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Conserved domains on  [gi|226371739|ref|NP_001139730|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 gamma isoform a [Homo sapiens]

Protein Classification

phosphatidylinositol 5-phosphate 4-kinase type-2 gamma( domain architecture ID 13022741)

phosphatidylinositol 5-phosphate 4-kinase type-2 gamma displays low enzymatic activity, and may be a GTP sensor; it has higher GTP-dependent kinase activity than ATP-dependent kinase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
46-418 0e+00

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: 546.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYLVS 125
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 126 LTRNPP-SESEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVDNEDSYMLVMR 204
Cdd:cd17311   81 LTRSPPySESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 205 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLL 284
Cdd:cd17311  161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 285 LGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidvyairsaegapq 364
Cdd:cd17311  241 LGIHDV-------------------------------------------------------------------------- 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226371739 365 keVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17311  247 --VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
 
Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
46-418 0e+00

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: 546.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYLVS 125
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 126 LTRNPP-SESEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVDNEDSYMLVMR 204
Cdd:cd17311   81 LTRSPPySESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 205 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLL 284
Cdd:cd17311  161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 285 LGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidvyairsaegapq 364
Cdd:cd17311  241 LGIHDV-------------------------------------------------------------------------- 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226371739 365 keVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17311  247 --VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
72-420 1.47e-145

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 417.55  E-value: 1.47e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739    72 LPDDFKASSKIKVNNHLfHRENLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPPSE---SEGSDGRFLIS 144
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLElssGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739   145 YDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHgNTLLPQFLGMYRVSVDNE---DSYMLVMRNMFSHRLPVHRKYDLKG 221
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739   222 SLVSREAsDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEA 300
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739   301 PVREDESEVDGDCSLTGPPAlvgsygtsPEGIGGYIHSHRPLGPGEFESfIDVYAIRSAEgapqkEVYFMGLIDILTQYD 380
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKA--------PDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYT 303
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 226371739   381 AKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITNIF 420
Cdd:smart00330 304 WDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
125-419 5.74e-67

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: 212.71  E-value: 5.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  125 SLTRNPPSE--SEG-SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVDNEDSYML 201
Cdd:pfam01504   1 LTGKSILSElsSPGkSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  202 VMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMD 280
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  281 YSLLLGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidvyairsae 360
Cdd:pfam01504 160 YSLLLGIHDL---------------------------------------------------------------------- 169
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 226371739  361 GAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITNI 419
Cdd:pfam01504 170 DEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
73-420 2.31e-42

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 158.84  E-value: 2.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  73 PDDFKASSKIKVNnhlFHREN---LPSH----FKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPPSESEGSDGR----F 141
Cdd:PLN03185 375 PSDFGPRASFWMN---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKsgsvF 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 142 LISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSVDNEDSY-MLVMRNMFSHRLPVHRKYDLK 220
Cdd:PLN03185 452 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLK 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 221 GSLVSREAsDKEKVKELPTLKDMDFlnkNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIH------------ 288
Cdd:PLN03185 531 GSSLGRSA-DKVEIDENTTLKDLDL---NYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsllp 606
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 289 ----------------DIIrgsEPEEEAPVR---------EDESEVDG------------------DCSLTGPPALVGSY 325
Cdd:PLN03185 607 ysrsitadglevvaeeDTI---EDEELSYPEglvlvprgaDDGSTVPGphirgsrlrasaagdeevDLLLPGTARLQIQL 683
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 326 GTSPEGIGGYIHSHRplgPGEFESFIDVYAIrsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHP 405
Cdd:PLN03185 684 GVNMPARAERIPGRE---DKEKQSFHEVYDV----------VLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDP 749
                        410
                 ....*....|....*
gi 226371739 406 EQYAKRFLDFITNIF 420
Cdd:PLN03185 750 TFYSKRFLEFIQKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
91-416 1.24e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 135.46  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  91 RENLPS---HFKFKEYCPQVFRNLRDRFGIDDQdyLVSLT-RNPPSESEG--SDGRFLISYDRTLVIKEVSSEDIADMHS 164
Cdd:COG5253  326 NEQFEEglyEFSCKDYFPEVFRELRALCGCDEA--LVSLLsRYILWESNGgkSGSFFLFTRDYKFIIKTISHSEHICFRP 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 165 NLSNYHQYiVKCHGNTLLPQFLGMYRVSVDNEDS-------YMLVMRNMFSHRLPvHRKYDLKGSLVSREASDKEKVKE- 236
Cdd:COG5253  404 MIFEYYVH-VLFNPLTLLCKIFGFYRVKSRSSISssksrkiYFIVMENLFYPHGI-HRIFDLKGSMRNRHVERTGKSMSv 481
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 237 LPTLKDMDFLNKNQKVYIGEEeKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIirgsepEEEAPVredesevdgdcslt 316
Cdd:COG5253  482 LLDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE------REEASV-------------- 540
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 317 gppalvgsygtspegiGGYIHSHRPLGPGEFesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAahaaktvkhga 396
Cdd:COG5253  541 ----------------GLIIDFIRTRMTGDK-------------------KLESGIKDKLTVGSFTKRK----------- 574
                        330       340
                 ....*....|....*....|
gi 226371739 397 gaEISTVHPEQYAKRFLDFI 416
Cdd:COG5253  575 --EPTAVTPRQYKNRFRKAM 592
 
Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
46-418 0e+00

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: 546.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYLVS 125
Cdd:cd17311    1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 126 LTRNPP-SESEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVDNEDSYMLVMR 204
Cdd:cd17311   81 LTRSPPySESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 205 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLL 284
Cdd:cd17311  161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 285 LGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidvyairsaegapq 364
Cdd:cd17311  241 LGIHDV-------------------------------------------------------------------------- 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226371739 365 keVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17311  247 --VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
46-418 0e+00

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: 522.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYLVS 125
Cdd:cd17305    1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 126 LTRNPPSESEG---SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVDNEDSYMLV 202
Cdd:cd17305   81 LTRSQPLASDSpgrSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 203 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYS 282
Cdd:cd17305  161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 283 LLLGIHDIIrgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidvyairsaega 362
Cdd:cd17305  241 LLVGIHDCI----------------------------------------------------------------------- 249
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226371739 363 pqkevYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17305  250 -----YFMAIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
36-418 1.63e-170

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: 479.93  E-value: 1.63e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  36 QKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRF 115
Cdd:cd17310    2 QKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 116 GIDDQDYLVSLTRNPP--SESEGSDG-RFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVS 192
Cdd:cd17310   82 GIDDQDYQNSVTRSAPinSDSQGRCGtRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 193 VDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEF 272
Cdd:cd17310  162 VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 273 LVQLKIMDYSLLLGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfid 352
Cdd:cd17310  242 LAQLKIMDYSLLVGIHDV-------------------------------------------------------------- 259
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226371739 353 vyairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17310  260 --------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
37-418 9.03e-159

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: 449.81  E-value: 9.03e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  37 KVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFG 116
Cdd:cd17309    1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 117 IDDQDYLVSLTRNPP--SESEGSDG-RFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSV 193
Cdd:cd17309   81 IDDQDFQNSLTRSAPlaNDSQARSGaRFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 194 DNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFL 273
Cdd:cd17309  161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 274 VQLKIMDYSLLLGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidv 353
Cdd:cd17309  241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226371739 354 yairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17309  258 -------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
72-420 1.47e-145

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 417.55  E-value: 1.47e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739    72 LPDDFKASSKIKVNNHLfHRENLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPPSE---SEGSDGRFLIS 144
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLElssGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739   145 YDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHgNTLLPQFLGMYRVSVDNE---DSYMLVMRNMFSHRLPVHRKYDLKG 221
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739   222 SLVSREAsDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEA 300
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739   301 PVREDESEVDGDCSLTGPPAlvgsygtsPEGIGGYIHSHRPLGPGEFESfIDVYAIRSAEgapqkEVYFMGLIDILTQYD 380
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKA--------PDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYT 303
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 226371739   381 AKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITNIF 420
Cdd:smart00330 304 WDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
97-418 2.42e-79

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: 245.56  E-value: 2.42e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  97 HFKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPP----SESEG-SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQ 171
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENlrelKESEGkSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 172 YIVKcHGNTLLPQFLGMYRVSVDNEDS-YMLVMRNMFSHRLPVHRKYDLKGSLVSREAS-DKEKVKELPTLKDMDFLNKN 249
Cdd:cd00139   82 HIKK-NPNSLLTRFYGLYSIKLQKGKKvYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 250 QKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtsp 329
Cdd:cd00139  161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 330 egiggyihshrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYA 409
Cdd:cd00139  202 -------------------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYA 244

