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Conserved domains on  [gi|939186216|pdb|3WZZ|A]
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Chain A, Phosphatidylinositol 5-phosphate 4-kinase type-2 beta

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 ...
7-390 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: 657.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        7 GQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 86
Cdd:cd17310   1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       87 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 166
Cdd:cd17310  81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      167 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 246
Cdd:cd17310 161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      247 FLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvy 326
Cdd:cd17310 241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3WZZ_A      327 amkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17310 260 ------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
7-390 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: 657.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        7 GQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 86
Cdd:cd17310   1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       87 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 166
Cdd:cd17310  81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      167 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 246
Cdd:cd17310 161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      247 FLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvy 326
Cdd:cd17310 241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3WZZ_A      327 amkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17310 260 ------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
44-392 1.56e-125

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 365.55  E-value: 1.56e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A          44 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 119
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         120 YDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHgNTLLPQFLGMYRLTVDG---VETYMVVTRNVFSHRLTVHRKYDLKG 196
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         197 STVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEV 275
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         276 EERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAMKSHEsspkkEVYFMAIIDILTPYDTKK 355
Cdd:smart00330 238 PPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAIRARR-----VVLYLGIIDILQTYTWDK 306
                          330       340       350
                   ....*....|....*....|....*....|....*..
3WZZ_A         356 KAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 392
Cdd:smart00330 307 KLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
108-391 5.17e-79

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: 242.76  E-value: 5.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        108 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLT 187
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        188 VHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 266
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        267 raeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesSPKKEVYFMAIID 346
Cdd:pfam01504 171 -------------------------------------------------------------------EDGKEIYYLGIID 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
3WZZ_A        347 ILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 391
Cdd:pfam01504 184 ILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
6-391 8.36e-41

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 153.45  E-value: 8.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         6 PGQKV-KLFRASEPILSvLMWGVNHTINELSnvPVPVM-LMPDDFKAYSKIKVDnhlFNKENLP-------SRFKFKEYC 76
Cdd:PLN03185 337 PGETIiKGHRSYDLMLS-LQLGIRYTVGKIT--PIQRReVRPSDFGPRASFWMN---FPKAGSQltpshqsEDFKWKDYC 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        77 PMVFRNLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFiVECHGNT 155
Cdd:PLN03185 411 PMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENT 489
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       156 LLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDfLNegQKLHVGEESK 234
Cdd:PLN03185 490 LITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLD-LN--YSFYLEPSWR 565
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       235 KNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG-----------------GNLLCSY 297
Cdd:PLN03185 566 DALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvvaeedtiedeelsypeGLVLVPR 641
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       298 GTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE-------------VYFMAIIDIL 348
Cdd:PLN03185 642 GADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREdkekqsfhevydvVLYLGIIDIL 721
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
3WZZ_A       349 TPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 391
Cdd:PLN03185 722 QEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
55-264 2.23e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 140.08  E-value: 2.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       55 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSS 131
Cdd:COG5253 320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISH 395
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      132 edvAEMHNILKKYHQFIVEC--HGNTLLPQFLGMYRL-------TVDGVETYMVVTRNVFSHRLtVHRKYDLKGSTVARE 202
Cdd:COG5253 396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVksrssisSSKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRH 471
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3WZZ_A      203 ASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHD 264
Cdd:COG5253 472 VERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD 533
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
7-390 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: 657.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        7 GQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 86
Cdd:cd17310   1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       87 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 166
Cdd:cd17310  81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      167 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 246
Cdd:cd17310 161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      247 FLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvy 326
Cdd:cd17310 241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3WZZ_A      327 amkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17310 260 ------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
18-390 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: 585.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       18 PILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 97
Cdd:cd17305   1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       98 VTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV 177
Cdd:cd17305  81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      178 TRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 257
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      258 LLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkk 337
Cdd:cd17305 241 LLVGIHDC------------------------------------------------------------------------ 248
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
3WZZ_A      338 eVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17305 249 -IYFMAIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
9-390 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: 550.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        9 KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG 88
Cdd:cd17309   1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       89 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTV 168
Cdd:cd17309  81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      169 DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFL 248
Cdd:cd17309 161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      249 AQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyam 328
Cdd:cd17309 241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3WZZ_A      329 kshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17309 258 ----------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
18-390 2.85e-168

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: 472.43  E-value: 2.85e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       18 PILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 97
Cdd:cd17311   1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       98 VTRSAPINSDSQGrcGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV 177
Cdd:cd17311  81 LTRSPPYSESEGS--DGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      178 TRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 257
Cdd:cd17311 159 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      258 LLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkk 337
Cdd:cd17311 239 LLLGIHDV------------------------------------------------------------------------ 246
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
3WZZ_A      338 eVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17311 247 -VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
44-392 1.56e-125

