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Conserved domains on  [gi|1937892641|ref|NP_001036086|]
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phosphatidylinositol 4-phosphate 5-kinase type-1 alpha [Rattus norvegicus]

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 ...
64-439 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: 690.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  64 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 143
Cdd:cd17306     1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 144 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 223
Cdd:cd17306    81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 224 RIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFK 303
Cdd:cd17306   161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 304 IMDYSLLMSIHNMDhaqrepmnsetqysidtrrpapqkalystamesiqgeARRGGTVETEDHMGGIPARNNKGERLLLY 383
Cdd:cd17306   241 IMDYSLLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLY 283
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937892641 384 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 439
Cdd:cd17306   284 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 339
 
Name Accession Description Interval E-value
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
64-439 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: 690.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  64 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 143
Cdd:cd17306     1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 144 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 223
Cdd:cd17306    81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 224 RIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFK 303
Cdd:cd17306   161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 304 IMDYSLLMSIHNMDhaqrepmnsetqysidtrrpapqkalystamesiqgeARRGGTVETEDHMGGIPARNNKGERLLLY 383
Cdd:cd17306   241 IMDYSLLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLY 283
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937892641 384 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 439
Cdd:cd17306   284 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 339
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
93-433 8.08e-165

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 471.48  E-value: 8.08e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641   93 LMQDFYVVESIFFPSEGS-NLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSS 171
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  172 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGK---NIRIVVMNNLLPRSVKMHMKYDLKGST 248
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  249 YKRRASqKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQREPMNSET 328
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  329 QYSIDTRRPAPQKALYSTamESIQGEARRGGTVETEDHMGGIPARNNKGERLLLYIGIIDILQSYRFVKKLEHSWKALVH 408
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGH 317
                          330       340
                   ....*....|....*....|....*
gi 1937892641  409 DGDTVSVHRPGFYAERFQRFMCNTV 433
Cdd:smart00330 318 DGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
148-432 7.14e-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: 354.85  E-value: 7.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 148 SLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVV 227
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 228 MNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPT-FKDLDFLQDIPDgLFLDADMYSALCKTLQRDCLVLQSFKIMD 306
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 307 YSLLMSIHNMDhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmggiparnnKGERLLLYIGI 386
Cdd:pfam01504 160 YSLLLGIHDLD----------------------------------------------------------EDGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1937892641 387 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNT 432
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
51-434 3.11e-73

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 247.82  E-value: 3.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  51 RSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYNDFRFKTYAP 128
Cdd:PLN03185  332 KEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWmnFPKAGSQLTPSHQSEDFKWKDYCP 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 129 VAFRYFRELFGIRPDDYLYSLC-SEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLL 207
Cdd:PLN03185  412 MVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLI 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 208 PKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTlPTFKDLdflqDIPDGLFLDADMYS 286
Cdd:PLN03185  492 TKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN-TTLKDL----DLNYSFYLEPSWRD 566
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 287 ALCKTLQRDCLVLQSFKIMDYSLLMSIH---------NMDHAQR---EPMNS-ETQYSIDTRRPAPQKALYSTAMES--- 350
Cdd:PLN03185  567 ALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSitaDGLEVvAEEDTIEDEELSYPEGLVLVPRGAddg 646
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 351 -------IQGEARRG-------------GTVETEDHMG-GIPARNNK------GER--------LLLYIGIIDILQSYRF 395
Cdd:PLN03185  647 stvpgphIRGSRLRAsaagdeevdlllpGTARLQIQLGvNMPARAERipgredKEKqsfhevydVVLYLGIIDILQEYNM 726
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1937892641 396 VKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMcNTVF 434
Cdd:PLN03185  727 SKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
109-450 1.85e-35

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 140.47  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 109 GSNLTPAHHYnDFRFKTYAPVAFRYFRELFGIrpDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFL 188
Cdd:COG5253   325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 189 QKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-------AGGKNIRIVVMNNLLPRSvKMHMKYDLKGSTYKRRASQKER-EK 260
Cdd:COG5253   402 RPMIFEYYVHVLFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKsMS 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 261 TLPTFKDLDFLQDIPdgLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMdhaqrepmnsetqysidtrrpapq 340
Cdd:COG5253   481 VLLDMNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE------------------------ 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 341 kaLYSTAMESIQGEARrggTVETEDhmggiparnnkgerLLLYIGIIDILQSYRFVKKLEhswkalvhdgdtVSVHRPGF 420
Cdd:COG5253   535 --REEASVGLIIDFIR---TRMTGD--------------KKLESGIKDKLTVGSFTKRKE------------PTAVTPRQ 583
                         330       340       350
                  ....*....|....*....|....*....|
gi 1937892641 421 YAERFQRFMCNTVfkkiplKPSPTKKFRSG 450
Cdd:COG5253   584 YKNRFRKAMEAYI------DPFPDKKTQEG 607
 
