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Conserved domains on  [gi|578801562|ref|XP_006711627|]
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phosphatidylinositol 4-phosphate 5-kinase type-1 alpha isoform X6 [Homo sapiens]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase type-1 alpha( domain architecture ID 13022706)

phosphatidylinositol 4-phosphate 5-kinase type-1 alpha catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
80-455 0e+00

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: 699.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  80 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 159
Cdd:cd17306    1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 160 DYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 239
Cdd:cd17306   81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 240 RIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFK 319
Cdd:cd17306  161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 320 IMDYSLLMSIHNIDhaqreplssetqysvdtrrpapqkalystamesiqgeARRGGTMETDDHMGGIPARNSKGERLLLY 399
Cdd:cd17306  241 IMDYSLLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLY 283
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801562 400 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 455
Cdd:cd17306  284 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 339
 
Name Accession Description Interval E-value
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
80-455 0e+00

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: 699.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  80 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 159
Cdd:cd17306    1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 160 DYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 239
Cdd:cd17306   81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 240 RIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFK 319
Cdd:cd17306  161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 320 IMDYSLLMSIHNIDhaqreplssetqysvdtrrpapqkalystamesiqgeARRGGTMETDDHMGGIPARNSKGERLLLY 399
Cdd:cd17306  241 IMDYSLLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLY 283
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801562 400 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 455
Cdd:cd17306  284 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 339
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
109-449 1.09e-168

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 481.88  E-value: 1.09e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   109 LMQDFYVVESIFFPSEGS-NLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSS 187
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   188 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGK---NIRIVVMNNLLPRSVKMHIKYDLKGST 264
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   265 YKRRASqKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSSET 344
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   345 QYSVDTRRPAPQKALYSTamESIQGEARRGGTMETDDHMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVH 424
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGH 317
                          330       340
                   ....*....|....*....|....*
gi 578801562   425 DGDTVSVHRPGFYAERFQRFMCNTV 449
Cdd:smart00330 318 DGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
164-448 9.16e-121

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: 355.24  E-value: 9.16e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  164 SLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVV 243
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  244 MNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPT-FKDLDFLQDIPDgLFLDADMYNALCKTLQRDCLVLQSFKIMD 322
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  323 YSLLMSIHNIDhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmggiparnsKGERLLLYIGI 402
Cdd:pfam01504 160 YSLLLGIHDLD----------------------------------------------------------EDGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578801562  403 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNT 448
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
67-450 8.20e-73

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 247.44  E-value: 8.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  67 RSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYNDFRFKTYAP 144
Cdd:PLN03185 332 KEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWmnFPKAGSQLTPSHQSEDFKWKDYCP 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 145 VAFRYFRELFGIRPDDYLYSLC-SEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLL 223
Cdd:PLN03185 412 MVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLI 491
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 224 PKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPlPTFKDLdflqDIPDGLFLDADMYN 302
Cdd:PLN03185 492 TKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN-TTLKDL----DLNYSFYLEPSWRD 566
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 303 ALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSS-------------ETQYSVDTRRPAPQKALYSTAMES--- 366
Cdd:PLN03185 567 ALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPysrsitadglevvAEEDTIEDEELSYPEGLVLVPRGAddg 646
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 367 -------IQG---EARRGGTMETDDHMGG-----------IPAR--------NSKGERL------LLYIGIIDILQSYRF 411
Cdd:PLN03185 647 stvpgphIRGsrlRASAAGDEEVDLLLPGtarlqiqlgvnMPARaeripgreDKEKQSFhevydvVLYLGIIDILQEYNM 726
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 578801562 412 VKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMcNTVF 450
Cdd:PLN03185 727 SKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
125-469 1.11e-35

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 141.24  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 125 GSNLTPAHHYnDFRFKTYAPVAFRYFRELFGIrpDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFL 204
Cdd:COG5253  325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 205 QKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-------AGGKNIRIVVMNNLLPRSvKMHIKYDLKGSTYKRRASQKER-EK 276
Cdd:COG5253  402 RPMIFEYYVHVLFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKsMS 480
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 277 PLPTFKDLDFLQDIPdgLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIdhaqreplssetqysvdtrrpapq 356
Cdd:COG5253  481 VLLDMNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE------------------------ 534
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 357 kaLYSTAMESIQGEARrggTMETDDhmggiparnskgerLLLYIGIIDILQSYRFVKKLEhswkalvhdgdtVSVHRPGF 436
Cdd:COG5253  535 --REEASVGLIIDFIR---TRMTGD--------------KKLESGIKDKLTVGSFTKRKE------------PTAVTPRQ 583
                        330       340       350
                 ....*....|....*....|....*....|...
gi 578801562 437 YAERFQRFMCNTVfkkiplKPSPSKKFRSGSSF 469
Cdd:COG5253  584 YKNRFRKAMEAYI------DPFPDKKTQEGFKT 610
 
Name Accession Description Interval E-value
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
80-455 0e+00

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: 699.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  80 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 159
Cdd:cd17306    1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 160 DYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 239
Cdd:cd17306   81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 240 RIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFK 319
Cdd:cd17306  161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 320 IMDYSLLMSIHNIDhaqreplssetqysvdtrrpapqkalystamesiqgeARRGGTMETDDHMGGIPARNSKGERLLLY 399
Cdd:cd17306  241 IMDYSLLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLY 283
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801562 400 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 455
Cdd:cd17306  284 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 339
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
83-453 0e+00

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: 673.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  83 SALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYL 162
Cdd:cd17301    1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 163 YSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIV 242
Cdd:cd17301   81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 243 VMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMD 322
Cdd:cd17301  161 VMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 323 YSLLMSIHNIdhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmGGIPARNSKGERLLLYIGI 402
Cdd:cd17301  241 YSLLLGVHNL---------------------------------------------------GGIPARNSKGERLLLFIGI 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578801562 403 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKI 453
Cdd:cd17301  270 IDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI 320
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
82-452 0e+00

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: 627.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  82 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDY 161
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 162 LYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRI 241
Cdd:cd17308   81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 242 VVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIM 321
Cdd:cd17308  161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 322 DYSLLMSIHNidhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhMGGIPARNSKGERLLLYIG 401
Cdd:cd17308  241 DYSLLLGVHN---------------------------------------------------IGGIPAVNGKGERLLLYIG 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578801562 402 IIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKK 452
Cdd:cd17308  270 IIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRK 320
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
83-453 0e+00

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: 625.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  83 SALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYL 162
Cdd:cd17307    1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 163 YSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIV 242
Cdd:cd17307   81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 243 VMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMD 322
Cdd:cd17307  161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 323 YSLLMSIHNIdhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmGGIPARNSKGERLLLYIGI 402
Cdd:cd17307  241 YSLLLGIHVL---------------------------------------------------GGIPAKNHKGEKLLLFMGI 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578801562 403 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKI 453
Cdd:cd17307  270 IDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKV 320
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
109-449 1.09e-168

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 481.88  E-value: 1.09e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   109 LMQDFYVVESIFFPSEGS-NLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSS 187
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   188 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGK---NIRIVVMNNLLPRSVKMHIKYDLKGST 264
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   265 YKRRASqKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSSET 344
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562   345 QYSVDTRRPAPQKALYSTamESIQGEARRGGTMETDDHMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVH 424
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGH 317
                          330       340
                   ....*....|....*....|....*
gi 578801562   425 DGDTVSVHRPGFYAERFQRFMCNTV 449
Cdd:smart00330 318 DGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
164-448 9.16e-121

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: 355.24  E-value: 9.16e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  164 SLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVV 243
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  244 MNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPT-FKDLDFLQDIPDgLFLDADMYNALCKTLQRDCLVLQSFKIMD 322
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  323 YSLLMSIHNIDhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmggiparnsKGERLLLYIGI 402
Cdd:pfam01504 160 YSLLLGIHDLD----------------------------------------------------------EDGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578801562  403 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNT 448
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
136-447 1.26e-94

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: 289.09  E-value: 1.26e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 136 DFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLI--ELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYM 213
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLreLKESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 214 NLNQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQ-KEREKPLPTFKDLDFLQDIp 291
Cdd:cd00139   82 HIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKeKEKKKGLKVLKDLDFLEKG- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 292 DGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHnidhaqreplssetqysvdtrrpapqkalystamesiqgea 371
Cdd:cd00139  161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH----------------------------------------- 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801562 372 rrggtmetddhmggiparnskgeRLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDT-VSVHRPGFYAERFQRFMCN 447
Cdd:cd00139  200 -----------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
90-447 2.54e-91

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: 283.03  E-value: 2.54e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  90 QLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYN-DFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-S 167
Cdd:cd17302    9 QLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSsDFKWKDYCPMVFRNLRELFGIDAADYMLSLCgD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 168 EPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCV-QAGGKNIRIVVMNN 246
Cdd:cd17302   89 DALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 247 LLPRSVKMHIKYDLKGSTYKRRASQKERE-KPLPTFKDLDFlqdipDGLF-LDADMYNALCKTLQRDCLVLQSFKIMDYS 324
Cdd:cd17302  169 LFCTELRIHRRFDLKGSTHGRTTGKPESEiDPNTTLKDLDL-----DFKFrLEKGWRDALMRQIDADCAFLEALRIMDYS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 325 LLMSIHNidhaqREPLSSETQYSVdtrrpapqkalystamesiqgearrggtmetddhmggiparnskgerlLLYIGIID 404
Cdd:cd17302  244 LLLGVHF-----RAGDSTGEPYDV------------------------------------------------VLYFGIID 270
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 578801562 405 ILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCN 447
Cdd:cd17302  271 ILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIRK 313
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
91-445 1.91e-87

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: 273.02  E-value: 1.91e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  91 LGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYnDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSE-P 169
Cdd:cd17303    9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKyI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 170 LIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLL 248
Cdd:cd17303   88 LSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKmPRGRKIHFVVMNNLF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 249 PRSVKMHIKYDLKGSTYKRRASQ-KEREKPLPTFKDLDFLQDiPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLM 327
Cdd:cd17303  168 PPHRDIHQTFDLKGSTVGRETPEdKLAKGPRATLKDLNWLRR-KRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 328 SIHNIDhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmGGIPARNSKGER--LLLYIGIIDI 405
Cdd:cd17303  247 GIHDLD--------------------------------------------------GGFQATDENNEPgdEIYYLGIIDI 276
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 578801562 406 LQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFM 445
Cdd:cd17303  277 LTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFI 316
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
67-450 8.20e-73

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 247.44  E-value: 8.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  67 RSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYNDFRFKTYAP 144
Cdd:PLN03185 332 KEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWmnFPKAGSQLTPSHQSEDFKWKDYCP 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 145 VAFRYFRELFGIRPDDYLYSLC-SEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLL 223
Cdd:PLN03185 412 MVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLI 491
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 224 PKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPlPTFKDLdflqDIPDGLFLDADMYN 302
Cdd:PLN03185 492 TKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN-TTLKDL----DLNYSFYLEPSWRD 566
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 303 ALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSS-------------ETQYSVDTRRPAPQKALYSTAMES--- 366
Cdd:PLN03185 567 ALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPysrsitadglevvAEEDTIEDEELSYPEGLVLVPRGAddg 646
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 367 -------IQG---EARRGGTMETDDHMGG-----------IPAR--------NSKGERL------LLYIGIIDILQSYRF 411
Cdd:PLN03185 647 stvpgphIRGsrlRASAAGDEEVDLLLPGtarlqiqlgvnMPARaeripgreDKEKQSFhevydvVLYLGIIDILQEYNM 726
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 578801562 412 VKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMcNTVF 450
Cdd:PLN03185 727 SKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
85-447 5.91e-68

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: 221.76  E-value: 5.91e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  85 LKGAIQLGITHTVGSLSTKPERDVLM-QDFYV-----VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFGIRP 158
Cdd:cd17305    2 LLSVFMWGINHSINELSHVPIPVMLMpDDFKAyskikVDNHLFNKE--NL-PSH----FKVKEYCPLVFRNLRERFGIDD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 159 DDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNL-NQNPRTLLPKFYGLYCVQAGGK 237
Cdd:cd17305   75 DDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRITVNGV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 238 NIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDgLFLDADMYNALCKTLQRDCLVLQS 317
Cdd:cd17305  155 ETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTK-IYIGDEAKAKLLETLKRDVEFLAK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 318 FKIMDYSLLMSIHNIdhaqreplssetqysvdtrrpapqkaLYstamesiqgearrggtmetddhmggiparnskgerll 397
Cdd:cd17305  234 LNLMDYSLLVGIHDC--------------------------IY------------------------------------- 250
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578801562 398 lYIGIIDILQSYRFVKKLEHSWKALVHDGDT-VSVHRPGFYAERFQRFMCN 447
Cdd:cd17305  251 -FMAIIDILTHYGAKKRAAHAAKTVKHGAGAeISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
82-447 1.77e-45

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: 162.53  E-value: 1.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  82 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFG 155
Cdd:cd17310   10 SEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NL-PSR----FKFKEYCPMVFRNLRERFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 156 IRPDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQA 234
Cdd:cd17310   83 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 235 GGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDiPDGLFLDADMYNALCKTLQRDCLV 314
Cdd:cd17310  163 DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 315 LQSFKIMDYSLLMSIHNIdhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmggiparnskge 394
Cdd:cd17310  242 LAQLKIMDYSLLVGIHDV-------------------------------------------------------------- 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578801562 395 rlLLYIGIIDILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 447
Cdd:cd17310  260 --VYFMAIIDILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
92-447 4.17e-41

