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Conserved domains on  [gi|635092791|ref|XP_008011094|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 beta [Chlorocebus sabaeus]

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 ...
30-413 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: 656.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  30 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 109
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 110 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 189
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 190 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 269
Cdd:cd17310  161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 270 FLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvy 349
Cdd:cd17310  241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635092791 350 amkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17310  260 ------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
30-413 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: 656.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  30 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 109
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 110 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 189
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 190 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 269
Cdd:cd17310  161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 270 FLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvy 349
Cdd:cd17310  241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635092791 350 amkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17310  260 ------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
67-415 1.35e-125

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 366.71  E-value: 1.35e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791    67 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 142
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791   143 YDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHgNTLLPQFLGMYRLTVDG---VETYMVVTRNVFSHRLTVHRKYDLKG 219
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791   220 STVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEV 298
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791   299 EERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAMKSHEsspkkEVYFMAIIDILTPYDTKK 378
Cdd:smart00330 238 PPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAIRARR-----VVLYLGIIDILQTYTWDK 306
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 635092791   379 KAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 415
Cdd:smart00330 307 KLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
131-414 5.06e-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: 243.53  E-value: 5.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  131 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLT 210
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  211 VHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 289
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  290 raeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesSPKKEVYFMAIID 369
Cdd:pfam01504 171 -------------------------------------------------------------------EDGKEIYYLGIID 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 635092791  370 ILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 414
Cdd:pfam01504 184 ILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
33-414 1.94e-40

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 153.06  E-value: 1.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  33 VKLFRASEPILSvLMWGVNHTINELSnvPVPVM-LMPDDFKAYSKIKVDnhlFNKENLP-------SRFKFKEYCPMVFR 104
Cdd:PLN03185 342 IKGHRSYDLMLS-LQLGIRYTVGKIT--PIQRReVRPSDFGPRASFWMN---FPKAGSQltpshqsEDFKWKDYCPMVFR 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 105 NLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFiVECHGNTLLPQF 183
Cdd:PLN03185 416 NLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKF 494
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 184 LGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDfLNegQKLHVGEESKKNFLE 262
Cdd:PLN03185 495 FGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLD-LN--YSFYLEPSWRDALLR 570
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 263 KLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG-----------------GNLLCSYGTPPD 325
Cdd:PLN03185 571 QIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvvaeedtiedeelsypeGLVLVPRGADDG 646
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 326 S--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE-------------VYFMAIIDILTPYDT 376
Cdd:PLN03185 647 StvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNM 726
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 635092791 377 KKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 414
Cdd:PLN03185 727 SKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
78-287 4.36e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 139.70  E-value: 4.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  78 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSS 154
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISH 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 155 edvAEMHNILKKYHQFIVEC--HGNTLLPQFLGMYRL-------TVDGVETYMVVTRNVFSHRLtVHRKYDLKGSTVARE 225
Cdd:COG5253  396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVksrssisSSKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRH 471
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 635092791 226 ASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHD 287
Cdd:COG5253  472 VERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD 533
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
30-413 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: 656.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  30 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 109
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 110 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 189
Cdd:cd17310   81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 190 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 269
Cdd:cd17310  161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 270 FLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvy 349
Cdd:cd17310  241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635092791 350 amkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17310  260 ------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
41-413 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: 585.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  41 PILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 120
Cdd:cd17305    1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 121 VTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV 200
Cdd:cd17305   81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 201 TRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 280
Cdd:cd17305  161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 281 LLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkk 360
Cdd:cd17305  241 LLVGIHDC------------------------------------------------------------------------ 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 635092791 361 eVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17305  249 -IYFMAIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
32-413 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  32 KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG 111
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 112 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTV 191
Cdd:cd17309   81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 192 DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFL 271
Cdd:cd17309  161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 272 AQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyam 351
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635092791 352 kshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17309  258 ----------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
41-413 1.79e-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: 473.97  E-value: 1.79e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  41 PILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 120
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 121 VTRSAPINSDSQGrcGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV 200
Cdd:cd17311   81 LTRSPPYSESEGS--DGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 201 TRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 280
Cdd:cd17311  159 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 281 LLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkk 360
Cdd:cd17311  239 LLLGIHDV------------------------------------------------------------------------ 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 635092791 361 eVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17311  247 -VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
67-415 1.35e-125