Name Accession Description Interval E-value
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
64-439 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: 690.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  64 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 143
Cdd:cd17306     1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 144 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 223
Cdd:cd17306    81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 224 RIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFK 303
Cdd:cd17306   161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 304 IMDYSLLMSIHNMDhaqrepmnsetqysidtrrpapqkalystamesiqgeARRGGTVETEDHMGGIPARNNKGERLLLY 383
Cdd:cd17306   241 IMDYSLLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLY 283
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937892641 384 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 439
Cdd:cd17306   284 IGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPL 339
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
67-437 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: 672.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  67 SALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYL 146
Cdd:cd17301     1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 147 YSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIV 226
Cdd:cd17301    81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 227 VMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMD 306
Cdd:cd17301   161 VMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 307 YSLLMSIHNmdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhMGGIPARNNKGERLLLYIGI 386
Cdd:cd17301   241 YSLLLGVHN---------------------------------------------------LGGIPARNSKGERLLLFIGI 269
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937892641 387 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKI 437
Cdd:cd17301   270 IDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI 320
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
66-436 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: 632.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  66 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDY 145
Cdd:cd17308     1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 146 LYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRI 225
Cdd:cd17308    81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 226 VVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIM 305
Cdd:cd17308   161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 306 DYSLLMSIHNmdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhMGGIPARNNKGERLLLYIG 385
Cdd:cd17308   241 DYSLLLGVHN---------------------------------------------------IGGIPAVNGKGERLLLYIG 269
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937892641 386 IIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKK 436
Cdd:cd17308   270 IIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRK 320
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
67-437 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: 629.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  67 SALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYL 146
Cdd:cd17307     1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 147 YSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIV 226
Cdd:cd17307    81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 227 VMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMD 306
Cdd:cd17307   161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 307 YSLLMSIHNmdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhMGGIPARNNKGERLLLYIGI 386
Cdd:cd17307   241 YSLLLGIHV---------------------------------------------------LGGIPAKNHKGEKLLLFMGI 269
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937892641 387 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKI 437
Cdd:cd17307   270 IDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKV 320
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
93-433 8.08e-165

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 471.48  E-value: 8.08e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641   93 LMQDFYVVESIFFPSEGS-NLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSS 171
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  172 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGK---NIRIVVMNNLLPRSVKMHMKYDLKGST 248
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  249 YKRRASqKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQREPMNSET 328
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  329 QYSIDTRRPAPQKALYSTamESIQGEARRGGTVETEDHMGGIPARNNKGERLLLYIGIIDILQSYRFVKKLEHSWKALVH 408
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGH 317
                          330       340
                   ....*....|....*....|....*
gi 1937892641  409 DGDTVSVHRPGFYAERFQRFMCNTV 433
Cdd:smart00330 318 DGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
148-432 7.14e-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: 354.85  E-value: 7.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 148 SLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVV 227
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 228 MNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPT-FKDLDFLQDIPDgLFLDADMYSALCKTLQRDCLVLQSFKIMD 306
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 307 YSLLMSIHNMDhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmggiparnnKGERLLLYIGI 386
Cdd:pfam01504 160 YSLLLGIHDLD----------------------------------------------------------EDGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1937892641 387 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNT 432
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
120-431 6.03e-95

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: 289.47  E-value: 6.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 120 DFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLI-ELSNS-GASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYM 197
Cdd:cd00139     2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLrELKESeGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 198 NLNQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQ-KEREKTLPTFKDLDFLQDIp 275
Cdd:cd00139    82 HIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKeKEKKKGLKVLKDLDFLEKG- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 276 DGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHnmdhaqrepmnsetqysidtrrpapqkalystamesiqgea 355
Cdd:cd00139   161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH----------------------------------------- 199
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937892641 356 rrggtvetedhmggiparnnkgeRLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDT-VSVHRPGFYAERFQRFMCN 431
Cdd:cd00139   200 -----------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
74-431 1.39e-89

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: 278.02  E-value: 1.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  74 QLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYN-DFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-S 151
Cdd:cd17302     9 QLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSsDFKWKDYCPMVFRNLRELFGIDAADYMLSLCgD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 152 EPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCV-QAGGKNIRIVVMNN 230
Cdd:cd17302    89 DALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 231 LLPRSVKMHMKYDLKGSTYKRRASQKERE---KTlpTFKDLDFlqdipDGLF-LDADMYSALCKTLQRDCLVLQSFKIMD 306
Cdd:cd17302   169 LFCTELRIHRRFDLKGSTHGRTTGKPESEidpNT--TLKDLDL-----DFKFrLEKGWRDALMRQIDADCAFLEALRIMD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 307 YSLLMSIHnmdhaqrepmnsetqysidTRRPAPqkalystamesiqgearrggTVETEDhmggiparnnkgerLLLYIGI 386
Cdd:cd17302   242 YSLLLGVH-------------------FRAGDS--------------------TGEPYD--------------VVLYFGI 268
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1937892641 387 IDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCN 431
Cdd:cd17302   269 IDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIRK 313
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
75-429 6.01e-86

