 416 NLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH------------- 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 184 cgipisgwqkrckfiVECHGNTLLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDL 262
Cdd:PLN03185 483 ---------------VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDEN 546
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 263 PTFKDNDfLNegQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG-- 340
Cdd:PLN03185 547 TTLKDLD-LN--YSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvv 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 341 ---------------GNLLCSYGTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE- 388
Cdd:PLN03185 620 aeedtiedeelsypeGLVLVPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREd 699
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767996099 389 ------------VYFMAIIDILTPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 441
Cdd:PLN03185 700 kekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
49-440 1.08e-32

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: 125.93  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  49 GVNHTINELSNVPVPVMLMPDDFKAyskiKVDNHLFNKENlpsrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP-I 127
Cdd:cd17304   13 GLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 128 NSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslpcgipisgwqkrckfiVECHGNTLL 207
Cdd:cd17304   85 QFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQH----------------------------LENYPHSLL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 208 PQFLGMYRLTVDG-VETYMVVTRNVFSHRLTVHRKYDLKGSTVAR-EASDKEKAKDLPTFKDNDFlnEGQKLHVGEEsKK 285
Cdd:cd17304  137 VKFLGVHSIKLPGkKKKYFIVMQSVFYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQ-RS 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 286 NFLEKLKRDVEFLAQLKIMDYSLLVGI----HDVDRaeqeemeveeraedeecendgvggNLLcsygtpPDSPGNLlsfp 361
Cdd:cd17304  214 WFLRQVEIDTEFLKGLNVLDYSLLVGFqplhSDENR------------------------RLL------PNYKNAL---- 259
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996099 362 rffgpgefdpsvdvyamksHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 440
Cdd:cd17304  260 -------------------HVVDGPEYRYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWVED 318
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
78-314 1.73e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 130.07  E-value: 1.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099  78 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSs 154
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTIS- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 155 edvaemHNILKKYHQMagslaclcilslpcgipISGWQKRCKFivecHGNTLLPQFLGMYRL-------TVDGVETYMVV 227
Cdd:COG5253  395 ------HSEHICFRPM-----------------IFEYYVHVLF----NPLTLLCKIFGFYRVksrssisSSKSRKIYFIV 447
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 228 TRNVFSHRLtVHRKYDLKGSTVAREASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDY 306
Cdd:COG5253  448 MENLFYPHG-IHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDY 525

                 ....*...
gi 767996099 307 SLLVGIHD 314
Cdd:COG5253  526 SLLVGIDD 533
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
103-312 5.38e-28

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: 111.45  E-value: 5.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 103 FRNLRERFGIDDQDYQNSVTRSAPINSdSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKY-HQMAGSLaclcils 181
Cdd:cd17300   13 FHALRSLYCGGEDDFIRSLSRCVKWDA-SGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfEYMAKAL------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996099 182 lpcgipisgwqkrckfivECHGNTLLPQFLGMYRLTVDGVET------YMVVTRNVFsHRLTVHRKYDLKGSTVAREASD 255
Cdd:cd17300   85 ------------------FHKRPSLLAKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNV 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767996099 256 KEKakDLPTFKDNDFLNE--GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 312
Cdd:cd17300  146 AED--EDSVLLDENFLEYtkGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 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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