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 366.71  E-value: 1.35e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791    67 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 142
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791   143 YDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHgNTLLPQFLGMYRLTVDG---VETYMVVTRNVFSHRLTVHRKYDLKG 219
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791   220 STVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEV 298
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791   299 EERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAMKSHEsspkkEVYFMAIIDILTPYDTKK 378
Cdd:smart00330 238 PPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAIRARR-----VVLYLGIIDILQTYTWDK 306
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 635092791   379 KAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 415
Cdd:smart00330 307 KLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
92-413 1.54e-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: 271.37  E-value: 1.54e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  92 RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSD--SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ 169
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 170 FIVEcHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAS-DKEKAKDLPTFKDNDFLNEG 247
Cdd:cd00139   82 HIKK-NPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 248 QKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdsp 327
Cdd:cd00139  161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 328 gnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRF 407
Cdd:cd00139  202 ----------------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERF 247

                 ....*.
gi 635092791 408 NEFMSN 413
Cdd:cd00139  248 LKFMES 253
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
131-414 5.06e-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: 243.53  E-value: 5.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  131 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLT 210
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  211 VHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 289
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  290 raeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesSPKKEVYFMAIID 369
Cdd:pfam01504 171 -------------------------------------------------------------------EDGKEIYYLGIID 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 635092791  370 ILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 414
Cdd:pfam01504 184 ILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
66-413 1.56e-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: 232.57  E-value: 1.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  66 LMPDDFKAYSKIKVDnHLFNKENLPSR--FKFKEYCPMVFRNLRERFGIDDQDYQNSVTrSAPINS--DSQGRCGTRFLT 141
Cdd:cd17303   26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLT-GKYILSelGSPGKSGSFFYF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 142 TYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGS 220
Cdd:cd17303  104 SRDYRFIIKTIHHSEHKFLRKILPDYYNHVKE-NPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 221 TVAREAS-DKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeve 299
Cdd:cd17303  183 TVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD---------- 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 300 eraedeecendgvGGnllcsygtppdspgnllsfprFFGPGEFDpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKK 379
Cdd:cd17303  253 -------------GG---------------------FQATDENN-------------EPGDEIYYLGIIDILTPYNAKKK 285
                        330       340       350
                 ....*....|....*....|....*....|....
gi 635092791 380 AAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17303  286 LEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
93-414 2.88e-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: 185.19  E-value: 2.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  93 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFi 171
Cdd:cd17302   57 FKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 172 VECHGNTLLPQFLGMYRLT-VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFlneGQK 249
Cdd:cd17302  136 VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTtLKDLDL---DFK 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 250 LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgn 329
Cdd:cd17302  213 FRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH------------------------------------------- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 330 llsfprFFGPGEFDPSVDVyamkshesspkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFNE 409
Cdd:cd17302  250 ------FRAGDSTGEPYDV-------------VLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRRFRD 309

                 ....*
gi 635092791 410 FMSNI 414
Cdd:cd17302  310 FIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
42-413 5.30e-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: 184.76  E-value: 5.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  42 ILSVLMWGVNHTINELSNVPVPVMLMpDDFKayskiKVDNHLFNKE---NLP----SRFKFKEYCPMVFRNLRERFGIDD 114
Cdd:cd17301    3 LMGAIQLGIGHSVGSLSSKPERDVLM-QDFE-----VVESVFFPSEgstLTPahhySDFRFKTYAPVAFRYFRELFGIKP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 115 QDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGV 194
Cdd:cd17301   77 DDYLLSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 195 ETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLN---EGQKLhvgEESKKNFLEK-LKRDVEF 270
Cdd:cd17301  156 NIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEdhpEGILL---EPDTYDALLKtIQRDCRV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 271 LAQLKIMDYSLLVGIHDvdraeqeemeveeraedeecendgVGGnllcsygtppdspgnllsfprffgpgefdpsvdvya 350
Cdd:cd17301  233 LESFKIMDYSLLLGVHN------------------------LGG------------------------------------ 252
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 635092791 351 MKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17301  253 IPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMAN 314
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
49-286 1.08e-45

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: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  49 GVNHTINELSNVPVPVMLMPDDFKAYSKI--KVDNHLFNKENLPSrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP 126
Cdd:cd17307   10 GIGYTVGNLTSKPDRDVLMQDFYVVESVFlpSEGSNLTPAHHYPD-FRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 127 INSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFS 206
Cdd:cd17307   89 IELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 207 HRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQK-LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 285
Cdd:cd17307  168 RSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGI 247