                 ....*....
gi 226371739 410 KRFLDFITN 418
Cdd:cd00139  245 ERFLKFMES 253
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
71-418 6.78e-69

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: 221.02  E-value: 6.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  71 LLPDDFKASSKIKVNNHlfHRENLPSH---FKFKEYCPQVFRNLRDRFGIDDQDYLVSLT-RNPPSE--SEGSDGRFL-I 143
Cdd:cd17303   26 LTDADFKAVHKFSFDIT--GNELTPSSkydFKFKDYAPWVFRFLRELFGIDPADYLMSLTgKYILSElgSPGKSGSFFyF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 144 SYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSV-DNEDSYMLVMRNMFSHRLPVHRKYDLKGS 222
Cdd:cd17303  104 SRDYRFIIKTIHHSEHKFLRKILPDYYNH-VKENPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 223 LVSREAS-DKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDiirgsepeeeap 301
Cdd:cd17303  183 TVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHD------------ 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 302 vredesevdgdcsltgppalvgsygtspegIGGYIHShrplgpgefesfidvyaiRSAEGAPQKEVYFMGLIDILTQYDA 381
Cdd:cd17303  251 ------------------------------LDGGFQA------------------TDENNEPGDEIYYLGIIDILTPYNA 282
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 226371739 382 KKKAAHAAKTVKHgAGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17303  283 KKKLEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
125-419 5.74e-67

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: 212.71  E-value: 5.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  125 SLTRNPPSE--SEG-SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVDNEDSYML 201
Cdd:pfam01504   1 LTGKSILSElsSPGkSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  202 VMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMD 280
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  281 YSLLLGIHDIirgsepeeeapvredesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfidvyairsae 360
Cdd:pfam01504 160 YSLLLGIHDL---------------------------------------------------------------------- 169
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 226371739  361 GAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITNI 419
Cdd:pfam01504 170 DEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
54-418 1.44e-51

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: 175.90  E-value: 1.44e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  54 GVAHSINELSQVPPpVMLLPDDFKASSKIkvnnhLFHRE---NLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYLVSL 126
Cdd:cd17301   10 GIGHSVGSLSSKPE-RDVLMQDFEVVESV-----FFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGIKPDDYLLSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 127 TRNPPSE--SEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVDNEDSYMLVM 203
Cdd:cd17301   84 CNEPLRElsNPGASGSlFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGKNIRFVVM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 204 RNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEK-LKRDVEFLVQLKIMDYS 282
Cdd:cd17301  163 NNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKtIQRDCRVLESFKIMDYS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 283 LLLGIHDiirgsepeeeapvredesevdgdcsLTGPPAlvgsygtspegiggyihshrplgpgefesfidvyaiRSAEGa 362
Cdd:cd17301  243 LLLGVHN-------------------------LGGIPA------------------------------------RNSKG- 260
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226371739 363 pQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITN 418
Cdd:cd17301  261 -ERLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMAN 314
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
54-419 4.24e-51

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: 174.40  E-value: 4.24e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  54 GVAHSINELSQVPPpVMLLPDDFKASSKIKVNnhlFHRE--NLPSH----FKFKEYCPQVFRNLRDRFGIDDQDYLVSLT 127
Cdd:cd17302   11 GIRYSVGKIAPVAR-RDLKPSDFDPKAKQWFP---FPGSgsTPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSLC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 128 RN-------PPSESeGSdgRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRV-SVDNEDSY 199
Cdd:cd17302   87 GDdalrelsSPGKS-GS--VFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH-VKAYENTLLTKFFGVHRVkPVGGRKVR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 200 MLVMRNMFSHRLPVHRKYDLKGSLVSREAS-DKEKVKELPTLKDMDFlnkNQKVYIGEEEKKIFLEKLKRDVEFLVQLKI 278
Cdd:cd17302  163 FVVMGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNTTLKDLDL---DFKFRLEKGWRDALMRQIDADCAFLEALRI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 279 MDYSLLLGIHDiirgSEPEEEAPVRedesevdgdcsltgppalvgsygtspegiggyihshrplgpgefesfiDVyairs 358
Cdd:cd17302  240 MDYSLLLGVHF----RAGDSTGEPY------------------------------------------------DV----- 262
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371739 359 aegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAeISTVHPEQYAKRFLDFITNI 419
Cdd:cd17302  263 --------VLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRRFRDFIRKV 314
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
73-420 2.31e-42

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 158.84  E-value: 2.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  73 PDDFKASSKIKVNnhlFHREN---LPSH----FKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPPSESEGSDGR----F 141
Cdd:PLN03185 375 PSDFGPRASFWMN---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKsgsvF 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 142 LISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSVDNEDSY-MLVMRNMFSHRLPVHRKYDLK 220
Cdd:PLN03185 452 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLK 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 221 GSLVSREAsDKEKVKELPTLKDMDFlnkNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIH------------ 288
Cdd:PLN03185 531 GSSLGRSA-DKVEIDENTTLKDLDL---NYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsllp 606
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 289 ----------------DIIrgsEPEEEAPVR---------EDESEVDG------------------DCSLTGPPALVGSY 325
Cdd:PLN03185 607 ysrsitadglevvaeeDTI---EDEELSYPEglvlvprgaDDGSTVPGphirgsrlrasaagdeevDLLLPGTARLQIQL 683
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 326 GTSPEGIGGYIHSHRplgPGEFESFIDVYAIrsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHP 405
Cdd:PLN03185 684 GVNMPARAERIPGRE---DKEKQSFHEVYDV----------VLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDP 749
                        410
                 ....*....|....*
gi 226371739 406 EQYAKRFLDFITNIF 420
Cdd:PLN03185 750 TFYSKRFLEFIQKVF 764
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
47-417 1.17e-39

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: 144.36  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  47 LVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHlfhrENL-PSH----FKFKEYCPQVFRNLRDRFGIDDQD 121
Cdd:cd17307    3 IKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEG----SNLtPAHhypdFRFKTYAPLAFRYFRELFGIKPDD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 122 YLVSLTRNPPSE--SEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVDNEDS 198
Cdd:cd17307   79 YLYSICSEPLIElsNPGASGSlFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCMQSGGINI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 199 YMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQK-VYIGEEEKKIFLEKLKRDVEFLVQLK 277
Cdd:cd17307  158 RIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDgLYFDPETYNALMKTLQRDCRVLESFK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 278 IMDYSLLLGIHdiirgsepeeeapvredesevdgdcSLTGPPAlvgsygtspegiggyiHSHRplgpGEfesfidvyair 357
Cdd:cd17307  238 IMDYSLLLGIH-------------------------VLGGIPA----------------KNHK----GE----------- 261
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 358 saegapqKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIT 417
Cdd:cd17307  262 -------KLLLFMGIIDILQSYRLMKKLEHSWKALVYD-GDTVSVHRPSFYADRFLKFMN 313
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
47-308 4.28e-38

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: 140.52  E-value: 4.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  47 LVGVFLWGVAHSINELSQVPPPVMLLPDDFKasskikVNNHLFHRE--NL-PSH----FKFKEYCPQVFRNLRDRFGIDD 119
Cdd:cd17306    6 LKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFGIRP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 120 QDYLVSLTRNPPSE--SEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSVDNE 196
Cdd:cd17306   80 DDYLYSLCSEPLIElsNSGASGSlFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMN-LNQNPRTLLPKFYGLYCVQAGGK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 197 DSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKIFLEKLKRDVEFLVQ 275
Cdd:cd17306  159 NIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLVLQS 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 226371739 276 LKIMDYSLLLGIHDI--IRGSEPEEE-----APVREDESE 308
Cdd:cd17306  239 FKIMDYSLLVGIHNIdaRRGGTIETDdqmggIPARNSKGE 278
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
47-419 1.08e-37

