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Conserved domains on  [gi|578818419|ref|XP_006717513|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 alpha isoform X1 [Homo sapiens]

Protein Classification

phosphatidylinositol phosphate kinase family protein( domain architecture ID 1000257)

phosphatidylinositol phosphate kinase (PIPK) family protein may catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc super family cl28923
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
27-352 3.41e-166

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.


The actual alignment was detected with superfamily member cd17309:

Pssm-ID: 475131  Cd Length: 309  Bit Score: 465.99  E-value: 3.41e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 107 IDDQDFQ---------------------------------------------------YIVECHGITLLPQFLGMYRLNV 135
Cdd:cd17309   81 IDDQDFQnsltrsaplandsqarsgarfhtsydkryiiktitsedvaemhnilkkyhqYIVECHGNTLLPQFLGMYRLTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 136 DGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFL 215
Cdd:cd17309  161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 216 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchen 295
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578818419 296 sprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 352
Cdd:cd17309  258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-352 3.41e-166

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: 465.99  E-value: 3.41e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 107 IDDQDFQ---------------------------------------------------YIVECHGITLLPQFLGMYRLNV 135
Cdd:cd17309   81 IDDQDFQnsltrsaplandsqarsgarfhtsydkryiiktitsedvaemhnilkkyhqYIVECHGNTLLPQFLGMYRLTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 136 DGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFL 215
Cdd:cd17309  161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 216 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchen 295
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578818419 296 sprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 352
Cdd:cd17309  258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
62-354 4.56e-100

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 299.30  E-value: 4.56e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419    62 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDF------------------------- 112
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYlrslcrspplelssggksgsffyls 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   113 --------------------------QYIVECHgITLLPQFLGMYRLNVDG---VEIYVIVTRNVFSHRLSVYRKYDLKG 163
Cdd:smart00330  80 lddrfiiktvskseiksllpmlpnyyEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   164 STVAREAsDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVEC 242
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   243 EENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPnIDVYGIKCHEnsprkEVYFMAIIDILTHYDAKKKAAHA 322
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHW 311
                          330       340       350
                   ....*....|....*....|....*....|..
gi 578818419   323 AKTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 354
Cdd:smart00330 312 VKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
112-353 2.20e-55

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: 180.74  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  112 FQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPT-LKDNDFINE 190
Cdd:pfam01504  49 YEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLER 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  191 GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntl 270
Cdd:pfam01504 128 KLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDL-------------------------------------- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  271 nsspplapgefdpnidvygikcheNSPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFI 350
Cdd:pfam01504 170 ------------------------DEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFI 224

                  ...
gi 578818419  351 GHI 353
Cdd:pfam01504 225 EKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1-350 3.69e-26

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 109.54  E-value: 3.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   1 MATPGNLGSSVLASKTKTKKKHFVAQK-----VKLFRASDPLLSvLMWGVNHSINELSHVQiPVMLMPDDFKAYSKIKVD 75
Cdd:PLN03185 310 LVLNNSFSSTSRRAKRRQKKLVKEIKRpgetiIKGHRSYDLMLS-LQLGIRYTVGKITPIQ-RREVRPSDFGPRASFWMN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  76 nhlFNKEN---MPSH----FKFKEYCPMVFRNLRERFGID-----------------------------DQDFQYI---- 115
Cdd:PLN03185 388 ---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDaadymmsicgndalrelsspgksgsvfflSQDDRFMiktl 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 116 ------------------VECHGITLLPQFLGMYRLN-VDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAsDKEKA 176
Cdd:PLN03185 465 rksevkvllrmlpdyhhhVKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEI 543
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 177 KELPTLKDNDFINEgqkIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEENDG 247
Cdd:PLN03185 544 DENTTLKDLDLNYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVVA 620
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 248 EEEGESDGTH---------PVGTPPDS--PGNTLNSSPPLAPGEFDPNID-----------------------VYGIKCH 293
Cdd:PLN03185 621 EEDTIEDEELsypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgvnmparaerIPGREDK 700
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818419 294 ENSPRKEVY----FMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 350
Cdd:PLN03185 701 EKQSFHEVYdvvlYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
73-233 3.80e-25

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 106.57  E-value: 3.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  73 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDD--------------------------QDFQYIVEC----- 118
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEalvsllsryilwesnggksgsfflftRDYKFIIKTishse 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 119 -----------------HGITLLPQFLGMYRLNV-------DGVEIYVIVTRNVFSHRLsVYRKYDLKGSTVAREASDKE 174
Cdd:COG5253  398 hicfrpmifeyyvhvlfNPLTLLCKIFGFYRVKSrssisssKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRHVERTG 476
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 175 KAKE-LPTLKDNDFINEGQKIyIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 233
Cdd:COG5253  477 KSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-352 3.41e-166

