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Conserved domains on  [gi|1821955873|ref|NP_001365949|]
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phosphatidylinositol 4-phosphate 5-kinase-like protein 1 isoform 1 [Mus musculus]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase-like protein 1( domain architecture ID 13022693)

phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PIP5KL1) acts as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
93-435 0e+00

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: 507.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  93 HELHRMTRMMQEGLWAATQVSKNNPPTGPTTQKDYLEVMTQVHE--EGFELGTLAGPAFARLRKSIGLTEEDYQATLGPG 170
Cdd:cd17304     1 HEFYSLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTEVLTQVIPkhKGFEFRTYAGPVFATLRQSLGISEKEYQNSLSPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 171 DPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLARLLGVYSLRVAQGKKKYFIIMQC 250
Cdd:cd17304    81 EPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKLPGKKKKYFIVMQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 251 IFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQEKTMRLGAQRSWFLRQMELDTAFLREVNVLDYSLLVAI 330
Cdd:cd17304   161 VFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLLVGF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 331 QFLHEDEkgihhsvfstfksiqgvskskgtgdqNCRMLPDLPNALHILDGPDQRYFLGLVDMTTVYGFRKRLEHVWKMVR 410
Cdd:cd17304   241 QPLHSDE--------------------------NRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVYGLRKRLEHLWKSLR 294
                         330       340
                  ....*....|....*....|....*
gi 1821955873 411 YPGQSVSTVSPAHYARRLCRWAEVH 435
Cdd:cd17304   295 YPGQSFSTVSPEKYARRFCQWVEDH 319
 
Name Accession Description Interval E-value
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
93-435 0e+00

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: 507.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  93 HELHRMTRMMQEGLWAATQVSKNNPPTGPTTQKDYLEVMTQVHE--EGFELGTLAGPAFARLRKSIGLTEEDYQATLGPG 170
Cdd:cd17304     1 HEFYSLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTEVLTQVIPkhKGFEFRTYAGPVFATLRQSLGISEKEYQNSLSPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 171 DPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLARLLGVYSLRVAQGKKKYFIIMQC 250
Cdd:cd17304    81 EPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKLPGKKKKYFIVMQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 251 IFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQEKTMRLGAQRSWFLRQMELDTAFLREVNVLDYSLLVAI 330
Cdd:cd17304   161 VFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLLVGF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 331 QFLHEDEkgihhsvfstfksiqgvskskgtgdqNCRMLPDLPNALHILDGPDQRYFLGLVDMTTVYGFRKRLEHVWKMVR 410
Cdd:cd17304   241 QPLHSDE--------------------------NRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVYGLRKRLEHLWKSLR 294
                         330       340
                  ....*....|....*....|....*
gi 1821955873 411 YPGQSVSTVSPAHYARRLCRWAEVH 435
Cdd:cd17304   295 YPGQSFSTVSPEKYARRFCQWVEDH 319
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
171-431 1.78e-85

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: 260.86  E-value: 1.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 171 DPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLARLLGVYSLRVaQGKKKYFIIMQC 250
Cdd:pfam01504   5 SILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKP-GGKKIYFVVMNN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 251 IFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNF--QEKTMRLGAQ-RSWFLRQMELDTAFLREVNVLDYSLL 327
Cdd:pfam01504  84 LFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFleRKLKLRLGPEkREALLKQLERDCEFLESLNIMDYSLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 328 VAIQFLHEDEKGIhhsvfstfksiqgvskskgtgdqncrmlpdlpnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWK 407
Cdd:pfam01504 164 LGIHDLDEDGKEI--------------------------------------------YYLGIIDILTEYNLKKKLEHAWK 199
                         250       260
                  ....*....|....*....|....
gi 1821955873 408 MVRYPGQSVSTVSPAHYARRLCRW 431
Cdd:pfam01504 200 SLVHDGDSISAVPPKEYAERFLKF 223
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
148-430 1.05e-56