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: 139.36  E-value: 1.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  47 LVGVFLWGVAHSINELSQVPPPVMLLPDDFKasskikVNNHLFHRE--NL-PSH----FKFKEYCPQVFRNLRDRFGIDD 119
Cdd:cd17308    4 LKGAIQLGIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhypdFRFKTYAPVAFRYFRELFGIRP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 120 QDYLVSLTRNPPSE--SEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVDNE 196
Cdd:cd17308   78 DDYLYSLCNEPLIElsNPGASGSlFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 197 DSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKIFLEKLKRDVEFLVQ 275
Cdd:cd17308  157 NIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVLES 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 276 LKIMDYSLLLGIHDiirgsepeeeapvredesevdgdcsltgppalvgsygtspegIGGyihshrplgpgefesfidvya 355
Cdd:cd17308  237 FKIMDYSLLLGVHN------------------------------------------IGG--------------------- 253
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226371739 356 IRSAEGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITNI 419
Cdd:cd17308  254 IPAVNGKGERLLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSNT 316
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
91-416 1.24e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 135.46  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  91 RENLPS---HFKFKEYCPQVFRNLRDRFGIDDQdyLVSLT-RNPPSESEG--SDGRFLISYDRTLVIKEVSSEDIADMHS 164
Cdd:COG5253  326 NEQFEEglyEFSCKDYFPEVFRELRALCGCDEA--LVSLLsRYILWESNGgkSGSFFLFTRDYKFIIKTISHSEHICFRP 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 165 NLSNYHQYiVKCHGNTLLPQFLGMYRVSVDNEDS-------YMLVMRNMFSHRLPvHRKYDLKGSLVSREASDKEKVKE- 236
Cdd:COG5253  404 MIFEYYVH-VLFNPLTLLCKIFGFYRVKSRSSISssksrkiYFIVMENLFYPHGI-HRIFDLKGSMRNRHVERTGKSMSv 481
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 237 LPTLKDMDFLNKNQKVYIGEEeKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIirgsepEEEAPVredesevdgdcslt 316
Cdd:COG5253  482 LLDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE------REEASV-------------- 540
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 317 gppalvgsygtspegiGGYIHSHRPLGPGEFesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAahaaktvkhga 396
Cdd:COG5253  541 ----------------GLIIDFIRTRMTGDK-------------------KLESGIKDKLTVGSFTKRK----------- 574
                        330       340
                 ....*....|....*....|
gi 226371739 397 gaEISTVHPEQYAKRFLDFI 416
Cdd:COG5253  575 --EPTAVTPRQYKNRFRKAM 592
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
108-287 1.10e-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: 126.47  E-value: 1.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 108 FRNLRDRFGIDDQDYLVSLTRNPPSESEG--SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGN---TLL 182
Cdd:cd17300   13 FHALRSLYCGGEDDFIRSLSRCVKWDASGgkSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHkrpSLL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 183 PQFLGMYRVSVDNEDS------YMLVMRNMFsHRLPVHRKYDLKGSLVSREASDKEKVKElpTLKDMDFLN--KNQKVYI 254
Cdd:cd17300   93 AKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAEDEDS--VLLDENFLEytKGSPLYL 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371739 255 GEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGI 287
Cdd:cd17300  170 REHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
54-416 1.03e-30

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: 120.16  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739  54 GVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHlfhrenlpSHFKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPP-- 131
Cdd:cd17304   13 GLRAAIQNSIDVPPKESLSDDDYTEVLTQVIPKH--------KGFEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyl 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 132 ---SESEgSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVD-NEDSYMLVMRNMF 207
Cdd:cd17304   85 qfiSNSK-SGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLEN-YPHSLLVKFLGVHSIKLPgKKKKYFIVMQSVF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 208 SHRLPVHRKYDLKGSLVSR-EASDKEKVKELPTLKDMDFLNKnqKVYIGEEeKKIFLEKLKRDVEFLVQLKIMDYSLLLG 286
Cdd:cd17304  163 YPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNFEGN--SINLGQQ-RSWFLRQVEIDTEFLKGLNVLDYSLLVG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371739 287 IHdiirgsepeeeaPVREDEsevdgdcsltgppalvgsygtspegiggyihsHRPLGPGEFEsfidvyAIRSAEGAPQKe 366
Cdd:cd17304  240 FQ------------PLHSDE--------------------------------NRRLLPNYKN------ALHVVDGPEYR- 268
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 226371739 367 vYFMGLIDILTQYDAKKKAAHAAKTVKHgAGAEISTVHPEQYAKRFLDFI 416
Cdd:cd17304  269 -YFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWV 316
 
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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