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: 465.99  E-value: 3.41e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 107 IDDQDFQ---------------------------------------------------YIVECHGITLLPQFLGMYRLNV 135
Cdd:cd17309   81 IDDQDFQnsltrsaplandsqarsgarfhtsydkryiiktitsedvaemhnilkkyhqYIVECHGNTLLPQFLGMYRLTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 136 DGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFL 215
Cdd:cd17309  161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 216 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchen 295
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578818419 296 sprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 352
Cdd:cd17309  258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
36-352 1.45e-160

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: 451.34  E-value: 1.45e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDF--- 112
Cdd:cd17305    1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYlns 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 113 ------------------------------------------------QYIVECHGITLLPQFLGMYRLNVDGVEIYVIV 144
Cdd:cd17305   81 ltrsqplasdspgrsgsrflvsydkkyviktisseevaqmhhilkqyhQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 145 TRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYS 224
Cdd:cd17305  161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 225 LLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFM 304
Cdd:cd17305  241 LLVGIHDC--------------------------------------------------------------------IYFM 252
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 578818419 305 AIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 352
Cdd:cd17305  253 AIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
25-350 3.14e-159

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: 448.34  E-value: 3.14e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  25 AQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRER 104
Cdd:cd17310    1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 105 FGIDDQDFQ---------------------------------------------------YIVECHGITLLPQFLGMYRL 133
Cdd:cd17310   81 FGIDDQDYQnsvtrsapinsdsqgrcgtrflttydrrfviktvssedvaemhnilkkyhqFIVECHGNTLLPQFLGMYRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 134 NVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVE 213
Cdd:cd17310  161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 214 FLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikch 293
Cdd:cd17310  241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578818419 294 ensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 350
Cdd:cd17310  260 -------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
36-350 1.24e-128

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: 370.35  E-value: 1.24e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDF--- 112
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYqvs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 113 ----------------------------------------------QYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTR 146
Cdd:cd17311   81 ltrsppysesegsdgrfllsydrtlvikeissedvadmhsilshyhQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 147 NVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLL 226
Cdd:cd17311  161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 227 VGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntlnsspplapgefdpnidvygikchensprkeVYFMAI 306
Cdd:cd17311  241 LGIHDV--------------------------------------------------------------------VYFMGL 252
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 578818419 307 IDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 350
Cdd:cd17311  253 IDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFI 296
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
62-354 4.56e-100

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 299.30  E-value: 4.56e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419    62 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDF------------------------- 112
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYlrslcrspplelssggksgsffyls 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   113 --------------------------QYIVECHgITLLPQFLGMYRLNVDG---VEIYVIVTRNVFSHRLSVYRKYDLKG 163
Cdd:smart00330  80 lddrfiiktvskseiksllpmlpnyyEHIVQNP-NTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   164 STVAREAsDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVEC 242
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   243 EENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPnIDVYGIKCHEnsprkEVYFMAIIDILTHYDAKKKAAHA 322
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHW 311
                          330       340       350
                   ....*....|....*....|....*....|..
gi 578818419   323 AKTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 354
Cdd:smart00330 312 VKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
87-350 1.40e-56

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: 184.70  E-value: 1.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  87 HFKFKEYCPMVFRNLRERFGIDDQDF-----------------------------------------------------Q 113
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYleslspeenlrelkesegksgsfffftsdgkfiiktitkselkfllkilpdyyE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 114 YIVECHGiTLLPQFLGMYRLNV-DGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAS-DKEKAKELPTLKDNDFINEG 191
Cdd:cd00139   82 HIKKNPN-SLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 192 QKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntln 271
Cdd:cd00139  161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818419 272 sspplapgefdpnidvygikchensprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 350
Cdd:cd00139  202 -----------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERFLKFM 251
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
112-353 2.20e-55

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: 180.74  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  112 FQYIVEcHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPT-LKDNDFINE 190
Cdd:pfam01504  49 YEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLER 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  191 GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdgthpvgtppdspgntl 270
Cdd:pfam01504 128 KLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDL-------------------------------------- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  271 nsspplapgefdpnidvygikcheNSPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFI 350
Cdd:pfam01504 170 ------------------------DEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFI 224

                  ...
gi 578818419  351 GHI 353
Cdd:pfam01504 225 EKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
61-351 2.08e-51