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: 268.78  E-value: 6.01e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  75 LGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYnDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSE-P 153
Cdd:cd17303     9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKyI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 154 LIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLL 232
Cdd:cd17303    88 LSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKmPRGRKIHFVVMNNLF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 233 PRSVKMHMKYDLKGSTYKRRASQ-KEREKTLPTFKDLDFLQDiPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLM 311
Cdd:cd17303   168 PPHRDIHQTFDLKGSTVGRETPEdKLAKGPRATLKDLNWLRR-KRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 312 SIHNMDhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmGGIPARNNKGER--LLLYIGIIDI 389
Cdd:cd17303   247 GIHDLD--------------------------------------------------GGFQATDENNEPgdEIYYLGIIDI 276
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1937892641 390 LQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFM 429
Cdd:cd17303   277 LTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFI 316
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
51-434 3.11e-73

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 247.82  E-value: 3.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  51 RSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYNDFRFKTYAP 128
Cdd:PLN03185  332 KEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWmnFPKAGSQLTPSHQSEDFKWKDYCP 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 129 VAFRYFRELFGIRPDDYLYSLC-SEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLL 207
Cdd:PLN03185  412 MVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLI 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 208 PKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTlPTFKDLdflqDIPDGLFLDADMYS 286
Cdd:PLN03185  492 TKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN-TTLKDL----DLNYSFYLEPSWRD 566
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 287 ALCKTLQRDCLVLQSFKIMDYSLLMSIH---------NMDHAQR---EPMNS-ETQYSIDTRRPAPQKALYSTAMES--- 350
Cdd:PLN03185  567 ALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSitaDGLEVvAEEDTIEDEELSYPEGLVLVPRGAddg 646
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 351 -------IQGEARRG-------------GTVETEDHMG-GIPARNNK------GER--------LLLYIGIIDILQSYRF 395
Cdd:PLN03185  647 stvpgphIRGSRLRAsaagdeevdlllpGTARLQIQLGvNMPARAERipgredKEKqsfhevydVVLYLGIIDILQEYNM 726
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1937892641 396 VKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMcNTVF 434
Cdd:PLN03185  727 SKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
69-431 1.55e-67

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: 220.22  E-value: 1.55e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  69 LKGAIQLGITHTVGSLSTKPERDVLM-QDFYV-----VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFGIRP 142
Cdd:cd17305     2 LLSVFMWGINHSINELSHVPIPVMLMpDDFKAyskikVDNHLFNKE--NL-PSH----FKVKEYCPLVFRNLRERFGIDD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 143 DDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNL-NQNPRTLLPKFYGLYCVQAGGK 221
Cdd:cd17305    75 DDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRITVNGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 222 NIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDgLFLDADMYSALCKTLQRDCLVLQS 301
Cdd:cd17305   155 ETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTK-IYIGDEAKAKLLETLKRDVEFLAK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 302 FKIMDYSLLMSIHnmdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmggiparnnkgeRLL 381
Cdd:cd17305   234 LNLMDYSLLVGIH----------------------------------------------------------------DCI 249
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937892641 382 LYIGIIDILQSYRFVKKLEHSWKALVHDGDT-VSVHRPGFYAERFQRFMCN 431
Cdd:cd17305   250 YFMAIIDILTHYGAKKRAAHAAKTVKHGAGAeISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
66-431 5.81e-46

