NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528486960|ref|XP_005166786|]
View 

phosphatidylinositol 4-phosphate 5-kinase type-1 beta isoform X1 [Danio rerio]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase type-1 beta( domain architecture ID 13022714)

phosphatidylinositol 4-phosphate 5-kinase type-1 beta 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-393 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: 700.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  27 SALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17307    1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 107 YSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRLV 186
Cdd:cd17307   81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 187 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFV-DMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 265
Cdd:cd17307  161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLqDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 266 YSLLLGVHVLdqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmGGIPAKTHRDEKVLIFLGIIDIL 345
Cdd:cd17307  241 YSLLLGIHVL-----------------------------------------------GGIPAKNHKGEKLLLFMGIIDIL 273
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528486960 346 QSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSSRVFRKNQ 393
Cdd:cd17307  274 QSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ 321
 
Name Accession Description Interval E-value
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-393 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: 700.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  27 SALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17307    1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 107 YSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRLV 186
Cdd:cd17307   81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 187 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFV-DMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 265
Cdd:cd17307  161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLqDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 266 YSLLLGVHVLdqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmGGIPAKTHRDEKVLIFLGIIDIL 345
Cdd:cd17307  241 YSLLLGIHVL-----------------------------------------------GGIPAKNHKGEKLLLFMGIIDIL 273
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528486960 346 QSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSSRVFRKNQ 393
Cdd:cd17307  274 QSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ 321
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
53-386 1.98e-144

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 418.71  E-value: 1.98e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960    53 LMQDFYVVESVFLPSEGS-NLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICKEPLIELSNPGASGSLFYLTS 131
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960   132 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGG---INIRLVVMNNVLPRSVKMHYKYDLKGST 208
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960   209 YKRRASrKEREKPCPTYKDLDFVDMH-DGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGVHVLDQSHRDGDGSAV 287
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWnQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960   288 --DGKRTVGQKVLYSTAMESIQGDGKAAEALTTDDTMGGIPAKTHRDEKVLIFLGIIDILQSYRFIKKLEHSWKALVYDG 365
Cdd:smart00330 240 vyGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHDG 319
                          330       340
                   ....*....|....*....|.
gi 528486960   366 DTVSVHRPSFYANRFLKFMSS 386
Cdd:smart00330 320 KTISVVHPEQYAKRFRDFMDK 340
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
108-386 3.07e-123

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: 360.24  E-value: 3.07e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  108 SICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRLVV 187
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  188 MNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPT-YKDLDFVDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDY 266
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  267 SLLLGVHVLDQshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmggipakthrDEKVLIFLGIIDILQ 346
Cdd:pfam01504 161 SLLLGIHDLDE------------------------------------------------------DGKEIYYLGIIDILT 186
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 528486960  347 SYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSS 386
Cdd:pfam01504 187 EYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEK 226
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
18-389 1.11e-77

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 259.38  E-value: 1.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  18 EKTYKKTTSSALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFL--PSEGSNLTPAHHYPDFRFKTYAPLAFRYFR 95
Cdd:PLN03185 339 ETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMnfPKAGSQLTPSHQSEDFKWKDYCPMVFRNLR 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  96 ELFGIKPDDYLYSIC-KEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLY 174
Cdd:PLN03185 419 EMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLH 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 175 CVQ-SGGINIRLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCpTYKDLdfvDMHDGLYFDPETYNALMKTLQR 253
Cdd:PLN03185 499 RIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENT-TLKDL---DLNYSFYLEPSWRDALLRQIEI 574
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 254 DCRVLESFKIMDYSLLLGVHVLDQSH----------------------------------------RDGDGSAVdgkrTV 293
Cdd:PLN03185 575 DSKFLEAQRIMDYSLLLGVHFRAPQHlrsllpysrsitadglevvaeedtiedeelsypeglvlvpRGADDGST----VP 650
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 294 GQKVLYSTAMESIQGD--------GKAAEALTTDDTMggiPAKTHRDEK--------------VLIFLGIIDILQSYRFI 351
Cdd:PLN03185 651 GPHIRGSRLRASAAGDeevdlllpGTARLQIQLGVNM---PARAERIPGredkekqsfhevydVVLYLGIIDILQEYNMS 727
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 528486960 352 KKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMsSRVF 389
Cdd:PLN03185 728 KKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
69-399 4.20e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 136.23  E-value: 4.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  69 GSNLTPAHHYpDFRFKTYAPLAFRYFRELFGIkpDDYLYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFL 148
Cdd:COG5253  325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 149 QKLLPGYYMNLNQNPRTLLPKFYGLYCVQ------SGGIN-IRLVVMNNVLPRSvKMHYKYDLKGSTYKRRASRKER-EK 220
Cdd:COG5253  402 RPMIFEYYVHVLFNPLTLLCKIFGFYRVKsrssisSSKSRkIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKsMS 480
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 221 PCPTYKDLDFVdmHDGLYFDPETYNALMKT-LQRDCRVLESFKIMDYSLLLGVHVLDQSHRDGDGSAVDGKRTVGQKVLY 299
Cdd:COG5253  481 VLLDMNDVEWI--RESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGLIIDFIRTRMTGDKKLE 558
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 300 StamesiqgdgkaaealttddtmggipakthrdekvliflGIIDILQSYRFIKKLEhswkalvydgdtVSVHRPSFYANR 379
Cdd:COG5253  559 S---------------------------------------GIKDKLTVGSFTKRKE------------PTAVTPRQYKNR 587
                        330       340
                 ....*....|....*....|....*
gi 528486960 380 FLKFMSSRVFRKNQP-----NRFSP 399
Cdd:COG5253  588 FRKAMEAYIDPFPDKktqegFKTNP 612
 