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 190.29  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  148 AFARLRKSIGLTEEDYQATLGpGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLA 227
Cdd:smart00330  39 VFRNLRELFGIDPADYLRSLC-RSPPLELSSGGKSGSFFYLSLDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLP 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  228 RLLGVYSLRVAQG--KKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPaPEGSPLVlVLKDLNFQEKT---MRLGAQ- 301
Cdd:smart00330 118 KFFGLYRVKVKGGteKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREADK-KKVKELP-VLKDLDLVEMWnqpIYVDPLa 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  302 RSWFLRQMELDTAFLREVNVLDYSLLVAIQFL----HEDEKGIHHSVFSTFKSIQGVSKSKGTGDQNCRMLPDLPNALHI 377
Cdd:smart00330 196 KKALLKQIKRDCEFLESLKIMDYSLLVGIHDIergqREEIELPPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGP 275
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821955873  378 LDGPDQR--------YFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCR 430
Cdd:smart00330 276 FGGIPARairarrvvLYLGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRD 336
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
149-427 4.80e-29

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 120.32  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLAR 228
Cdd:PLN03185  414 FRNLREMFKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITK 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 229 LLGVYSLRVAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQektMRLgaQRSW---F 305
Cdd:PLN03185  494 FFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENTTLKDLDLNYS---FYL--EPSWrdaL 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 306 LRQMELDTAFLREVNVLDYSLLVAIQF---LHEDEKGIHHS--------VFSTFKSIQ---------------GVSKSKG 359
Cdd:PLN03185  569 LRQIEIDSKFLEAQRIMDYSLLLGVHFrapQHLRSLLPYSRsitadgleVVAEEDTIEdeelsypeglvlvprGADDGST 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 360 T---------------GDQNCRML---------------PDLPNALHILDGPDQRYF---------LGLVDMTTVYGFRK 400
Cdd:PLN03185  649 VpgphirgsrlrasaaGDEEVDLLlpgtarlqiqlgvnmPARAERIPGREDKEKQSFhevydvvlyLGIIDILQEYNMSK 728
                         330       340
                  ....*....|....*....|....*..
gi 1821955873 401 RLEHVWKMVRYPGQSVSTVSPAHYARR 427
Cdd:PLN03185  729 KIEHAYKSLQFDSLSISAVDPTFYSKR 755
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
135-433 1.04e-28

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 118.90  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 135 HEEGFELGTLAG--PAFARLRKSIGLTEEDyqatlgPGdpylqffstsKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLP 212
Cdd:COG5253   343 PEVFRELRALCGcdEALVSLLSRYILWESN------GG----------KSGSFFLFTRDYKFIIKTISHSEHICFRPMIF 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 213 RYVEHLQQYPHSLLARLLGVYSLRVAQG------KKKYFIIMQCIFYPtSRISERYDIKGCNISRWVDP-APEGSPLvLV 285
Cdd:COG5253   407 EYYVHVLFNPLTLLCKIFGFYRVKSRSSisssksRKIYFIVMENLFYP-HGIHRIFDLKGSMRNRHVERtGKSMSVL-LD 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 286 LKDLNFQEKTMRL--GAQRSWFLRQMELDTAFLREVNVLDYSLLVAIQFLHEDekgihhsvfSTFKSIQGVSKSKGTGdq 363
Cdd:COG5253   485 MNDVEWIRESPKIvfGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREE---------ASVGLIIDFIRTRMTG-- 553
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 364 ncrmlpdlpnalhildgpDQRYFLGLVDMTTVYGFRKRLEhvwkmvrypgqsVSTVSPAHYARRLCRWAE 433
Cdd:COG5253   554 ------------------DKKLESGIKDKLTVGSFTKRKE------------PTAVTPRQYKNRFRKAME 593
 
Name Accession Description Interval E-value
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
93-435 0e+00

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: 507.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  93 HELHRMTRMMQEGLWAATQVSKNNPPTGPTTQKDYLEVMTQVHE--EGFELGTLAGPAFARLRKSIGLTEEDYQATLGPG 170
Cdd:cd17304     1 HEFYSLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTEVLTQVIPkhKGFEFRTYAGPVFATLRQSLGISEKEYQNSLSPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 171 DPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLARLLGVYSLRVAQGKKKYFIIMQC 250
Cdd:cd17304    81 EPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKLPGKKKKYFIVMQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 251 IFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQEKTMRLGAQRSWFLRQMELDTAFLREVNVLDYSLLVAI 330
Cdd:cd17304   161 VFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLLVGF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 331 QFLHEDEkgihhsvfstfksiqgvskskgtgdqNCRMLPDLPNALHILDGPDQRYFLGLVDMTTVYGFRKRLEHVWKMVR 410
Cdd:cd17304   241 QPLHSDE--------------------------NRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVYGLRKRLEHLWKSLR 294
                         330       340
                  ....*....|....*....|....*
gi 1821955873 411 YPGQSVSTVSPAHYARRLCRWAEVH 435
Cdd:cd17304   295 YPGQSFSTVSPEKYARRFCQWVEDH 319
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
145-433 1.49e-86