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: 173.25  E-value: 2.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  61 LMPDDFKAYSKIKVDnHLFNKENMPSH--FKFKEYCPMVFRNLRERFGIDDQDF------QYI----------------- 115
Cdd:cd17303   26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYlmsltgKYIlselgspgksgsffyfs 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 116 ----------------------------VECHGITLLPQFLGMYRLNV-DGVEIYVIVTRNVFSHRLSVYRKYDLKGSTV 166
Cdd:cd17303  105 rdyrfiiktihhsehkflrkilpdyynhVKENPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGSTV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 167 AREAS-DKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVEraeqeeveceen 245
Cdd:cd17303  185 GRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD------------ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 246 dgeeegesDGTHPVGTppdspgntlnsspplapgefdpnidvygikchENSPRKEVYFMAIIDILTHYDAKKKAAHAAKT 325
Cdd:cd17303  253 --------GGFQATDE--------------------------------NNEPGDEIYYLGIIDILTPYNAKKKLEHFFKS 292
                        330       340
                 ....*....|....*....|....*.
gi 578818419 326 VKHgAGAEISTVNPEQYSKRFLDFIG 351
Cdd:cd17303  293 LRH-DRHTISAVPPKEYARRFLKFIE 317
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
35-351 4.19e-39

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: 141.23  E-value: 4.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  35 DPLLSVLMWGVNHSINELSHVQIPVMLMpDDFKayskiKVDNHLFNKE---NMPSH----FKFKEYCPMVFRNLRERFGI 107
Cdd:cd17301    1 SELMGAIQLGIGHSVGSLSSKPERDVLM-QDFE-----VVESVFFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 108 DDQDF----------------------------QYIV------EC----------------HGITLLPQFLGMYRLNVDG 137
Cdd:cd17301   75 KPDDYllslcneplrelsnpgasgslfylthddEFIIktvqhkEAeflqkllpgyymnlnqNPRTLLPKFYGLYCYQSGG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 138 VEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQK-IYIDDNNKKVFLEKLKKDVEFLA 216
Cdd:cd17301  155 KNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEgILLEPDTYDALLKTIQRDCRVLE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 217 QLKLMDYSLLVGIHDveraeqeeveceendgeeegesdgthPVGTPpdspgnTLNSSpplapgefdpnidvyGIKChens 296
Cdd:cd17301  235 SFKIMDYSLLLGVHN--------------------------LGGIP------ARNSK---------------GERL---- 263
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578818419 297 prkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIG 351
Cdd:cd17301  264 ----LLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMA 313
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
83-353 2.74e-37

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: 136.27  E-value: 2.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  83 NMPSH----FKFKEYCPMVFRNLRERFGIDDQDF-----------------------------QYI-------------- 115
Cdd:cd17302   48 TPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYmlslcgddalrelsspgksgsvfylshddRFMiktmrksemkvllr 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 116 --------VECHGITLLPQFLGMYRLN-VDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAS-DKEKAKELPTLKDN 185
Cdd:cd17302  128 mlpayykhVKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNTTLKDL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 186 DFineGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDveraeqeeveceendgeeegesdgthpvgTPPDS 265
Cdd:cd17302  208 DL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVHF-----------------------------RAGDS 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 266 PGntlnsspplapgefdpnidvygikchenSPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSKR 345
Cdd:cd17302  256 TG----------------------------EPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRR 306

                 ....*...
gi 578818419 346 FLDFIGHI 353
Cdd:cd17302  307 FRDFIRKV 314
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
85-230 2.33e-28

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: 112.39  E-value: 2.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  85 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQY------IVECHGI--------------------------------- 121
Cdd:cd17307   48 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYsicsepLIELSNPgasgslfyvtsddefiiktvqhkeaeflqkllp 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 122 -----------TLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINE 190
Cdd:cd17307  128 gyymnlnqnprTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQD 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578818419 191 GQK-IYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIH 230
Cdd:cd17307  208 MHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1-350 3.69e-26

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 109.54  E-value: 3.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419   1 MATPGNLGSSVLASKTKTKKKHFVAQK-----VKLFRASDPLLSvLMWGVNHSINELSHVQiPVMLMPDDFKAYSKIKVD 75
Cdd:PLN03185 310 LVLNNSFSSTSRRAKRRQKKLVKEIKRpgetiIKGHRSYDLMLS-LQLGIRYTVGKITPIQ-RREVRPSDFGPRASFWMN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  76 nhlFNKEN---MPSH----FKFKEYCPMVFRNLRERFGID-----------------------------DQDFQYI---- 115
Cdd:PLN03185 388 ---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDaadymmsicgndalrelsspgksgsvfflSQDDRFMiktl 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 116 ------------------VECHGITLLPQFLGMYRLN-VDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREAsDKEKA 176
Cdd:PLN03185 465 rksevkvllrmlpdyhhhVKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSA-DKVEI 543
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 177 KELPTLKDNDFINEgqkIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEENDG 247
Cdd:PLN03185 544 DENTTLKDLDLNYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVVA 620
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 248 EEEGESDGTH---------PVGTPPDS--PGNTLNSSPPLAPGEFDPNID-----------------------VYGIKCH 293
Cdd:PLN03185 621 EEDTIEDEELsypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgvnmparaerIPGREDK 700
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818419 294 ENSPRKEVY----FMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 350
Cdd:PLN03185 701 EKQSFHEVYdvvlYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
34-232 8.18e-26