Name Accession Description Interval E-value
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-393 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: 700.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  27 SALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17307    1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 107 YSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRLV 186
Cdd:cd17307   81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 187 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFV-DMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 265
Cdd:cd17307  161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLqDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 266 YSLLLGVHVLdqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmGGIPAKTHRDEKVLIFLGIIDIL 345
Cdd:cd17307  241 YSLLLGIHVL-----------------------------------------------GGIPAKNHKGEKLLLFMGIIDIL 273
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528486960 346 QSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSSRVFRKNQ 393
Cdd:cd17307  274 QSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ 321
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
27-391 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: 655.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  27 SALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17301    1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 107 YSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRLV 186
Cdd:cd17301   81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 187 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFVDMH-DGLYFDPETYNALMKTLQRDCRVLESFKIMD 265
Cdd:cd17301  161 VMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHpEGILLEPDTYDALLKTIQRDCRVLESFKIMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 266 YSLLLGVHVLdqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmGGIPAKTHRDEKVLIFLGIIDIL 345
Cdd:cd17301  241 YSLLLGVHNL-----------------------------------------------GGIPARNSKGERLLLFIGIIDIL 273
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 528486960 346 QSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSSRVFRK 391
Cdd:cd17301  274 QSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKK 319
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
26-392 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: 611.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  26 SSALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDY 105
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 106 LYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRL 185
Cdd:cd17308   81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 186 VVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFV-DMHDGLYFDPETYNALMKTLQRDCRVLESFKIM 264
Cdd:cd17308  161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMqDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 265 DYSLLLGVHvldqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddTMGGIPAKTHRDEKVLIFLGIIDI 344
Cdd:cd17308  241 DYSLLLGVH-----------------------------------------------NIGGIPAVNGKGERLLLYIGIIDI 273
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528486960 345 LQSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSSRVFRKN 392
Cdd:cd17308  274 LQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKS 321
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
24-391 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: 576.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  24 TTSSALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPD 103
Cdd:cd17306    1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 104 DYLYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINI 183
Cdd:cd17306   81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 184 RLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFV-DMHDGLYFDPETYNALMKTLQRDCRVLESFK 262
Cdd:cd17306  161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLqDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 263 IMDYSLLLGVHVLDqSHRDGdgsavdgkrtvgqkvlystamesiqgdgkaaeALTTDDTMGGIPAKTHRDEKVLIFLGII 342
Cdd:cd17306  241 IMDYSLLVGIHNID-ARRGG--------------------------------TIETDDQMGGIPARNSKGERLLLYIGII 287
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 528486960 343 DILQSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSSRVFRK 391
Cdd:cd17306  288 DILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKK 336
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
53-386 1.98e-144

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 418.71  E-value: 1.98e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960    53 LMQDFYVVESVFLPSEGS-NLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICKEPLIELSNPGASGSLFYLTS 131
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960   132 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGG---INIRLVVMNNVLPRSVKMHYKYDLKGST 208
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960   209 YKRRASrKEREKPCPTYKDLDFVDMH-DGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGVHVLDQSHRDGDGSAV 287
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWnQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960   288 --DGKRTVGQKVLYSTAMESIQGDGKAAEALTTDDTMGGIPAKTHRDEKVLIFLGIIDILQSYRFIKKLEHSWKALVYDG 365
Cdd:smart00330 240 vyGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHDG 319
                          330       340
                   ....*....|....*....|.
gi 528486960   366 DTVSVHRPSFYANRFLKFMSS 386
Cdd:smart00330 320 KTISVVHPEQYAKRFRDFMDK 340
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
108-386 3.07e-123