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 365.55  E-value: 1.56e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A          44 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 119
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         120 YDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHgNTLLPQFLGMYRLTVDG---VETYMVVTRNVFSHRLTVHRKYDLKG 196
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         197 STVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEV 275
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         276 EERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAMKSHEsspkkEVYFMAIIDILTPYDTKK 355
Cdd:smart00330 238 PPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAIRARR-----VVLYLGIIDILQTYTWDK 306
                          330       340       350
                   ....*....|....*....|....*....|....*..
3WZZ_A         356 KAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 392
Cdd:smart00330 307 KLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
69-390 1.49e-89

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: 270.60  E-value: 1.49e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       69 RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSD--SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ 146
Cdd:cd00139   2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      147 FIVEcHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAS-DKEKAKDLPTFKDNDFLNEG 224
Cdd:cd00139  82 HIKK-NPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      225 QKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdsp 304
Cdd:cd00139 161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      305 gnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRF 384
Cdd:cd00139 202 ----------------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERF 247

                ....*.
3WZZ_A      385 NEFMSN 390
Cdd:cd00139 248 LKFMES 253
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
108-391 5.17e-79

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: 242.76  E-value: 5.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        108 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLT 187
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        188 VHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 266
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        267 raeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesSPKKEVYFMAIID 346
Cdd:pfam01504 171 -------------------------------------------------------------------EDGKEIYYLGIID 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
3WZZ_A        347 ILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 391
Cdd:pfam01504 184 ILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
43-390 2.27e-73

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: 231.42  E-value: 2.27e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       43 LMPDDFKAYSKIKVDnHLFNKENLPSR--FKFKEYCPMVFRNLRERFGIDDQDYQNSVTrSAPINS--DSQGRCGTRFLT 118
Cdd:cd17303  26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLT-GKYILSelGSPGKSGSFFYF 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      119 TYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGS 197
Cdd:cd17303 104 SRDYRFIIKTIHHSEHKFLRKILPDYYNHVKE-NPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGS 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      198 TVAREAS-DKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeve 276
Cdd:cd17303 183 TVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD---------- 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      277 eraedeecendgvGGnllcsygtppdspgnllsfprFFGPGEFDpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKK 356
Cdd:cd17303 253 -------------GG---------------------FQATDENN-------------EPGDEIYYLGIIDILTPYNAKKK 285
                       330       340       350
                ....*....|....*....|....*....|....
3WZZ_A      357 AAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17303 286 LEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
70-391 2.02e-55

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: 184.80  E-value: 2.02e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       70 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFi 148
Cdd:cd17302  57 FKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH- 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      149 VECHGNTLLPQFLGMYRLT-VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFlneGQK 226
Cdd:cd17302 136 VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTtLKDLDL---DFK 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      227 LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgn 306
Cdd:cd17302 213 FRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH------------------------------------------- 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      307 llsfprFFGPGEFDPSVDVyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFNE 386
Cdd:cd17302 250 ------FRAGDSTGEPYDV-------------VLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRRFRD 309

                ....*
3WZZ_A      387 FMSNI 391
Cdd:cd17302 310 FIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
19-390 5.50e-55

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: 183.99  E-value: 5.50e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       19 ILSVLMWGVNHTINELSNVPVPVMLMpDDFKayskiKVDNHLFNKE---NLP----SRFKFKEYCPMVFRNLRERFGIDD 91
Cdd:cd17301   3 LMGAIQLGIGHSVGSLSSKPERDVLM-QDFE-----VVESVFFPSEgstLTPahhySDFRFKTYAPVAFRYFRELFGIKP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       92 QDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGV 171
Cdd:cd17301  77 DDYLLSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      172 ETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLN---EGQKLhvgEESKKNFLEK-LKRDVEF 247
Cdd:cd17301 156 NIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEdhpEGILL---EPDTYDALLKtIQRDCRV 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      248 LAQLKIMDYSLLVGIHDvdraeqeemeveeraedeecendgVGGnllcsygtppdspgnllsfprffgpgefdpsvdvya 327
Cdd:cd17301 233 LESFKIMDYSLLLGVHN------------------------LGG------------------------------------ 252
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3WZZ_A      328 MKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17301 253 IPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMAN 314
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
26-263 8.22e-46

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: 160.16  E-value: 8.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       26 GVNHTINELSNVPVPVMLMPDDFKAYSKI--KVDNHLFNKENLPSrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP 103
Cdd:cd17307  10 GIGYTVGNLTSKPDRDVLMQDFYVVESVFlpSEGSNLTPAHHYPD-FRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      104 INSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFS 183
Cdd:cd17307  89 IELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      184 HRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQK-LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 262
Cdd:cd17307 168 RSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGI 247

                .
3WZZ_A      263 H 263
Cdd:cd17307 248 H 248
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
26-392 3.97e-43