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: 264.43  E-value: 1.49e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 145 AGPAFARLRKSIGLTEEDYQATLGPGDPYLQFFSTS-KSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPH 223
Cdd:cd00139     9 APEVFRKLRELFGISEEDYLESLSPEENLRELKESEgKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYEHIKKNPN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 224 SLLARLLGVYSLRVAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQEKTMRL---GA 300
Cdd:cd00139    89 SLLTRFYGLYSIKLQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEKEKKKGLKVLKDLDFLEKGEKIilgPE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 301 QRSWFLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHHSVfstfksiqgvskskgtgdqncrmlpdlpnalhildg 380
Cdd:cd00139   169 DRAELLEQLEKDVEFLRSLNIMDYSLLV----------GIHRLV------------------------------------ 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1821955873 381 pdqrYFLGLVDMTTVYGFRKRLEHVWKMVRYPG-QSVSTVSPAHYARRLCRWAE 433
Cdd:cd00139   203 ----YYLGIIDILQEYNLRKKLERFLKSLLYGKdSGISCVPPDEYAERFLKFME 252
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
171-431 1.78e-85

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: 260.86  E-value: 1.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 171 DPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLARLLGVYSLRVaQGKKKYFIIMQC 250
Cdd:pfam01504   5 SILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKP-GGKKIYFVVMNN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 251 IFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNF--QEKTMRLGAQ-RSWFLRQMELDTAFLREVNVLDYSLL 327
Cdd:pfam01504  84 LFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFleRKLKLRLGPEkREALLKQLERDCEFLESLNIMDYSLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 328 VAIQFLHEDEKGIhhsvfstfksiqgvskskgtgdqncrmlpdlpnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWK 407
Cdd:pfam01504 164 LGIHDLDEDGKEI--------------------------------------------YYLGIIDILTEYNLKKKLEHAWK 199
                         250       260
                  ....*....|....*....|....
gi 1821955873 408 MVRYPGQSVSTVSPAHYARRLCRW 431
Cdd:pfam01504 200 SLVHDGDSISAVPPKEYAERFLKF 223
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
148-430 1.05e-56

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 190.29  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  148 AFARLRKSIGLTEEDYQATLGpGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLA 227
Cdd:smart00330  39 VFRNLRELFGIDPADYLRSLC-RSPPLELSSGGKSGSFFYLSLDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLP 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  228 RLLGVYSLRVAQG--KKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPaPEGSPLVlVLKDLNFQEKT---MRLGAQ- 301
Cdd:smart00330 118 KFFGLYRVKVKGGteKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREADK-KKVKELP-VLKDLDLVEMWnqpIYVDPLa 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873  302 RSWFLRQMELDTAFLREVNVLDYSLLVAIQFL----HEDEKGIHHSVFSTFKSIQGVSKSKGTGDQNCRMLPDLPNALHI 377
Cdd:smart00330 196 KKALLKQIKRDCEFLESLKIMDYSLLVGIHDIergqREEIELPPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGP 275
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821955873  378 LDGPDQR--------YFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCR 430
Cdd:smart00330 276 FGGIPARairarrvvLYLGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRD 336
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
149-430 1.62e-53

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: 181.33  E-value: 1.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLAR 228
Cdd:cd17302    67 FRNLRELFGIDAADYMLSLCGDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTK 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 229 LLGVYSLRVAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVD-PAPEGSPLVlVLKDLNFQektMRLGAQRSW--- 304
Cdd:cd17302   147 FFGVHRVKPVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNT-TLKDLDLD---FKFRLEKGWrda 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 305 FLRQMELDTAFLREVNVLDYSLLVAIQFLHEDEKGIHHSVfstfksiqgvskskgtgdqncrmlpdlpnalhILdgpdqr 384
Cdd:cd17302   223 LMRQIDADCAFLEALRIMDYSLLLGVHFRAGDSTGEPYDV--------------------------------VL------ 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1821955873 385 yFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCR 430
Cdd:cd17302   265 -YFGIIDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRD 309
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
148-427 3.74e-53

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: 180.18  E-value: 3.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 148 AFARLRKSIGLTEEDYQATLGPGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLA 227
Cdd:cd17303    63 VFRFLRELFGIDPADYLMSLTGKYILSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 228 RLLGVYSLRVAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQEKTMRLG---AQRSW 304
Cdd:cd17303   143 QFYGLHRVKMPRGRKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPEDKLAKGPRATLKDLNWLRRKRKLAlgpEKRKQ 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 305 FLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHhsvfstfkSIQGVSKSKGTGDQncrmlpdlpnalhildGPDQR 384
Cdd:cd17303   223 FLTQLKRDVEFLASLNIMDYSLLV----------GIH--------DLDGGFQATDENNE----------------PGDEI 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1821955873 385 YFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARR 427
Cdd:cd17303   269 YYLGIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARR 311
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
149-428 6.78e-36

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: 133.94  E-value: 6.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPYLQFfSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHL-QQYPHSLLA 227
Cdd:cd17305    63 FRNLRERFGIDDDDYLNSLTRSQPLASD-SPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLP 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 228 RLLGVYSLRVaQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRwVDPAPEGSPLVLVLKDLNFQEKTMRL---GAQRSW 304
Cdd:cd17305   142 QYLGMYRITV-NGVETYLVVMRNVFSPRLPIHKKYDLKGSTVDR-QASDKEKAKDLPTLKDNDFLNDGTKIyigDEAKAK 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 305 FLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHhsvfstfksiqgvskskgtgdqncrmlpdlpnalhildgpDQR 384
Cdd:cd17305   220 LLETLKRDVEFLAKLNLMDYSLLV----------GIH----------------------------------------DCI 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1821955873 385 YFLGLVDMTTVYGFRKRLEHVWKMVRY-PGQSVSTVSPAHYARRL 428
Cdd:cd17305   250 YFMAIIDILTHYGAKKRAAHAAKTVKHgAGAEISTVKPEQYAKRF 294
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
149-431 3.57e-33

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: 125.70  E-value: 3.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPylqfFSTS--KSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHL-----QQY 221
Cdd:cd17300    13 FHALRSLYCGGEDDFIRSLSRCVK----WDASggKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMakalfHKR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 222 PhSLLARLLGVYSLRV-----AQGKKKYFIIMQCIFYpTSRISERYDIKGCNISRWVDPAPEGSPlvlVLKDLNFQEKTM 296
Cdd:cd17300    89 P-SLLAKILGVYRISVknsttNKTSKQDLLVMENLFY-GRNISQVYDLKGSLRNRYVNVAEDEDS---VLLDENFLEYTK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 297 RL-----GAQRSWFLRQMELDTAFLREVNVLDYSLLVaiqflhedekgihhsvfstfksiqGVSKSKGTgdqncrmlpdl 371
Cdd:cd17300   164 GSplylrEHSKAVLMAAIWNDTLFLSSQNVMDYSLLV------------------------GIDEEKKE----------- 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821955873 372 pnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWK-MVRYPGQSVSTV-SPAHYARRLCRW 431
Cdd:cd17300   209 -------------LVVGIIDYIRTYTWDKKLESWVKsLGILGGGGEPTViSPELYKKRFREA 257
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
132-427 1.20e-30

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: 120.04  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 132 TQVHEEG-FELGTLAGPAFARLRKSIGLTEEDYQATLGpGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAH 210
Cdd:cd17301    47 TPAHHYSdFRFKTYAPVAFRYFRELFGIKPDDYLLSLC-NEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 211 LPRYVEHLQQYPHSLLARLLGVYSLRvAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRwvdPAPE-----GSPlvlV 285
Cdd:cd17301   126 LPGYYMNLNQNPRTLLPKFYGLYCYQ-SGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKR---KASKkerqkKSP---T 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 286 LKDLNFQE---KTMRLGAQ-RSWFLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHHsvfstFKSIQGVSkSKGTg 361
Cdd:cd17301   199 LKDLDFMEdhpEGILLEPDtYDALLKTIQRDCRVLESFKIMDYSLLL----------GVHN-----LGGIPARN-SKGE- 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821955873 362 dqncRMLpdlpnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARR 427
Cdd:cd17301   262 ----RLL----------------LFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAER 307
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
149-427 4.80e-29

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 120.32  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLAR 228
Cdd:PLN03185  414 FRNLREMFKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITK 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 229 LLGVYSLRVAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQektMRLgaQRSW---F 305
Cdd:PLN03185  494 FFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENTTLKDLDLNYS---FYL--EPSWrdaL 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 306 LRQMELDTAFLREVNVLDYSLLVAIQF---LHEDEKGIHHS--------VFSTFKSIQ---------------GVSKSKG 359
Cdd:PLN03185  569 LRQIEIDSKFLEAQRIMDYSLLLGVHFrapQHLRSLLPYSRsitadgleVVAEEDTIEdeelsypeglvlvprGADDGST 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 360 T---------------GDQNCRML---------------PDLPNALHILDGPDQRYF---------LGLVDMTTVYGFRK 400
Cdd:PLN03185  649 VpgphirgsrlrasaaGDEEVDLLlpgtarlqiqlgvnmPARAERIPGREDKEKQSFhevydvvlyLGIIDILQEYNMSK 728
                         330       340
                  ....*....|....*....|....*..
gi 1821955873 401 RLEHVWKMVRYPGQSVSTVSPAHYARR 427
Cdd:PLN03185  729 KIEHAYKSLQFDSLSISAVDPTFYSKR 755
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
135-433 1.04e-28

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 118.90  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 135 HEEGFELGTLAG--PAFARLRKSIGLTEEDyqatlgPGdpylqffstsKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLP 212
Cdd:COG5253   343 PEVFRELRALCGcdEALVSLLSRYILWESN------GG----------KSGSFFLFTRDYKFIIKTISHSEHICFRPMIF 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 213 RYVEHLQQYPHSLLARLLGVYSLRVAQG------KKKYFIIMQCIFYPtSRISERYDIKGCNISRWVDP-APEGSPLvLV 285
Cdd:COG5253   407 EYYVHVLFNPLTLLCKIFGFYRVKSRSSisssksRKIYFIVMENLFYP-HGIHRIFDLKGSMRNRHVERtGKSMSVL-LD 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 286 LKDLNFQEKTMRL--GAQRSWFLRQMELDTAFLREVNVLDYSLLVAIQFLHEDekgihhsvfSTFKSIQGVSKSKGTGdq 363
Cdd:COG5253   485 MNDVEWIRESPKIvfGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREE---------ASVGLIIDFIRTRMTG-- 553
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 364 ncrmlpdlpnalhildgpDQRYFLGLVDMTTVYGFRKRLEhvwkmvrypgqsVSTVSPAHYARRLCRWAE 433
Cdd:COG5253   554 ------------------DKKLESGIKDKLTVGSFTKRKE------------PTAVTPRQYKNRFRKAME 593
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
135-431 3.78e-25

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: 105.07  E-value: 3.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 135 HEEGFELGTLAGPAFARLRKSIGLTEEDYQATLGpGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRY 214
Cdd:cd17307    51 HYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSIC-SEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGY 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 215 VEHLQQYPHSLLARLLGVYSLRvAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPlVLVLKDLNFQEK 294
Cdd:cd17307   130 YMNLNQNPRTLLPKFYGLYCMQ-SGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKS-CPTYKDLDFLQD 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 295 T---MRLGAQR-SWFLRQMELDTAFLREVNVLDYSLLVAIQFLhedekgihhsvfstfksiQGVSKSKGTGDqncRMLpd 370
Cdd:cd17307   208 MhdgLYFDPETyNALMKTLQRDCRVLESFKIMDYSLLLGIHVL------------------GGIPAKNHKGE---KLL-- 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821955873 371 lpnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCRW 431
Cdd:cd17307   265 --------------LFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKF 311
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
135-431 1.12e-24

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: 103.92  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 135 HEEGFELGTLAGPAFARLRKSIGLTEEDYQATLGpGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRY 214
Cdd:cd17306    54 HYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-SEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGY 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 215 VEHLQQYPHSLLARLLGVYSLRvAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVlVLKDLNFQEK 294
Cdd:cd17306   133 YMNLNQNPRTLLPKFYGLYCVQ-AGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLP-TYKDLDFLQD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 295 T---MRLGAQ-RSWFLRQMELDTAFLREVNVLDYSLLVAIQFLHEDEKGihhsVFSTFKSIQGVSKSKGTGDqncRMLpd 370
Cdd:cd17306   211 IpdgLFLDSDmYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNIDARRGG----TIETDDQMGGIPARNSKGE---RLL-- 281
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821955873 371 lpnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCRW 431
Cdd:cd17306   282 --------------LYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRF 328
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
135-431 5.32e-24