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: 360.24  E-value: 3.07e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  108 SICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGINIRLVV 187
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  188 MNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPT-YKDLDFVDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDY 266
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  267 SLLLGVHVLDQshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmggipakthrDEKVLIFLGIIDILQ 346
Cdd:pfam01504 161 SLLLGIHDLDE------------------------------------------------------DGKEIYYLGIIDILT 186
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 528486960  347 SYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSS 386
Cdd:pfam01504 187 EYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEK 226
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
79-386 5.27e-97

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: 294.10  E-value: 5.27e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  79 PDFRFKTYAPLAFRYFRELFGIKPDDYLYSICKEPLIELSN--PGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYY 156
Cdd:cd00139    1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKesEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 157 MNLNQNPRTLLPKFYGLYCVQ-SGGINIRLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPC-PTYKDLDFVDMH 234
Cdd:cd00139   81 EHIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEKEKKKGlKVLKDLDFLEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 235 DGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGVHvldqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaae 314
Cdd:cd00139  161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH----------------------------------------- 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528486960 315 alttddtmggipakthrdeKVLIFLGIIDILQSYRFIKKLEHSWKALVYDGDT-VSVHRPSFYANRFLKFMSS 386
Cdd:cd00139  200 -------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
34-385 9.00e-95

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: 290.73  E-value: 9.00e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  34 QLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHY-PDFRFKTYAPLAFRYFRELFGIKPDDYLYSIC-K 111
Cdd:cd17302    9 QLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQsSDFKWKDYCPMVFRNLRELFGIDAADYMLSLCgD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 112 EPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCV-QSGGINIRLVVMNN 190
Cdd:cd17302   89 DALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 191 VLPRSVKMHYKYDLKGSTYKRRASRKERE-KPCPTYKDLDFvdmhDGLYF-DPETYNALMKTLQRDCRVLESFKIMDYSL 268
Cdd:cd17302  169 LFCTELRIHRRFDLKGSTHGRTTGKPESEiDPNTTLKDLDL----DFKFRlEKGWRDALMRQIDADCAFLEALRIMDYSL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 269 LLGVHvldqsHRDGDgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmggiPAKTHRDekVLIFLGIIDILQSY 348
Cdd:cd17302  245 LLGVH-----FRAGD------------------------------------------STGEPYD--VVLYFGIIDILQEY 275
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 528486960 349 RFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMS 385
Cdd:cd17302  276 NISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIR 312
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
35-386 4.64e-89

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: 276.10  E-value: 4.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  35 LGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYpDFRFKTYAPLAFRYFRELFGIKPDDYLYSIC-KEP 113
Cdd:cd17303    9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTgKYI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 114 LIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGINIRLVVMNNVL 192
Cdd:cd17303   88 LSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKmPRGRKIHFVVMNNLF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 193 PRSVKMHYKYDLKGSTYKRRAS-RKEREKPCPTYKDLDFVDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLG 271
Cdd:cd17303  168 PPHRDIHQTFDLKGSTVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVG 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 272 VHVLDqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmGGIPAKTHRDEK--VLIFLGIIDILQSYR 349
Cdd:cd17303  248 IHDLD----------------------------------------------GGFQATDENNEPgdEIYYLGIIDILTPYN 281
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 528486960 350 FIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSS 386
Cdd:cd17303  282 AKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
18-389 1.11e-77