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: 150.40  E-value: 4.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  92 GITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSL 165
Cdd:cd17311    9 GVNHSINELSQVPVPVMLLPDDFKanskikVNNHLFNRE--NL-PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVSL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 166 CSEPliELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQAGGKNIRIVVM 244
Cdd:cd17311   82 TRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKcHGNTLLPQFLGMYRLSVDNEDSYMLVM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 245 NNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIpDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYS 324
Cdd:cd17311  160 RNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKN-QKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 325 LLMSIHNIdhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmggiparnskgerlLLYIGIID 404
Cdd:cd17311  239 LLLGIHDV----------------------------------------------------------------VYFMGLID 254
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 578801562 405 ILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 447
Cdd:cd17311  255 ILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
92-447 1.19e-39

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: 146.66  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562  92 GITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSL 165
Cdd:cd17309   18 GVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 166 C-SEPLIELcSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQAGGKNIRIVV 243
Cdd:cd17309   91 TrSAPLAND-SQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 244 MNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDiPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDY 323
Cdd:cd17309  170 TRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIND-GQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDY 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 324 SLLMSIHNIdhaqreplssetqysvdtrrpapqkalystamesiqgearrggtmetddhmggiparnskgerlLLYIGII 403
Cdd:cd17309  249 SLLVGIHDV----------------------------------------------------------------VYFMAII 264
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 578801562 404 DILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 447
Cdd:cd17309  265 DILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
137-445 4.60e-37

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: 139.80  E-value: 4.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 137 FRFKTYAPVAFRYFRELFGIRPDDYLYSL-CSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNL 215
Cdd:cd17304   49 FEFRTYAGPVFATLRQSLGISEKEYQNSLsPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 216 NQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRAS-QKEREKPLPTFKDLDFLqdipdG 293
Cdd:cd17304  129 ENYPHSLLVKFLGVHSIKlPGKKKKYFIVMQSVFYPDERINERYDIKGCQVSRYTDpEPEGSQIIVVLKDLNFE-----G 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 294 LFLDADMYNA-LCKTLQRDCLVLQSFKIMDYSLLMS---IHNIDHaqreplssetqysvdtRRPAPQkalYSTAMESIQG 369
Cdd:cd17304  204 NSINLGQQRSwFLRQVEIDTEFLKGLNVLDYSLLVGfqpLHSDEN----------------RRLLPN---YKNALHVVDG 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801562 370 EARRggtmetddhmggiparnskgerllLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFM 445
Cdd:cd17304  265 PEYR------------------------YFVGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWV 316
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
125-469 1.11e-35

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 141.24  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 125 GSNLTPAHHYnDFRFKTYAPVAFRYFRELFGIrpDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFL 204
Cdd:COG5253  325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 205 QKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-------AGGKNIRIVVMNNLLPRSvKMHIKYDLKGSTYKRRASQKER-EK 276
Cdd:COG5253  402 RPMIFEYYVHVLFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKsMS 480
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 277 PLPTFKDLDFLQDIPdgLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIdhaqreplssetqysvdtrrpapq 356
Cdd:COG5253  481 VLLDMNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE------------------------ 534
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 357 kaLYSTAMESIQGEARrggTMETDDhmggiparnskgerLLLYIGIIDILQSYRFVKKLEhswkalvhdgdtVSVHRPGF 436
Cdd:COG5253  535 --REEASVGLIIDFIR---TRMTGD--------------KKLESGIKDKLTVGSFTKRKE------------PTAVTPRQ 583
                        330       340       350
                 ....*....|....*....|....*....|...
gi 578801562 437 YAERFQRFMCNTVfkkiplKPSPSKKFRSGSSF 469
Cdd:COG5253  584 YKNRFRKAMEAYI------DPFPDKKTQEGFKT 610
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
137-445 1.34e-35

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: 134.18  E-value: 1.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 137 FRFKTYAPVAFRYFRELFGIRPDDYLYSLCSeplielCSS-----GASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGY 211
Cdd:cd17300    3 FTCTIYFAEQFHALRSLYCGGEDDFIRSLSR------CVKwdasgGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 212 --YM--NLNQNPRTLLPKFYGLYCVQ----AGGKNIR--IVVMNNLLPRSvKMHIKYDLKGSTYKRRASQKEREKplPTF 281
Cdd:cd17300   77 feYMakALFHKRPSLLAKILGVYRISvknsTTNKTSKqdLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDED--SVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 282 KDLDFLQDIPDG-LFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSihnIDHAQREplssetqysvdtrrpapqkaly 360
Cdd:cd17300  154 LDENFLEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVG---IDEEKKE---------------------- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801562 361 stamesiqgearrggtmetddhmggiparnskgerllLYIGIIDILQSYRFVKKLEHSWKALVHDGD----TVsVHrPGF 436
Cdd:cd17300  209 -------------------------------------LVVGIIDYIRTYTWDKKLESWVKSLGILGGggepTV-IS-PEL 249

                 ....*....
gi 578801562 437 YAERFQRFM 445
Cdd:cd17300  250 YKKRFREAM 258
 
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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