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: 101.61  E-value: 5.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 135 HEEGFELGTLAGPAFARLRKSIGLTEEDYQATLGpGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRY 214
Cdd:cd17308    52 HYPDFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-NEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGY 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 215 VEHLQQYPHSLLARLLGVYSLRvAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDpAPEGSPLVLVLKDLNFQ-- 292
Cdd:cd17308   131 YMNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRAS-KKEREKSKPTFKDLDFMqd 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 293 --EKTMRLGAQRSWFLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHhsvfstfkSIQGVSKSKGTGDqncRMLpd 370
Cdd:cd17308   209 mpEGLMLDADTFSALVKTLQRDCLVLESFKIMDYSLLL----------GVH--------NIGGIPAVNGKGE---RLL-- 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821955873 371 lpnalhildgpdqrYFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCRW 431
Cdd:cd17308   266 --------------LYIGIIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKF 312
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
149-428 1.19e-23

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: 100.51  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPyLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQ-YPHSLLA 227
Cdd:cd17310    74 FRNLRERFGIDDQDYQNSVTRSAP-INSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLP 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 228 RLLGVYSLRVaQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVlVLKDLNFQEKTMRL---GAQRSW 304
Cdd:cd17310   153 QFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLP-TFKDNDFLNEGQKLhvgEESKKN 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 305 FLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHHSVfstfksiqgvskskgtgdqncrmlpdlpnalhildgpdqr 384
Cdd:cd17310   231 FLEKLKRDVEFLAQLKIMDYSLLV----------GIHDVV---------------------------------------- 260
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1821955873 385 YFLGLVDMTTVYGFRKRLEHVWKMVRY-PGQSVSTVSPAHYARRL 428
Cdd:cd17310   261 YFMAIIDILTPYDAKKKAAHAAKTVKHgAGAEISTVNPEQYSKRF 305
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
149-428 1.99e-23

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: 99.56  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPYLQffsTSKSKASFFLTHDQRFFVKTQRRHEV---HVLLAHLPRYVehLQQYPHSL 225
Cdd:cd17311    63 FRNLRERFGIDDQDYQVSLTRSPPYSE---SEGSDGRFLLSYDRTLVIKEISSEDVadmHSILSHYHQYI--VKCHGNTL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 226 LARLLGVYSLRVaQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVlVLKDLNFQEKTMRL---GAQR 302
Cdd:cd17311   138 LPQFLGMYRLSV-DNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELP-TLKDMDFLNKNQKVyvgEEQK 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 303 SWFLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHHSVfstfksiqgvskskgtgdqncrmlpdlpnalhildgpd 382
Cdd:cd17311   216 RIFLEKLKRDVEFLVQLKIMDYSLLL----------GIHDVV-------------------------------------- 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1821955873 383 qrYFLGLVDMTTVYGFRKRLEHVWKMVRY-PGQSVSTVSPAHYARRL 428
Cdd:cd17311   248 --YFMGLIDILTQYDAKKKAAHAAKTVKHgAGAEISTVHPEQYAKRF 292
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
149-428 4.02e-21

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: 93.12  E-value: 4.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 149 FARLRKSIGLTEEDYQATLGPGDPYLQFfSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQ-YPHSLLA 227
Cdd:cd17309    72 FRNLRERFGIDDQDFQNSLTRSAPLAND-SQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGNTLLP 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 228 RLLGVYSLRVaQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVlVLKDLNFQEKTMRL---GAQRSW 304
Cdd:cd17309   151 QFLGMYRLTV-DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELP-TLKDNDFINDGQKIyidENNKKM 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821955873 305 FLRQMELDTAFLREVNVLDYSLLVaiqflhedekGIHhsvfstfksiqgvskskgtgdqncrmlpdlpnalhildgpDQR 384
Cdd:cd17309   229 FLEKLKKDVEFLAQLKLMDYSLLV----------GIH----------------------------------------DVV 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1821955873 385 YFLGLVDMTTVYGFRKRLEHVWKMVRY-PGQSVSTVSPAHYARRL 428
Cdd:cd17309   259 YFMAIIDILTHYDAKKKAAHAAKTVKHgAGAEISTVNPEQYSKRF 303
 
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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