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 259.38  E-value: 1.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  18 EKTYKKTTSSALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFL--PSEGSNLTPAHHYPDFRFKTYAPLAFRYFR 95
Cdd:PLN03185 339 ETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMnfPKAGSQLTPSHQSEDFKWKDYCPMVFRNLR 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  96 ELFGIKPDDYLYSIC-KEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLY 174
Cdd:PLN03185 419 EMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLH 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 175 CVQ-SGGINIRLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCpTYKDLdfvDMHDGLYFDPETYNALMKTLQR 253
Cdd:PLN03185 499 RIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENT-TLKDL---DLNYSFYLEPSWRDALLRQIEI 574
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 254 DCRVLESFKIMDYSLLLGVHVLDQSH----------------------------------------RDGDGSAVdgkrTV 293
Cdd:PLN03185 575 DSKFLEAQRIMDYSLLLGVHFRAPQHlrsllpysrsitadglevvaeedtiedeelsypeglvlvpRGADDGST----VP 650
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 294 GQKVLYSTAMESIQGD--------GKAAEALTTDDTMggiPAKTHRDEK--------------VLIFLGIIDILQSYRFI 351
Cdd:PLN03185 651 GPHIRGSRLRASAAGDeevdlllpGTARLQIQLGVNM---PARAERIPGredkekqsfhevydVVLYLGIIDILQEYNMS 727
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 528486960 352 KKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMsSRVF 389
Cdd:PLN03185 728 KKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
29-386 1.22e-66

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: 217.52  E-value: 1.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  29 LKGAIQLGIGYTVGNLTSKPDRDVLM-QDFYV-----VESVFLPSEgsNLtPAHhypdFRFKTYAPLAFRYFRELFGIKP 102
Cdd:cd17305    2 LLSVFMWGINHSINELSHVPIPVMLMpDDFKAyskikVDNHLFNKE--NL-PSH----FKVKEYCPLVFRNLRERFGIDD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 103 DDYLYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNL-NQNPRTLLPKFYGLYCVQSGGI 181
Cdd:cd17305   75 DDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRITVNGV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 182 NIRLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFVDMHDGLYFDPETYNALMKTLQRDCRVLESF 261
Cdd:cd17305  155 ETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 262 KIMDYSLLLGVHvldqshrdgdgsavdgkrtvgqKVLYstamesiqgdgkaaealttddtmggipakthrdekvliFLGI 341
Cdd:cd17305  235 NLMDYSLLVGIH----------------------DCIY--------------------------------------FMAI 254
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 528486960 342 IDILQSYRFIKKLEHSWKALVYDGDT-VSVHRPSFYANRFLKFMSS 386
Cdd:cd17305  255 IDILTHYGAKKRAAHAAKTVKHGAGAeISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
26-386 1.24e-48

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: 170.62  E-value: 1.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  26 SSALKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFlpSEGSNLTPAHHYPD-FRFKTYAPLAFRYFRELFGIKPDD 104
Cdd:cd17310   10 SEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKI--KVDNHLFNKENLPSrFKFKEYCPMVFRNLRERFGIDDQD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 105 YLYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGINI 183
Cdd:cd17310   88 YQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVET 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 184 RLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFVDMHDGLYFDPETYNALMKTLQRDCRVLESFKI 263
Cdd:cd17310  168 YMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 264 MDYSLLLGVHvldqshrdgdgsavdgkrtvgqkvlystamesiqgdgkaaealttddtmggipakthrdeKVLIFLGIID 343
Cdd:cd17310  248 MDYSLLVGIH------------------------------------------------------------DVVYFMAIID 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 528486960 344 ILQSYRFIKKLEHSWKALVYD-GDTVSVHRPSFYANRFLKFMSS 386
Cdd:cd17310  268 ILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
74-386 3.46e-43

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: 155.91  E-value: 3.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  74 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLP 153
Cdd:cd17309   59 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 154 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGINIRLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFVD 232
Cdd:cd17309  135 KYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 233 MHDGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGVHvldqshrdgdgsavdgkrtvgqkvlystamesiqgdgka 312
Cdd:cd17309  215 DGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIH--------------------------------------- 255
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528486960 313 aealttddtmggipakthrdeKVLIFLGIIDILQSYRFIKKLEHSWKALVYD-GDTVSVHRPSFYANRFLKFMSS 386
Cdd:cd17309  256 ---------------------DVVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
74-386 5.98e-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: 5.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  74 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICKEPliELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLP 153
Cdd:cd17311   50 PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILS 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 154 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGINIRLVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKPCPTYKDLDFVD 232
Cdd:cd17311  124 HYHQYIVKcHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLN 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 233 MHDGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGVHvldqshrdgdgsavdgkrtvgqkvlystamesiqgdgka 312
Cdd:cd17311  204 KNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIH--------------------------------------- 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528486960 313 aealttddtmggipakthrdeKVLIFLGIIDILQSYRFIKKLEHSWKALVYD-GDTVSVHRPSFYANRFLKFMSS 386
Cdd:cd17311  245 ---------------------DVVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
79-386 1.48e-36