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: 105.46  E-value: 8.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  34 SDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFG 106
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhypdFRFKTYAPVAFRYFRELFG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 107 IDDQDFQY------IVECHGI--------------------------------------------TLLPQFLGMYRLNVD 136
Cdd:cd17308   75 IRPDDYLYslcnepLIELSNPgasgslfyvtsddefiiktvmhkeaeflqkllpgyymnlnqnprTLLPKFYGLYCVQSG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 137 GVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKVFLEKLKKDVEFL 215
Cdd:cd17308  155 GKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVL 234
                        250
                 ....*....|....*..
gi 578818419 216 AQLKLMDYSLLVGIHDV 232
Cdd:cd17308  235 ESFKIMDYSLLLGVHNI 251
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
34-233 1.04e-25

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: 105.46  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  34 SDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFG 106
Cdd:cd17306    3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhyndFRFKTYAPVAFRYFRELFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 107 IDDQDFQY------IVECHGI--------------------------------------------TLLPQFLGMYRLNVD 136
Cdd:cd17306   77 IRPDDYLYslcsepLIELSNSgasgslfyvssddefiiktvqhkeaeflqkllpgyymnlnqnprTLLPKFYGLYCVQAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 137 GVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINE-GQKIYIDDNNKKVFLEKLKKDVEFL 215
Cdd:cd17306  157 GKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLVL 236
                        250
                 ....*....|....*...
gi 578818419 216 AQLKLMDYSLLVGIHDVE 233
Cdd:cd17306  237 QSFKIMDYSLLVGIHNID 254
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
73-233 3.80e-25

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 106.57  E-value: 3.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  73 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDD--------------------------QDFQYIVEC----- 118
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEalvsllsryilwesnggksgsfflftRDYKFIIKTishse 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 119 -----------------HGITLLPQFLGMYRLNV-------DGVEIYVIVTRNVFSHRLsVYRKYDLKGSTVAREASDKE 174
Cdd:COG5253  398 hicfrpmifeyyvhvlfNPLTLLCKIFGFYRVKSrssisssKSRKIYFIVMENLFYPHG-IHRIFDLKGSMRNRHVERTG 476
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 175 KAKE-LPTLKDNDFINEGQKIyIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 233
Cdd:COG5253  477 KSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
36-350 1.98e-18

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: 84.72  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAyskiKVDNHLFNKENmpshFKFKEYCPMVFRNLRERFGIDDQDFQYI 115
Cdd:cd17304    5 SLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 116 VECHGI---------------------------------------------------TLLPQFLGMYRLNVDG-VEIYVI 143
Cdd:cd17304   77 LSPDEPylqfisnsksgqdffltndkrfflktqtkreakfllsilrkyvqhlenyphSLLVKFLGVHSIKLPGkKKKYFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 144 VTRNVFSHRLSVYRKYDLKGSTVAR-EASDKEKAKELPTLKDNDFinEGQKIYIDDNNKkVFLEKLKKDVEFLAQLKLMD 222
Cdd:cd17304  157 VMQSVFYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQRS-WFLRQVEIDTEFLKGLNVLD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 223 YSLLVG---IHDVERAEQEeveceendgeeegesdgthpvgtpPDSPgNTLNssppLAPGEfdpnidvygikchensprK 299
Cdd:cd17304  234 YSLLVGfqpLHSDENRRLL------------------------PNYK-NALH----VVDGP------------------E 266
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578818419 300 EVYFMAIIDILTHYDAKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFLDFI 350
Cdd:cd17304  267 YRYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWV 316
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
112-229 1.69e-17

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: 81.02  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818419 112 FQYIVECH---GITLLPQFLGMYRLNV------DGVEIYVIVTRNVFsHRLSVYRKYDLKGSTVAREASDKEKakELPTL 182
Cdd:cd17300   77 FEYMAKALfhkRPSLLAKILGVYRISVknsttnKTSKQDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAED--EDSVL 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 578818419 183 KDNDFINE--GQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGI 229
Cdd:cd17300  154 LDENFLEYtkGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
 
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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