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Conserved domains on  [gi|1834199175|ref|NP_001369113|]
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phosphatidylinositol 4-phosphate 5-kinase 59B, isoform J [Drosophila melanogaster]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase type-1( domain architecture ID 13022639)

phosphatidylinositol 4-phosphate 5-kinase type-1 phosphorylates the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes

CATH:  3.30.800.10
EC:  2.7.1.68
PubMed:  9535851
SCOP:  4002087

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
78-473 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: 660.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  78 SQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFM 157
Cdd:cd17301     1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 158 MSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIRL 237
Cdd:cd17301    81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQ-SGGKNIRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 238 VVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIM 317
Cdd:cd17301   160 VVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHNLdvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidd 397
Cdd:cd17301   240 DYSLLLGVHNL--------------------------------------------------------------------- 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199175 398 eedvppGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKI 473
Cdd:cd17301   251 ------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI 320
 
Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
78-473 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: 660.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  78 SQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFM 157
Cdd:cd17301     1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 158 MSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIRL 237
Cdd:cd17301    81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQ-SGGKNIRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 238 VVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIM 317
Cdd:cd17301   160 VVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHNLdvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidd 397
Cdd:cd17301   240 DYSLLLGVHNL--------------------------------------------------------------------- 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199175 398 eedvppGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKI 473
Cdd:cd17301   251 ------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI 320
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
104-469 8.49e-146

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 434.50  E-value: 8.49e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  104 LMMDFWEIESITFPPEGSS-LTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPLRELSNPGASGSIFYLTT 182
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHLeLTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  183 DDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSN--AKNIRLVVMNNLLPSSVKMHLKYDLKGST 260
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgtEKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  261 FKRKANKaERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNLDVALKEKqseqr 340
Cdd:smart00330 161 RGREADK-KKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREE----- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  341 kplraplAEDSDVDADDPLDGDaatgisrnksvnrqRLVAHSTAMESIQAESEPIDDEEDVPPGGIPARSEKGERLLLYI 420
Cdd:smart00330 235 -------IELPPVYGSDESPSS--------------ESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYL 293
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1834199175  421 GIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTV 469
Cdd:smart00330 294 GIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
159-468 6.22e-114

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: 347.53  E-value: 6.22e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 159 SMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIRLV 238
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVK-PGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 239 VMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPT-YKDLDFMEQHPNgIFLEAETYAALIKTIQRDCTVLESFKIM 317
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHNLDvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidd 397
Cdd:pfam01504 159 DYSLLLGIHDLD-------------------------------------------------------------------- 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834199175 398 eedvppggiparseKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKT 468
Cdd:pfam01504 171 --------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
42-470 6.62e-84

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 285.57  E-value: 6.62e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  42 LGNRPNRASSKADKERKIGHRRVGEGGEITYKKIQTSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESI--TFPPE 119
Cdd:PLN03185  312 LNNSFSSTSRRAKRRQKKLVKEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFwmNFPKA 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 120 GSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMC-TSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEF 198
Cdd:PLN03185  392 GSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKV 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 199 LQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAErAKKSPTYK 278
Cdd:PLN03185  472 LLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVE-IDENTTLK 550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 279 DLDFMEQhpngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVH-----NLDVALKEKQSEQRKPLRAPLAEDS-D 352
Cdd:PLN03185  551 DLDLNYS----FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqHLRSLLPYSRSITADGLEVVAEEDTiE 626
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 353 VDADDPLDGDAatgisrnksvnrqrLVAHSTAMES----IQAESEPI------DDEED-VPPG----------GIPARSE 411
Cdd:PLN03185  627 DEELSYPEGLV--------------LVPRGADDGStvpgPHIRGSRLrasaagDEEVDlLLPGtarlqiqlgvNMPARAE 692
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834199175 412 K------GER--------LLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMaKTVF 470
Cdd:PLN03185  693 RipgredKEKqsfhevydVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
47-328 4.91e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 132.76  E-value: 4.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  47 NRASSKADKERKIGHRRVgEGGEITYkkiQTSQIMGSiqlGIQHTVGslaskpkrdllmmdfwEIESITFPPEGSSL--- 123
Cdd:COG5253   272 RLRDSETMDERLLNGMPL-EGGHRNP---QESYNMLT---GIRVTLS----------------RIEEIMIKKTDTHLneq 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 124 TPAHHYsEFRYKIYAPIAFRYFRDLFGIQPDdFMMSMCTSPLRElSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLL 203
Cdd:COG5253   329 FEEGLY-EFSCKDYFPEVFRELRALCGCDEA-LVSLLSRYILWE-SNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMI 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 204 PGYYMNLNQNPRTLLPKFFGLYCLQ------TSNAKNIRLVVMNNLLPSSvKMHLKYDLKGSTFKRKANKAERAKKS-PT 276
Cdd:COG5253   406 FEYYVHVLFNPLTLLCKIFGFYRVKsrssisSSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKSMSVlLD 484
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1834199175 277 YKDLDFMEQHPngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNL 328
Cdd:COG5253   485 MNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
 
Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
78-473 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: 660.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  78 SQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFM 157
Cdd:cd17301     1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 158 MSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIRL 237
Cdd:cd17301    81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQ-SGGKNIRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 238 VVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIM 317
Cdd:cd17301   160 VVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHNLdvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidd 397
Cdd:cd17301   240 DYSLLLGVHNL--------------------------------------------------------------------- 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199175 398 eedvppGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKI 473
Cdd:cd17301   251 ------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI 320
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
77-475 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: 532.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  77 TSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDF 156
Cdd:cd17308     1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 157 MMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIR 236
Cdd:cd17308    81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGKNIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 237 LVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKI 316
Cdd:cd17308   160 VVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 317 MDYSLLLGVHNLdvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepid 396
Cdd:cd17308   240 MDYSLLLGVHNI-------------------------------------------------------------------- 251
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834199175 397 deedvppGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKIPS 475
Cdd:cd17308   252 -------GGIPAVNGKGERLLLYIGIIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKSSS 323
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
78-473 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: 530.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  78 SQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFM 157
Cdd:cd17307     1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 158 MSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIRL 237
Cdd:cd17307    81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQ-SGGINIRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 238 VVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIM 317
Cdd:cd17307   160 VVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHNLdvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidd 397
Cdd:cd17307   240 DYSLLLGIHVL--------------------------------------------------------------------- 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199175 398 eedvppGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKI 473
Cdd:cd17307   251 ------GGIPAKNHKGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKV 320
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
77-474 3.98e-174

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: 507.23  E-value: 3.98e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  77 TSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDF 156
Cdd:cd17306     3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 157 MMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIR 236
Cdd:cd17306    83 LYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-AGGKNIR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 237 LVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKI 316
Cdd:cd17306   162 IVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFKI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 317 MDYSLLLGVHNLDValkekqseqrkplraplAEDSDVDADDPLdgdaatgisrnksvnrqrlvahstamesiqaesepid 396
Cdd:cd17306   242 MDYSLLVGIHNIDA-----------------RRGGTIETDDQM------------------------------------- 267
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834199175 397 deedvppGGIPARSEKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTVFRKIP 474
Cdd:cd17306   268 -------GGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIP 338
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
104-469 8.49e-146

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 434.50  E-value: 8.49e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  104 LMMDFWEIESITFPPEGSS-LTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPLRELSNPGASGSIFYLTT 182
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHLeLTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  183 DDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSN--AKNIRLVVMNNLLPSSVKMHLKYDLKGST 260
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgtEKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  261 FKRKANKaERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNLDVALKEKqseqr 340
Cdd:smart00330 161 RGREADK-KKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREE----- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  341 kplraplAEDSDVDADDPLDGDaatgisrnksvnrqRLVAHSTAMESIQAESEPIDDEEDVPPGGIPARSEKGERLLLYI 420
Cdd:smart00330 235 -------IELPPVYGSDESPSS--------------ESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYL 293
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1834199175  421 GIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTV 469
Cdd:smart00330 294 GIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
159-468 6.22e-114