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: 136.10  E-value: 1.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  79 PDFRFKTYAPLAFRYFRELFGIKPDDYLYSICKEPLIELSNpGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGY--Y 156
Cdd:cd17300    1 TKFTCTIYFAEQFHALRSLYCGGEDDFIRSLSRCVKWDASG-GKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfeY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 157 M--NLNQNPRTLLPKFYGLY--CVQSGGIN----IRLVVMNNVLPRSvKMHYKYDLKGSTYKRRASRKEREKPcpTYKDL 228
Cdd:cd17300   80 MakALFHKRPSLLAKILGVYriSVKNSTTNktskQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDEDS--VLLDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 229 DFV-DMHDG-LYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGVhvldqshrdgdgsavdgkrtvgqkvlystamesi 306
Cdd:cd17300  157 NFLeYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI---------------------------------- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 307 qgdgkaaealttDDTmggipakthrdEKVLIfLGIIDILQSYRFIKKLEHSWKALVYDGD----TVsVHrPSFYANRFLK 382
Cdd:cd17300  203 ------------DEE-----------KKELV-VGIIDYIRTYTWDKKLESWVKSLGILGGggepTV-IS-PELYKKRFRE 256

                 ....
gi 528486960 383 FMSS 386
Cdd:cd17300  257 AMDK 260
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
32-386 3.45e-36

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PIP5KL1) and similar proteins; PIP5KL1 (EC 2.7.1.68), also known as PI(4)P 5-kinase-like protein 1, or PtdIns(4)P-5-kinase-like protein 1, may act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment, and conversion to PI(3,4,5)P3.


Pssm-ID: 340441  Cd Length: 319  Bit Score: 137.10  E-value: 3.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  32 AIQLGIGYTVGNLTSKPDRDVLMQDFY--VVESVFLPSEGsnltpahhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSI 109
Cdd:cd17304    9 MMKEGLRAAIQNSIDVPPKESLSDDDYteVLTQVIPKHKG-----------FEFRTYAGPVFATLRQSLGISEKEYQNSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 110 -CKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGINIRLVV 187
Cdd:cd17304   78 sPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKlPGKKKKYFIV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 188 MNNVLPRSVKMHYKYDLKGSTYKRRAsrkereKPCP-------TYKDLDFVDmhDGLYFDPETyNALMKTLQRDCRVLES 260
Cdd:cd17304  158 MQSVFYPDERINERYDIKGCQVSRYT------DPEPegsqiivVLKDLNFEG--NSINLGQQR-SWFLRQVEIDTEFLKG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 261 FKIMDYSLLLGVHVLdqsHRDGDgsavdgkrtvgQKVL--YSTAMESIQGdgkaaealttddtmggipakthrdEKVLIF 338
Cdd:cd17304  229 LNVLDYSLLVGFQPL---HSDEN-----------RRLLpnYKNALHVVDG------------------------PEYRYF 270
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528486960 339 LGIIDILQSYRFIKKLEHSWKALVYDGDTVSVHRPSFYANRFLKFMSS 386
Cdd:cd17304  271 VGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVED 318
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
69-399 4.20e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 136.23  E-value: 4.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960  69 GSNLTPAHHYpDFRFKTYAPLAFRYFRELFGIkpDDYLYSICKEPLIELSNPGASGSLFYLTSDDEFIIKTVQHKEAEFL 148
Cdd:COG5253  325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 149 QKLLPGYYMNLNQNPRTLLPKFYGLYCVQ------SGGIN-IRLVVMNNVLPRSvKMHYKYDLKGSTYKRRASRKER-EK 220
Cdd:COG5253  402 RPMIFEYYVHVLFNPLTLLCKIFGFYRVKsrssisSSKSRkIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKsMS 480
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 221 PCPTYKDLDFVdmHDGLYFDPETYNALMKT-LQRDCRVLESFKIMDYSLLLGVHVLDQSHRDGDGSAVDGKRTVGQKVLY 299
Cdd:COG5253  481 VLLDMNDVEWI--RESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGLIIDFIRTRMTGDKKLE 558
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528486960 300 StamesiqgdgkaaealttddtmggipakthrdekvliflGIIDILQSYRFIKKLEhswkalvydgdtVSVHRPSFYANR 379
Cdd:COG5253  559 S---------------------------------------GIKDKLTVGSFTKRKE------------PTAVTPRQYKNR 587
                        330       340
                 ....*....|....*....|....*
gi 528486960 380 FLKFMSSRVFRKNQP-----NRFSP 399
Cdd:COG5253  588 FRKAMEAYIDPFPDKktqegFKTNP 612
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH