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Conserved domains on  [gi|85724748|ref|NP_001033806|]
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phosphatidylinositol 5-phosphate 4-kinase, isoform A [Drosophila melanogaster]

Protein Classification

phosphatidylinositol 5-phosphate 4-kinase type-2( domain architecture ID 13022698)

phosphatidylinositol 5-phosphate 4-kinase type-2 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)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
34-401 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: 545.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  34 PILSVFMWGINHTINELSHVNIPVMLLPDDFRAYSKIKVDNHLFNKENMPSHFKVKEYCPLVFRNLRERFGVDDVDYRES 113
Cdd:cd17305   1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 114 LTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHGKTLLPQYLGMYRITVESVQYYFVV 193
Cdd:cd17305  81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 194 MRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHDCvraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsieekreIYFIA 353
Cdd:cd17305 241 LLVGIHDC-------------------------------------------------------------------IYFMA 253
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 85724748 354 IIDVLTQYGVKKQAAKAAKTVKYGSNVdGISTCDPEQYAKRFLDFMDK 401
Cdd:cd17305 254 IIDILTHYGAKKRAAHAAKTVKHGAGA-EISTVKPEQYAKRFLEFISK 300
 
Name Accession Description Interval E-value
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
34-401 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: 545.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  34 PILSVFMWGINHTINELSHVNIPVMLLPDDFRAYSKIKVDNHLFNKENMPSHFKVKEYCPLVFRNLRERFGVDDVDYRES 113
Cdd:cd17305   1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 114 LTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHGKTLLPQYLGMYRITVESVQYYFVV 193
Cdd:cd17305  81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 194 MRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHDCvraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsieekreIYFIA 353
Cdd:cd17305 241 LLVGIHDC-------------------------------------------------------------------IYFMA 253
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 85724748 354 IIDVLTQYGVKKQAAKAAKTVKYGSNVdGISTCDPEQYAKRFLDFMDK 401
Cdd:cd17305 254 IIDILTHYGAKKRAAHAAKTVKHGAGA-EISTVKPEQYAKRFLEFISK 300
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
60-401 4.13e-101

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 303.92  E-value: 4.13e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748     60 LPDDFRAYSKIKVDNHLfNKENMPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPIQIDSSGKSGAQFYQS 135
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    136 YDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHgKTLLPQYLGMYRITVESVQY---YFVVMRNVFSSHLTIHKKFDLKG 212
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGTEkkiYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    213 STVDREASEKElEKNLPTFKDNDFIK-QKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDCVRAEEEALQG 291
Cdd:smart00330 159 STRGREADKKK-VKELPVLKDLDLVEmWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    292 dniltvgrSENSESEECDSGERWTYNTPPDSP---RGAQYKEVVYEVDIYDIPSIEEKREIYFIAIIDVLTQYGVKKQAA 368
Cdd:smart00330 238 --------PPVYGSDESPSSESSNGGKAPDITgnlLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLE 309
                          330       340       350
                   ....*....|....*....|....*....|...
gi 85724748    369 KAAKTVKYGSNVdgISTCDPEQYAKRFLDFMDK 401
Cdd:smart00330 310 HWVKSIGHDGKT--ISVVHPEQYAKRFRDFMDK 340
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
113-401 1.54e-80

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: 246.99  E-value: 1.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   113 SLTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVvERHGKTLLPQYLGMYRITVESVQYYFV 192
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHV-KQNPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   193 VMRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPT-FKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMD 271
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   272 YSLLVGVHDCVraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsiEEKREIYF 351
Cdd:pfam01504 160 YSLLLGIHDLD-------------------------------------------------------------EDGKEIYY 178
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 85724748   352 IAIIDVLTQYGVKKQAAKAAKTVKYgsNVDGISTCDPEQYAKRFLDFMDK 401
Cdd:pfam01504 179 LGIIDILTEYNLKKKLEHAWKSLVH--DGDSISAVPPKEYAERFLKFIEK 226
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
6-401 7.12e-48

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 173.87  E-value: 7.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    6 SSSSQPRILKKKHFR-VKHQK------VKLFRANEPILSVFMwGINHTINELShvniPVM---LLPDDFRAYSKIKVDnh 75
Cdd:PLN03185 315 SFSSTSRRAKRRQKKlVKEIKrpgetiIKGHRSYDLMLSLQL-GIRYTVGKIT----PIQrreVRPSDFGPRASFWMN-- 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   76 lFNKEN---MPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPI-QIDSSGKSGAQFYQSYDKFFIIKSLTS 147
Cdd:PLN03185 388 -FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALrELSSPGKSGSVFFLSQDDRFMIKTLRK 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  148 EEIERMHAFLKQYHPYvVERHGKTLLPQYLGMYRITVESVQ-YYFVVMRNVFSSHLTIHKKFDLKGSTVDREASEKELEK 226
Cdd:PLN03185 467 SEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQkFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDE 545
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  227 NlPTFKDNDfIKQKVKLDigKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHdcVRAEEE----ALQGDNILTVGRSEN 302
Cdd:PLN03185 546 N-TTLKDLD-LNYSFYLE--PSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRAPQHlrslLPYSRSITADGLEVV 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  303 SESEECDSgERWTYN---------------TPPDSPRGAQYKEVVY---EVDIY--------------------DIPSIE 344
Cdd:PLN03185 620 AEEDTIED-EELSYPeglvlvprgaddgstVPGPHIRGSRLRASAAgdeEVDLLlpgtarlqiqlgvnmparaeRIPGRE 698
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85724748  345 EK-----REIY----FIAIIDVLTQYGVKKQAAKAAKTVKYGSNvdGISTCDPEQYAKRFLDFMDK 401
Cdd:PLN03185 699 DKekqsfHEVYdvvlYLGIIDILQEYNMSKKIEHAYKSLQFDSL--SISAVDPTFYSKRFLEFIQK 762
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
71-403 1.05e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 135.46  E-value: 1.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  71 KVDNHLfnKENMPS---HFKVKEYCPLVFRNLRERFGVDdvdyrESLTR--SQPIQIDSS-GKSGAQFYQSYDKFFIIKS 144
Cdd:COG5253 320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-----EALVSllSRYILWESNgGKSGSFFLFTRDYKFIIKT 392
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 145 LTSEEIERMHAFLKQYHPYVVErHGKTLLPQYLGMYRITVESV-------QYYFVVMRNVFSSHLtIHKKFDLKGSTVDR 217
Cdd:COG5253 393 ISHSEHICFRPMIFEYYVHVLF-NPLTLLCKIFGFYRVKSRSSisssksrKIYFIVMENLFYPHG-IHRIFDLKGSMRNR 470
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 218 EASEK-ELEKNLPTFKDNDFIKQKVKLDIGKEaKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDcvraEEEALQGDNILT 296
Cdd:COG5253 471 HVERTgKSMSVLLDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD----EREEASVGLIID 545
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 297 VGRSENSeseecdsgerwtyntppdsprgaqykevvyeVDiydipsieekrEIYFIAIIDVLTQYGVKKQAAkaaktvky 376
Cdd:COG5253 546 FIRTRMT-------------------------------GD-----------KKLESGIKDKLTVGSFTKRKE-------- 575
                       330       340
                ....*....|....*....|....*..
gi 85724748 377 gsnvdgISTCDPEQYAKRFLDFMDKAI 403
Cdd:COG5253 576 ------PTAVTPRQYKNRFRKAMEAYI 596
 
Name Accession Description Interval E-value
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
34-401 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: 545.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  34 PILSVFMWGINHTINELSHVNIPVMLLPDDFRAYSKIKVDNHLFNKENMPSHFKVKEYCPLVFRNLRERFGVDDVDYRES 113
Cdd:cd17305   1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 114 LTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHGKTLLPQYLGMYRITVESVQYYFVV 193
Cdd:cd17305  81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 194 MRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHDCvraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsieekreIYFIA 353
Cdd:cd17305 241 LLVGIHDC-------------------------------------------------------------------IYFMA 253
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 85724748 354 IIDVLTQYGVKKQAAKAAKTVKYGSNVdGISTCDPEQYAKRFLDFMDK 401
Cdd:cd17305 254 IIDILTHYGAKKRAAHAAKTVKHGAGA-EISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
24-399 9.16e-151

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: 429.08  E-value: 9.16e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  24 QKVKLFRANEPILSVFMWGINHTINELSHVNIPVMLLPDDFRAYSKIKVDNHLFNKENMPSHFKVKEYCPLVFRNLRERF 103
Cdd:cd17310   2 QKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 104 GVDDVDYRESLTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHGKTLLPQYLGMYRIT 183
Cdd:cd17310  82 GIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 184 VESVQYYFVVMRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDL 263
Cdd:cd17310 162 VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEF 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 264 LTKLHIMDYSLLVGVHDCVraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsi 343
Cdd:cd17310 242 LAQLKIMDYSLLVGIHDVV------------------------------------------------------------- 260
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 85724748 344 eekreiYFIAIIDVLTQYGVKKQAAKAAKTVKYGSNVDgISTCDPEQYAKRFLDFM 399
Cdd:cd17310 261 ------YFMAIIDILTPYDAKKKAAHAAKTVKHGAGAE-ISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
25-399 1.52e-138

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: 397.81  E-value: 1.52e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  25 KVKLFRANEPILSVFMWGINHTINELSHVNIPVMLLPDDFRAYSKIKVDNHLFNKENMPSHFKVKEYCPLVFRNLRERFG 104
Cdd:cd17309   1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 105 VDDVDYRESLTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHGKTLLPQYLGMYRITV 184
Cdd:cd17309  81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 185 ESVQYYFVVMRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLL 264
Cdd:cd17309 161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 265 TKLHIMDYSLLVGVHDCVraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsie 344
Cdd:cd17309 241 AQLKLMDYSLLVGIHDVV-------------------------------------------------------------- 258
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 85724748 345 ekreiYFIAIIDVLTQYGVKKQAAKAAKTVKYGSNVDgISTCDPEQYAKRFLDFM 399
Cdd:cd17309 259 -----YFMAIIDILTHYDAKKKAAHAAKTVKHGAGAE-ISTVNPEQYSKRFLDFI 307
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
34-399 1.83e-122

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: 356.48  E-value: 1.83e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  34 PILSVFMWGINHTINELSHVNIPVMLLPDDFRAYSKIKVDNHLFNKENMPSHFKVKEYCPLVFRNLRERFGVDDVDYRES 113
Cdd:cd17311   1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 114 LTRSQPIQidSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHGKTLLPQYLGMYRITVESVQYYFVV 193
Cdd:cd17311  81 LTRSPPYS--ESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 194 MRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17311 159 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHDCVraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsieekreiYFIA 353
Cdd:cd17311 239 LLLGIHDVV-------------------------------------------------------------------YFMG 251
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 85724748 354 IIDVLTQYGVKKQAAKAAKTVKYGSNVDgISTCDPEQYAKRFLDFM 399
Cdd:cd17311 252 LIDILTQYDAKKKAAHAAKTVKHGAGAE-ISTVHPEQYAKRFLDFI 296
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
60-401 4.13e-101

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 303.92  E-value: 4.13e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748     60 LPDDFRAYSKIKVDNHLfNKENMPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPIQIDSSGKSGAQFYQS 135
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    136 YDKFFIIKSLTSEEIERMHAFLKQYHPYVVERHgKTLLPQYLGMYRITVESVQY---YFVVMRNVFSSHLTIHKKFDLKG 212
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGTEkkiYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    213 STVDREASEKElEKNLPTFKDNDFIK-QKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDCVRAEEEALQG 291
Cdd:smart00330 159 STRGREADKKK-VKELPVLKDLDLVEmWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    292 dniltvgrSENSESEECDSGERWTYNTPPDSP---RGAQYKEVVYEVDIYDIPSIEEKREIYFIAIIDVLTQYGVKKQAA 368
Cdd:smart00330 238 --------PPVYGSDESPSSESSNGGKAPDITgnlLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLE 309
                          330       340       350
                   ....*....|....*....|....*....|...
gi 85724748    369 KAAKTVKYGSNVdgISTCDPEQYAKRFLDFMDK 401
Cdd:smart00330 310 HWVKSIGHDGKT--ISVVHPEQYAKRFRDFMDK 340
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
85-401 6.98e-83

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: 254.03  E-value: 6.98e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  85 HFKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPIQID--SSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHP 162
Cdd:cd00139   2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 163 YVvERHGKTLLPQYLGMYRITVESVQY-YFVVMRNVFSSHLTIHKKFDLKGSTVDREAS-EKELEKNLPTFKDNDFIKQK 240
Cdd:cd00139  82 HI-KKNPNSLLTRFYGLYSIKLQKGKKvYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 241 VKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDCVraeeealqgdniltvgrsenseseecdsgerwtyntpp 320
Cdd:cd00139 161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRLV-------------------------------------- 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 321 dsprgaqykevvyevdiydipsieekreiYFIAIIDVLTQYGVKKQAAKAAKTVKYGSNvDGISTCDPEQYAKRFLDFMD 400
Cdd:cd00139 203 -----------------------------YYLGIIDILQEYNLRKKLERFLKSLLYGKD-SGISCVPPDEYAERFLKFME 252

                .
gi 85724748 401 K 401
Cdd:cd00139 253 S 253
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
113-401 1.54e-80

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: 246.99  E-value: 1.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   113 SLTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVvERHGKTLLPQYLGMYRITVESVQYYFV 192
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHV-KQNPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   193 VMRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPT-FKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMD 271
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   272 YSLLVGVHDCVraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevdiydipsiEEKREIYF 351
Cdd:pfam01504 160 YSLLLGIHDLD-------------------------------------------------------------EDGKEIYY 178
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 85724748   352 IAIIDVLTQYGVKKQAAKAAKTVKYgsNVDGISTCDPEQYAKRFLDFMDK 401
Cdd:pfam01504 179 LGIIDILTEYNLKKKLEHAWKSLVH--DGDSISAVPPKEYAERFLKFIEK 226
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
59-401 7.16e-74

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: 232.96  E-value: 7.16e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  59 LLPDDFRAYSKIKVDnHLFNKENMPSH--FKVKEYCPLVFRNLRERFGVDDVDYRESLTrSQPI--QIDSSGKSGAQFYQ 134
Cdd:cd17303  26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLT-GKYIlsELGSPGKSGSFFYF 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 135 SYDKFFIIKSLTSEEIERMHAFLKQYHPYVvERHGKTLLPQYLGMYRITV-ESVQYYFVVMRNVFSSHLTIHKKFDLKGS 213
Cdd:cd17303 104 SRDYRFIIKTIHHSEHKFLRKILPDYYNHV-KENPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGS 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 214 TVDREASEKELEKN-LPTFKDNDFIKQKVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDcvraeeeaLQGd 292
Cdd:cd17303 183 TVGRETPEDKLAKGpRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHD--------LDG- 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 293 niltvG-RSENSESEECDsgerwtyntppdsprgaqykevvyevdiydipsieekrEIYFIAIIDVLTQYGVKKQAAKAA 371
Cdd:cd17303 254 -----GfQATDENNEPGD--------------------------------------EIYYLGIIDILTPYNAKKKLEHFF 290
                       330       340       350
                ....*....|....*....|....*....|
gi 85724748 372 KTVkyGSNVDGISTCDPEQYAKRFLDFMDK 401
Cdd:cd17303 291 KSL--RHDRHTISAVPPKEYARRFLKFIED 318
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
81-401 9.63e-60

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: 196.36  E-value: 9.63e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  81 NMPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPI-QIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHA 155
Cdd:cd17302  48 TPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALrELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLR 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 156 FLKQYHPYVVErHGKTLLPQYLGMYRITVESVQ-YYFVVMRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPT-FKD 233
Cdd:cd17302 128 MLPAYYKHVKA-YENTLLTKFFGVHRVKPVGGRkVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTtLKD 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 234 NDfIKQKVKLDigKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDcvraeeealqgdniltvgRSENSESEecdsger 313
Cdd:cd17302 207 LD-LDFKFRLE--KGWRDALMRQIDADCAFLEALRIMDYSLLLGVHF------------------RAGDSTGE------- 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 314 wtyntppdsprgaqykevVYEVdiydipsieekreIYFIAIIDVLTQYGVKKQAAKAAKTVKYGSNvdGISTCDPEQYAK 393
Cdd:cd17302 259 ------------------PYDV-------------VLYFGIIDILQEYNISKKLEHAYKSLQYDPA--SISAVDPKLYSR 305

                ....*...
gi 85724748 394 RFLDFMDK 401
Cdd:cd17302 306 RFRDFIRK 313
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
42-403 5.32e-56

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: 187.07  E-value: 5.32e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  42 GINHTInELSHVNIPVMLLPDDFRayskiKVDNHLFNKE---NMPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESL 114
Cdd:cd17301  10 GIGHSV-GSLSSKPERDVLMQDFE-----VVESVFFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGIKPDDYLLSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 115 TRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYVVErHGKTLLPQYLGMYRITVESVQYYFVVM 194
Cdd:cd17301  84 CNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGKNIRFVVM 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 195 RNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVK-LDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17301 163 NNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEgILLEPDTYDALLKTIQRDCRVLESFKIMDYS 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHDCVRaeeealqgdniltvgrsenseseecdsgerwtynTPPDSPRGaqykevvyevdiydipsieeKREIYFIA 353
Cdd:cd17301 243 LLLGVHNLGG----------------------------------IPARNSKG--------------------ERLLLFIG 268
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 85724748 354 IIDVLTQYGVKKQAAKAAKTVKYGSnvDGISTCDPEQYAKRFLDFMDKAI 403
Cdd:cd17301 269 IIDILQSYRLKKKLEHTWKSVVHDG--DTVSVHRPSFYAERFQNFMANTV 316
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
6-401 7.12e-48

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 173.87  E-value: 7.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748    6 SSSSQPRILKKKHFR-VKHQK------VKLFRANEPILSVFMwGINHTINELShvniPVM---LLPDDFRAYSKIKVDnh 75
Cdd:PLN03185 315 SFSSTSRRAKRRQKKlVKEIKrpgetiIKGHRSYDLMLSLQL-GIRYTVGKIT----PIQrreVRPSDFGPRASFWMN-- 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748   76 lFNKEN---MPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPI-QIDSSGKSGAQFYQSYDKFFIIKSLTS 147
Cdd:PLN03185 388 -FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALrELSSPGKSGSVFFLSQDDRFMIKTLRK 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  148 EEIERMHAFLKQYHPYvVERHGKTLLPQYLGMYRITVESVQ-YYFVVMRNVFSSHLTIHKKFDLKGSTVDREASEKELEK 226
Cdd:PLN03185 467 SEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQkFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDE 545
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  227 NlPTFKDNDfIKQKVKLDigKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHdcVRAEEE----ALQGDNILTVGRSEN 302
Cdd:PLN03185 546 N-TTLKDLD-LNYSFYLE--PSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRAPQHlrslLPYSRSITADGLEVV 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  303 SESEECDSgERWTYN---------------TPPDSPRGAQYKEVVY---EVDIY--------------------DIPSIE 344
Cdd:PLN03185 620 AEEDTIED-EELSYPeglvlvprgaddgstVPGPHIRGSRLRASAAgdeEVDLLlpgtarlqiqlgvnmparaeRIPGRE 698
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85724748  345 EK-----REIY----FIAIIDVLTQYGVKKQAAKAAKTVKYGSNvdGISTCDPEQYAKRFLDFMDK 401
Cdd:PLN03185 699 DKekqsfHEVYdvvlYLGIIDILQEYNMSKKIEHAYKSLQFDSL--SISAVDPTFYSKRFLEFIQK 762
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
83-403 3.92e-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: 158.62  E-value: 3.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  83 PSH----FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLK 158
Cdd:cd17307  48 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 159 QYHpYVVERHGKTLLPQYLGMYRITVESVQYYFVVMRNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIK 238
Cdd:cd17307 128 GYY-MNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQ 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 239 QKVK-LDIGKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHdcvraeeeALQGdniltvgrsenseseecdsgerwtyn 317
Cdd:cd17307 207 DMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIH--------VLGG-------------------------- 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 318 TPPDSPRGaqykevvyevdiydipsieeKREIYFIAIIDVLTQYGVKKQAAKAAKTVKYGSnvDGISTCDPEQYAKRFLD 397
Cdd:cd17307 253 IPAKNHKG--------------------EKLLLFMGIIDILQSYRLMKKLEHSWKALVYDG--DTVSVHRPSFYADRFLK 310