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: 347.53  E-value: 6.22e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 159 SMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQtSNAKNIRLV 238
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVK-PGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 239 VMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPT-YKDLDFMEQHPNgIFLEAETYAALIKTIQRDCTVLESFKIM 317
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHNLDvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidd 397
Cdd:pfam01504 159 DYSLLLGIHDLD-------------------------------------------------------------------- 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834199175 398 eedvppggiparseKGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKT 468
Cdd:pfam01504 171 --------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
81-467 5.10e-99

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: 311.92  E-value: 5.10e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  81 MGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYS-EFRYKIYAPIAFRYFRDLFGIQPDDFMMS 159
Cdd:cd17302     5 MLNLQLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSsDFKWKDYCPMVFRNLRELFGIDAADYMLS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 160 MC-TSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLV 238
Cdd:cd17302    85 LCgDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVKPVGGRKVRFV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 239 VMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPT-YKDLDFmeqhpNGIF-LEAETYAALIKTIQRDCTVLESFKI 316
Cdd:cd17302   165 VMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTtLKDLDL-----DFKFrLEKGWRDALMRQIDADCAFLEALRI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 317 MDYSLLLGVHnldvalkekqseqrkpLRAPlaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiQAESEPid 396
Cdd:cd17302   240 MDYSLLLGVH----------------FRAG------------------------------------------DSTGEP-- 259
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834199175 397 deEDVppggiparsekgerlLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAK 467
Cdd:cd17302   260 --YDV---------------VLYFGIIDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIRK 313
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
131-467 7.00e-90

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: 285.24  E-value: 7.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 131 EFRYKIYAPIAFRYFRDLFGIQPDDFMMSMC-TSPLRELSN-PGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYM 208
Cdd:cd00139     2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSpEENLRELKEsEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 209 NLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKS-PTYKDLDFMEQHP 287
Cdd:cd00139    82 HIKKNPNSLLTRFYGLYSIKLQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEKEKKKGlKVLKDLDFLEKGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 288 nGIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHnldvalkekqseqrkplraplaedsdvdaddpldgdaatgi 367
Cdd:cd00139   162 -KIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH----------------------------------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 368 srnksvnrqrlvahstamesiqaesepiddeedvppggiparsekgeRLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGE 447
Cdd:cd00139   200 -----------------------------------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKD 232
                         330       340
                  ....*....|....*....|.
gi 1834199175 448 T-VSVCRPSFYAQRFQNFMAK 467
Cdd:cd00139   233 SgISCVPPDEYAERFLKFMES 253
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
42-470 6.62e-84

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 285.57  E-value: 6.62e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  42 LGNRPNRASSKADKERKIGHRRVGEGGEITYKKIQTSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESI--TFPPE 119
Cdd:PLN03185  312 LNNSFSSTSRRAKRRQKKLVKEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFwmNFPKA 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 120 GSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMC-TSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEF 198
Cdd:PLN03185  392 GSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKV 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 199 LQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAErAKKSPTYK 278
Cdd:PLN03185  472 LLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVE-IDENTTLK 550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 279 DLDFMEQhpngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVH-----NLDVALKEKQSEQRKPLRAPLAEDS-D 352
Cdd:PLN03185  551 DLDLNYS----FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqHLRSLLPYSRSITADGLEVVAEEDTiE 626
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 353 VDADDPLDGDAatgisrnksvnrqrLVAHSTAMES----IQAESEPI------DDEED-VPPG----------GIPARSE 411
Cdd:PLN03185  627 DEELSYPEGLV--------------LVPRGADDGStvpgPHIRGSRLrasaagDEEVDlLLPGtarlqiqlgvNMPARAE 692
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834199175 412 K------GER--------LLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMaKTVF 470
Cdd:PLN03185  693 RipgredKEKqsfhevydVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
86-467 2.12e-82

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: 268.01  E-value: 2.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  86 LGIQHTVGSLASKPKRDLLMMDFWEIESITFPPEGSSLTPAHHYsEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMcTSP- 164
Cdd:cd17303     9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSL-TGKy 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 165 -LRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNL 243
Cdd:cd17303    87 iLSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKMPRGRKIHFVVMNNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 244 LPSSVKMHLKYDLKGSTFKRKANKAE-RAKKSPTYKDLDFMEQHPNgIFLEAETYAALIKTIQRDCTVLESFKIMDYSLL 322
Cdd:cd17303   167 FPPHRDIHQTFDLKGSTVGRETPEDKlAKGPRATLKDLNWLRRKRK-LALGPEKRKQFLTQLKRDVEFLASLNIMDYSLL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 323 LGVHNLDvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepiddeedvp 402
Cdd:cd17303   246 VGIHDLD------------------------------------------------------------------------- 252
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199175 403 pGGIPARSEKGER--LLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAK 467
Cdd:cd17303   253 -GGFQATDENNEPgdEIYYLGIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
80-467 1.77e-57

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: 199.42  E-value: 1.77e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  80 IMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESITfppegssLTPAHHY------SEFRYKIYAPIAFRYFRDLFGIQP 153
Cdd:cd17305     2 LLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKI-------KVDNHLFnkenlpSHFKVKEYCPLVFRNLRERFGIDD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 154 DDFMMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNL-NQNPRTLLPKFFGLYCLqTSNA 232
Cdd:cd17305    75 DDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRI-TVNG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 233 KNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNgIFLEAETYAALIKTIQRDCTVLE 312
Cdd:cd17305   154 VETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTK-IYIGDEAKAKLLETLKRDVEFLA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 313 SFKIMDYSLLLGVHnldvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaes 392
Cdd:cd17305   233 KLNLMDYSLLVGIH------------------------------------------------------------------ 246
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199175 393 epiddeedvppggiparsekgeRLLLYIGIIDILQSYRLKKKLEHTFKSIIHD-GETVSVCRPSFYAQRFQNFMAK 467
Cdd:cd17305   247 ----------------------DCIYFMAIIDILTHYGAKKRAAHAAKTVKHGaGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
80-466 1.20e-38

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: 146.35  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  80 IMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESiTFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMS 159
Cdd:cd17310    13 ILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYS-KIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 160 MCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQ-NPRTLLPKFFGLYCLqTSNAKNIRLV 238
Cdd:cd17310    92 VTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRL-TVDGVETYMV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 239 VMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNgIFLEAETYAALIKTIQRDCTVLESFKIMD 318
Cdd:cd17310   171 VTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQK-LHVGEESKKNFLEKLKRDVEFLAQLKIMD 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 319 YSLLLGVHNldvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaesepidde 398
Cdd:cd17310   250 YSLLVGIHD----------------------------------------------------------------------- 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834199175 399 edvppggiparsekgerLLLYIGIIDILQSYRLKKKLEHTFKSIIHD-GETVSVCRPSFYAQRFQNFMA 466
Cdd:cd17310   259 -----------------VVYFMAIIDILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMS 310
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
130-467 2.37e-38

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: 143.81  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 130 SEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSpLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGY--Y 207
Cdd:cd17300     1 TKFTCTIYFAEQFHALRSLYCGGEDDFIRSLSRC-VKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfeY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 208 M--NLNQNPRTLLPKFFGLY-----CLQTSNAKNIRLVVMNNLLPSSvKMHLKYDLKGSTFKRKANKAEraKKSPTYKDL 280
Cdd:cd17300    80 MakALFHKRPSLLAKILGVYrisvkNSTTNKTSKQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAE--DEDSVLLDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 281 DFMEQHPNG-IFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGvhnldvalkekqseqrkplraplaedsdvdaddpl 359
Cdd:cd17300   157 NFLEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVG----------------------------------- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 360 dgdaatgisrnksvnrqrlvahstamesiqaesepIDDEEDVppggiparsekgerllLYIGIIDILQSYRLKKKLEHTF 439
Cdd:cd17300   202 -----------------------------------IDEEKKE----------------LVVGIIDYIRTYTWDKKLESWV 230
                         330       340       350
                  ....*....|....*....|....*....|
gi 1834199175 440 KSIIHDGETVS--VCRPSFYAQRFQNFMAK 467
Cdd:cd17300   231 KSLGILGGGGEptVISPELYKKRFREAMDK 260
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
130-466 1.92e-34

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: 133.95  E-value: 1.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 130 SEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMN 209
Cdd:cd17309    60 SHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 210 LNQ-NPRTLLPKFFGLYCLqTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPN 288
Cdd:cd17309   140 IVEcHGNTLLPQFLGMYRL-TVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQK 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 289 gIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNldvalkekqseqrkplraplaedsdvdaddpldgdaatgis 368
Cdd:cd17309   219 -IYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHD----------------------------------------- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 369 rnksvnrqrlvahstamesiqaesepiddeedvppggiparsekgerLLLYIGIIDILQSYRLKKKLEHTFKSIIHD-GE 447
Cdd:cd17309   257 -----------------------------------------------VVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGA 289
                         330
                  ....*....|....*....
gi 1834199175 448 TVSVCRPSFYAQRFQNFMA 466
Cdd:cd17309   290 EISTVNPEQYSKRFLDFIT 308
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
130-328 2.76e-32

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: 127.67  E-value: 2.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 130 SEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPlrELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMN 209
Cdd:cd17311    51 SHFKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQY 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 210 LNQ-NPRTLLPKFFGLYCLQTSNaKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPN 288
Cdd:cd17311   129 IVKcHGNTLLPQFLGMYRLSVDN-EDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQK 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1834199175 289 gIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNL 328
Cdd:cd17311   208 -VYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV 246
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
47-328 4.91e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 132.76  E-value: 4.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  47 NRASSKADKERKIGHRRVgEGGEITYkkiQTSQIMGSiqlGIQHTVGslaskpkrdllmmdfwEIESITFPPEGSSL--- 123
Cdd:COG5253   272 RLRDSETMDERLLNGMPL-EGGHRNP---QESYNMLT---GIRVTLS----------------RIEEIMIKKTDTHLneq 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 124 TPAHHYsEFRYKIYAPIAFRYFRDLFGIQPDdFMMSMCTSPLRElSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLL 203
Cdd:COG5253   329 FEEGLY-EFSCKDYFPEVFRELRALCGCDEA-LVSLLSRYILWE-SNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMI 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 204 PGYYMNLNQNPRTLLPKFFGLYCLQ------TSNAKNIRLVVMNNLLPSSvKMHLKYDLKGSTFKRKANKAERAKKS-PT 276
Cdd:COG5253   406 FEYYVHVLFNPLTLLCKIFGFYRVKsrssisSSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKSMSVlLD 484
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1834199175 277 YKDLDFMEQHPngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNL 328
Cdd:COG5253   485 MNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
84-466 2.34e-31

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: 125.55  E-value: 2.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175  84 IQLGIQHTV-GSLASKPKRDLLMMDFWEIESitfppegsSLTPAHHYSEFRYkiYAPIAFRYFRDLFGIQPDDFMMSM-C 161
Cdd:cd17304    10 MKEGLRAAIqNSIDVPPKESLSDDDYTEVLT--------QVIPKHKGFEFRT--YAGPVFATLRQSLGISEKEYQNSLsP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 162 TSP-LRELSNpGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVM 240
Cdd:cd17304    80 DEPyLQFISN-SKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKLPGKKKKYFIVM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 241 NNLLPSSVKMHLKYDLKGSTFKRKANKAerAKKSP---TYKDLDFMEqhpNGIFLEaETYAALIKTIQRDCTVLESFKIM 317
Cdd:cd17304   159 QSVFYPDERINERYDIKGCQVSRYTDPE--PEGSQiivVLKDLNFEG---NSINLG-QQRSWFLRQVEIDTEFLKGLNVL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199175 318 DYSLLLGVHnldvalkekqseqrkplraPLAEDSdvdaddpldgdaatgisrnksvNRQRLVAHSTAMESIQaesepidd 397
Cdd:cd17304   233 DYSLLVGFQ-------------------PLHSDE----------------------NRRLLPNYKNALHVVD-------- 263
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834199175 398 eedvppggiparsekGERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMA 466
Cdd:cd17304   264 ---------------GPEYRYFVGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVE 317
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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