                 .
gi 635092791 286 H 286
Cdd:cd17307  248 H 248
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
49-415 2.93e-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: 154.00  E-value: 2.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  49 GVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NLP-----SRFKFKEYCPMVFRNLRERFGIDDQDYQNSV 121
Cdd:cd17308   11 GIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLTpahhyPDFRFKTYAPVAFRYFRELFGIRPDDYLYSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 122 TRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVT 201
Cdd:cd17308   85 CNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 202 RNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 280
Cdd:cd17308  164 NNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVLESFKIMDYS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 281 LLVGIHdvdraeqeemeveeraedeecendgvggnllcsygtppdspgNLLSFPRFFGPGEfdpsvdvyamkshesspkK 360
Cdd:cd17308  244 LLLGVH------------------------------------------NIGGIPAVNGKGE------------------R 263
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 635092791 361 EVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 415
Cdd:cd17308  264 LLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSNTV 317
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
39-289 1.02e-42

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: 152.84  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  39 SEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NLP-----SRFKFKEYCPMVFRNLRERFG 111
Cdd:cd17306    3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLTpahhyNDFRFKTYAPVAFRYFRELFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 112 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTV 191
Cdd:cd17306   77 IRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 192 DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEF 270
Cdd:cd17306  156 GGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLV 235
                        250
                 ....*....|....*....
gi 635092791 271 LAQLKIMDYSLLVGIHDVD 289
Cdd:cd17306  236 LQSFKIMDYSLLVGIHNID 254
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
33-414 1.94e-40

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 153.06  E-value: 1.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  33 VKLFRASEPILSvLMWGVNHTINELSnvPVPVM-LMPDDFKAYSKIKVDnhlFNKENLP-------SRFKFKEYCPMVFR 104
Cdd:PLN03185 342 IKGHRSYDLMLS-LQLGIRYTVGKIT--PIQRReVRPSDFGPRASFWMN---FPKAGSQltpshqsEDFKWKDYCPMVFR 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 105 NLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFiVECHGNTLLPQF 183
Cdd:PLN03185 416 NLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKF 494
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 184 LGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDfLNegQKLHVGEESKKNFLE 262
Cdd:PLN03185 495 FGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEIDENTTLKDLD-LN--YSFYLEPSWRDALLR 570
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 263 KLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAEDEECENDGVG-----------------GNLLCSYGTPPD 325
Cdd:PLN03185 571 QIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPYSRSITADGLEvvaeedtiedeelsypeGLVLVPRGADDG 646
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 326 S--PGNLLSFPRFFGPGEFDPSVD--------------VYAMKSHESSPKKE-------------VYFMAIIDILTPYDT 376
Cdd:PLN03185 647 StvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNMPARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNM 726
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 635092791 377 KKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 414
Cdd:PLN03185 727 SKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
49-413 1.87e-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: 135.56  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  49 GVNHTINELSNVPVPVMLMPDDFKAyskiKVDNHLFNKENlpsrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP-I 127
Cdd:cd17304   13 GLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 128 NSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIvECHGNTLLPQFLGMYRLTVDG-VETYMVVTRNVFS 206
Cdd:cd17304   85 QFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL-ENYPHSLLVKFLGVHSIKLPGkKKKYFIVMQSVFY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 207 HRLTVHRKYDLKGSTVAR-EASDKEKAKDLPTFKDNDFlnEGQKLHVGEEsKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 285
Cdd:cd17304  164 PDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQ-RSWFLRQVEIDTEFLKGLNVLDYSLLVGF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 286 ----HDVDRaeqeemeveeraedeecendgvggNLLcsygtpPDSPGNLlsfprffgpgefdpsvdvyamksHESSPKKE 361
Cdd:cd17304  241 qplhSDENR------------------------RLL------PNYKNAL-----------------------HVVDGPEY 267
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 635092791 362 VYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 413
Cdd:cd17304  268 RYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWVED 318
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
78-287 4.36e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 139.70  E-value: 4.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791  78 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSS 154
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISH 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 155 edvAEMHNILKKYHQFIVEC--HGNTLLPQFLGMYRL-------TVDGVETYMVVTRNVFSHRLtVHRKYDLKGSTVARE 225
Cdd:COG5253  396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVksrssisSSKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRH 471
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 635092791 226 ASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHD 287
Cdd:COG5253  472 VERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD 533
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
103-285 4.34e-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: 4.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 103 FRNLRERFGIDDQDYQNSVTRSAPINSdSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGN---TL 179
Cdd:cd17300   13 FHALRSLYCGGEDDFIRSLSRCVKWDA-SGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHkrpSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635092791 180 LPQFLGMYRLTVDGVET------YMVVTRNVFsHRLTVHRKYDLKGSTVAREASDKEKakDLPTFKDNDFLNE--GQKLH 251
Cdd:cd17300   92 LAKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAED--EDSVLLDENFLEYtkGSPLY 168
                        170       180       190
                 ....*....|....*....|....*....|....
gi 635092791 252 VGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 285
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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