                ....*.
gi 85724748 398 FMDKAI 403
Cdd:cd17307 311 FMNSRV 316
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
42-399 1.50e-40

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: 146.68  E-value: 1.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  42 GINHTINELSHVNIPVMLLPDDFrayskiKVDNHLFNKEN---MPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESL 114
Cdd:cd17306  13 GITHTVGSLSTKPERDVLMQDFY------VVESIFFPSEGsnlTPAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 115 TRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHpYVVERHGKTLLPQYLGMYRITVESVQYYFVVM 194
Cdd:cd17306  87 CSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYY-MNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 195 RNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVK-LDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17306 166 NNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDgLFLDSDMYNALCKTLQRDCLVLQSFKIMDYS 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHDCvraeeEALQGDNIltvgrsensESEECDSGerwtynTPPDSPRGaqykevvyevdiydipsieeKREIYFIA 353
Cdd:cd17306 246 LLVGIHNI-----DARRGGTI---------ETDDQMGG------IPARNSKG--------------------ERLLLYIG 285
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 85724748 354 IIDVLTQYGVKKQAAKAAKTVKYGSnvDGISTCDPEQYAKRFLDFM 399
Cdd:cd17306 286 IIDILQSYRFVKKLEHSWKALVHDG--DTVSVHRPGFYAERFQRFM 329
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
42-403 1.75e-40

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: 146.29  E-value: 1.75e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  42 GINHTINELSHVNIPVMLLPDDFrayskiKVDNHLFNKEN---MPSH----FKVKEYCPLVFRNLRERFGVDDVDYRESL 114
Cdd:cd17308  11 GIGYTVGNLSSKPERDVLMQDFY------VVESIFFPSEGsnlTPAHhypdFRFKTYAPVAFRYFRELFGIRPDDYLYSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 115 TRSQPIQIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHpYVVERHGKTLLPQYLGMYRITVESVQYYFVVM 194
Cdd:cd17308  85 CNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYY-MNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 195 RNVFSSHLTIHKKFDLKGSTVDREASEKELEKNLPTFKDNDFIKQKVK-LDIGKEAKDKLMDTLSNDVDLLTKLHIMDYS 273
Cdd:cd17308 164 NNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEgLMLDADTFSALVKTLQRDCLVLESFKIMDYS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 274 LLVGVHdcvraeeealqgdniltvgrsenseseecdsgerwtyntppdsprgaqykevvyevDIYDIPSIEEKRE--IYF 351
Cdd:cd17308 244 LLLGVH--------------------------------------------------------NIGGIPAVNGKGErlLLY 267
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 85724748 352 IAIIDVLTQYGVKKQAAKAAKTVKYGSnvDGISTCDPEQYAKRFLDFMDKAI 403
Cdd:cd17308 268 IGIIDILQSYRLIKKLEHTWKALVHDG--DTVSVHRPSFYAERFFKFMSNTV 317
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
71-403 1.05e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 135.46  E-value: 1.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  71 KVDNHLfnKENMPS---HFKVKEYCPLVFRNLRERFGVDdvdyrESLTR--SQPIQIDSS-GKSGAQFYQSYDKFFIIKS 144
Cdd:COG5253 320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-----EALVSllSRYILWESNgGKSGSFFLFTRDYKFIIKT 392
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 145 LTSEEIERMHAFLKQYHPYVVErHGKTLLPQYLGMYRITVESV-------QYYFVVMRNVFSSHLtIHKKFDLKGSTVDR 217
Cdd:COG5253 393 ISHSEHICFRPMIFEYYVHVLF-NPLTLLCKIFGFYRVKSRSSisssksrKIYFIVMENLFYPHG-IHRIFDLKGSMRNR 470
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 218 EASEK-ELEKNLPTFKDNDFIKQKVKLDIGKEaKDKLMDTLSNDVDLLTKLHIMDYSLLVGVHDcvraEEEALQGDNILT 296
Cdd:COG5253 471 HVERTgKSMSVLLDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDD----EREEASVGLIID 545
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 297 VGRSENSeseecdsgerwtyntppdsprgaqykevvyeVDiydipsieekrEIYFIAIIDVLTQYGVKKQAAkaaktvky 376
Cdd:COG5253 546 FIRTRMT-------------------------------GD-----------KKLESGIKDKLTVGSFTKRKE-------- 575
                       330       340
                ....*....|....*....|....*..
gi 85724748 377 gsnvdgISTCDPEQYAKRFLDFMDKAI 403
Cdd:COG5253 576 ------PTAVTPRQYKNRFRKAMEAYI 596
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
86-278 6.27e-34