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: 163.68  E-value: 5.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  66 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFG 139
Cdd:cd17310    10 SEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NL-PSR----FKFKEYCPMVFRNLRERFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 140 IRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQA 218
Cdd:cd17310    83 IDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 219 GGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDiPDGLFLDADMYSALCKTLQRDCLV 298
Cdd:cd17310   163 DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 299 LQSFKIMDYSLLMSIHNmdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmggiparnnkge 378
Cdd:cd17310   242 LAQLKIMDYSLLVGIHD--------------------------------------------------------------- 258
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937892641 379 rLLLYIGIIDILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 431
Cdd:cd17310   259 -VVYFMAIIDILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
76-431 8.22e-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: 149.25  E-value: 8.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  76 GITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSL 149
Cdd:cd17311     9 GVNHSINELSQVPVPVMLLPDDFKanskikVNNHLFNRE--NL-PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 150 CSEPliELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQAGGKNIRIVVM 228
Cdd:cd17311    82 TRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKcHGNTLLPQFLGMYRLSVDNEDSYMLVM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 229 NNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIpDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYS 308
Cdd:cd17311   160 RNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKN-QKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 309 LLMSIHNMdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmggiparnnkgerlLLYIGIID 388
Cdd:cd17311   239 LLLGIHDV----------------------------------------------------------------VYFMGLID 254
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1937892641 389 ILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 431
Cdd:cd17311   255 ILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
76-431 1.44e-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: 146.28  E-value: 1.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641  76 GITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhyndFRFKTYAPVAFRYFRELFGIRPDDYLYSL 149
Cdd:cd17309    18 GVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 150 C-SEPLIELSNsGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQAGGKNIRIVV 227
Cdd:cd17309    91 TrSAPLANDSQ-ARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 228 MNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDiPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDY 307
Cdd:cd17309   170 TRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIND-GQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDY 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 308 SLLMSIHNmdhaqrepmnsetqysidtrrpapqkalystamesiqgearrggtvetedhmggiparnnkgerLLLYIGII 387
Cdd:cd17309   249 SLLVGIHD----------------------------------------------------------------VVYFMAII 264
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1937892641 388 DILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 431
Cdd:cd17309   265 DILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
121-429 3.91e-37

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: 138.03  E-value: 3.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 121 FRFKTYAPVAFRYFRELFGIRPDDYLYSLC-SEPLIelSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGY--YM 197
Cdd:cd17300     3 FTCTIYFAEQFHALRSLYCGGEDDFIRSLSrCVKWD--ASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfeYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 198 --NLNQNPRTLLPKFYGLYCVQ----AGGKNIR--IVVMNNLLPRSvKMHMKYDLKGSTYKRRASQKERE-KTLPtfkDL 268
Cdd:cd17300    81 akALFHKRPSLLAKILGVYRISvknsTTNKTSKqdLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDEdSVLL---DE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 269 DFLQDIPDG-LFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIhnmDHAQREpmnsetqysidtrrpapqkalysta 347
Cdd:cd17300   157 NFLEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI---DEEKKE------------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 348 mesiqgearrggtvetedhmggiparnnkgerllLYIGIIDILQSYRFVKKLEHSWKALVHDGD----TVsVHrPGFYAE 423
Cdd:cd17300   209 ----------------------------------LVVGIIDYIRTYTWDKKLESWVKSLGILGGggepTV-IS-PELYKK 252

                  ....*.
gi 1937892641 424 RFQRFM 429
Cdd:cd17300   253 RFREAM 258
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
121-429 6.37e-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: 139.42  E-value: 6.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 121 FRFKTYAPVAFRYFRELFGIRPDDYLYSL-CSEPLIE-LSNSgASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMN 198
Cdd:cd17304    49 FEFRTYAGPVFATLRQSLGISEKEYQNSLsPDEPYLQfISNS-KSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 199 LNQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRAS-QKEREKTLPTFKDLDFLQDIpd 276
Cdd:cd17304   128 LENYPHSLLVKFLGVHSIKlPGKKKKYFIVMQSVFYPDERINERYDIKGCQVSRYTDpEPEGSQIIVVLKDLNFEGNS-- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 277 gLFLDaDMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMdhaqrepmnsetqYSIDTRRPAPQkalYSTAMESIQGEAR 356
Cdd:cd17304   206 -INLG-QQRSWFLRQVEIDTEFLKGLNVLDYSLLVGFQPL-------------HSDENRRLLPN---YKNALHVVDGPEY 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937892641 357 RggtvetedhmggiparnnkgerllLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFM 429
Cdd:cd17304   268 R------------------------YFVGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWV 316
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
109-450 1.85e-35

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 140.47  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 109 GSNLTPAHHYnDFRFKTYAPVAFRYFRELFGIrpDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFL 188
Cdd:COG5253   325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 189 QKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-------AGGKNIRIVVMNNLLPRSvKMHMKYDLKGSTYKRRASQKER-EK 260
Cdd:COG5253   402 RPMIFEYYVHVLFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKsMS 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 261 TLPTFKDLDFLQDIPdgLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMdhaqrepmnsetqysidtrrpapq 340
Cdd:COG5253   481 VLLDMNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE------------------------ 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937892641 341 kaLYSTAMESIQGEARrggTVETEDhmggiparnnkgerLLLYIGIIDILQSYRFVKKLEhswkalvhdgdtVSVHRPGF 420
Cdd:COG5253   535 --REEASVGLIIDFIR---TRMTGD--------------KKLESGIKDKLTVGSFTKRKE------------PTAVTPRQ 583
                         330       340       350
                  ....*....|....*....|....*....|
gi 1937892641 421 YAERFQRFMCNTVfkkiplKPSPTKKFRSG 450
Cdd:COG5253   584 YKNRFRKAMEAYI------DPFPDKKTQEG 607
 
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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