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: 152.84  E-value: 3.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       26 GVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NLP-----SRFKFKEYCPMVFRNLRERFGIDDQDYQNSV 98
Cdd:cd17308  11 GIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLTpahhyPDFRFKTYAPVAFRYFRELFGIRPDDYLYSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       99 TRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVT 178
Cdd:cd17308  85 CNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      179 RNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 257
Cdd:cd17308 164 NNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVLESFKIMDYS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      258 LLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgNLLSFPRFFGPGEfdpsvdvyamkshesspkK 337
Cdd:cd17308 244 LLLGVH------------------------------------------NIGGIPAVNGKGE------------------R 263
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
3WZZ_A      338 EVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 392
Cdd:cd17308 264 LLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSNTV 317
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
16-266 9.14e-43

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: 152.46  E-value: 9.14e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       16 SEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NLP-----SRFKFKEYCPMVFRNLRERFG 88
Cdd:cd17306   3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLTpahhyNDFRFKTYAPVAFRYFRELFG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       89 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTV 168
Cdd:cd17306  77 IRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      169 DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEF 247
Cdd:cd17306 156 GGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLV 235
                       250
                ....*....|....*....
3WZZ_A      248 LAQLKIMDYSLLVGIHDVD 266
Cdd:cd17306 236 LQSFKIMDYSLLVGIHNID 254
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
6-391 8.36e-41

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 153.45  E-value: 8.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A         6 PGQKV-KLFRASEPILSvLMWGVNHTINELSnvPVPVM-LMPDDFKAYSKIKVDnhlFNKENLP-------SRFKFKEYC 76
Cdd:PLN03185 337 PGETIiKGHRSYDLMLS-LQLGIRYTVGKIT--PIQRReVRPSDFGPRASFWMN---FPKAGSQltpshqsEDFKWKDYC 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A        77 PMVFRNLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFiVECHGNT 155
Cdd:PLN03185 411 PMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENT 489
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       156 LLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDfLNegQKLHVGEESK 234
Cdd:PLN03185 490 LITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLD-LN--YSFYLEPSWR 565
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       235 KNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG-----------------GNLLCSY 297
Cdd:PLN03185 566 DALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvvaeedtiedeelsypeGLVLVPR 641
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       298 GTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE-------------VYFMAIIDIL 348
Cdd:PLN03185 642 GADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREdkekqsfhevydvVLYLGIIDIL 721
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
3WZZ_A       349 TPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 391
Cdd:PLN03185 722 QEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
55-264 2.23e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 140.08  E-value: 2.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       55 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSS 131
Cdd:COG5253 320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISH 395
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      132 edvAEMHNILKKYHQFIVEC--HGNTLLPQFLGMYRL-------TVDGVETYMVVTRNVFSHRLtVHRKYDLKGSTVARE 202
Cdd:COG5253 396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVksrssisSSKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRH 471
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3WZZ_A      203 ASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHD 264
Cdd:COG5253 472 VERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD 533
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
26-390 2.36e-36

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: 134.79  E-value: 2.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       26 GVNHTINELSNVPVPVMLMPDDFKAyskiKVDNHLFNKENlpsrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP-I 104
Cdd:cd17304  13 GLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      105 NSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIvECHGNTLLPQFLGMYRLTVDGV-ETYMVVTRNVFS 183
Cdd:cd17304  85 QFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL-ENYPHSLLVKFLGVHSIKLPGKkKKYFIVMQSVFY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      184 HRLTVHRKYDLKGSTVAR-EASDKEKAKDLPTFKDNDFlnEGQKLHVGEEsKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 262
Cdd:cd17304 164 PDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQ-RSWFLRQVEIDTEFLKGLNVLDYSLLVGF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      263 ----HDVDRaeqeemeveeraedeecendgvggNLLcsygtpPDSPGNLlsfprffgpgefdpsvdvyamksHESSPKKE 338
Cdd:cd17304 241 qplhSDENR------------------------RLL------PNYKNAL-----------------------HVVDGPEY 267
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
3WZZ_A      339 VYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 390
Cdd:cd17304 268 RYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWVED 318
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
80-262 2.70e-31

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


Pssm-ID: 340437  Cd Length: 262  Bit Score: 119.54  E-value: 2.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A       80 FRNLRERFGIDDQDYQNSVTRSAPINSdSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGN---TL 156
Cdd:cd17300  13 FHALRSLYCGGEDDFIRSLSRCVKWDA-SGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHkrpSL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WZZ_A      157 LPQFLGMYRLTVDGVET------YMVVTRNVFsHRLTVHRKYDLKGSTVAREASDKEKakDLPTFKDNDFLNE--GQKLH 228
Cdd:cd17300  92 LAKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAED--EDSVLLDENFLEYtkGSPLY 168
                       170       180       190
                ....*....|....*....|....*....|....
3WZZ_A      229 VGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 262
Cdd:cd17300 169 LREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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