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: 126.86  E-value: 6.27e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  86 FKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQPIQIdSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQYHPYV- 164
Cdd:cd17300   3 FTCTIYFAEQFHALRSLYCGGEDDFIRSLSRCVKWDA-SGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMa 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 165 -VERHGK-TLLPQYLGMYRITVESVQ------YYFVVMRNVFSSHlTIHKKFDLKGSTVDREASEKEleKNLPTFKDNDF 236
Cdd:cd17300  82 kALFHKRpSLLAKILGVYRISVKNSTtnktskQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAE--DEDSVLLDENF 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 85724748 237 IKQ--KVKLDIGKEAKDKLMDTLSNDVDLLTKLHIMDYSLLVGV 278
Cdd:cd17300 159 LEYtkGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
42-400 3.96e-30

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: 118.23  E-value: 3.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748  42 GINHTINELSHVNIPVMLLPDDFRAyskiKVDNHLFNKENmpshFKVKEYCPLVFRNLRERFGVDDVDYRESLTRSQP-I 120
Cdd:cd17304  13 GLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 121 QIDSSGKSGAQFYQSYDKFFIIKSLTSEEIERMHAFLKQY--HpyvVERHGKTLLPQYLGMYRITV-ESVQYYFVVMRNV 197
Cdd:cd17304  85 QFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYvqH---LENYPHSLLVKFLGVHSIKLpGKKKKYFIVMQSV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 198 FSSHLTIHKKFDLKGSTVDR-EASEKELEKNLPTFKDNDFIKQKVKLDigkEAKDKLMDTLSNDVDLLTKLHIMDYSLLV 276
Cdd:cd17304 162 FYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNFEGNSINLG---QQRSWFLRQVEIDTEFLKGLNVLDYSLLV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85724748 277 GVhdcvraeeEALQGDniltvgrsENseseecdsgERWTYNtppdsprgaqYKEVVYEVDiydipsIEEKReiYFIAIID 356
Cdd:cd17304 239 GF--------QPLHSD--------EN---------RRLLPN----------YKNALHVVD------GPEYR--YFVGIID 275
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 85724748 357 VLTQYGVKKQAAKAAKTVKYGSNvdGISTCDPEQYAKRFLDFMD 400
Cdd:cd17304 276 IFTVYGLRKRLEHLWKSLRYPGQ--SFSTVSPEKYARRFCQWVE 317
 
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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