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Conserved domains on  [gi|6320414|ref|NP_010494|]
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1-phosphatidylinositol-4-phosphate 5-kinase [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
4-772 0e+00

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


:

Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 692.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    4 LRSQPPSVVPLHLTtstsrkteqepSLLHSaIIERHQDRSVPNSNSNPDSNHriKKDRNNHTSYHSSSNSESNMESPRLS 83
Cdd:COG5253   1 TEERPPISRSGTGI-----------SMTHD-KSTRPNDRSMSNDSSLCGLNQ--ASDANGNEYSPNNKVSKKDTFSDQLH 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   84 DGESSTPTSIEELNPTINNSRLVKRNYSISIDPLHDNSNNNTDDDHPNTITSPRPNSTSNKEMQKYSFPEGKESKKIttP 163
Cdd:COG5253  67 DALSKEFTLERERDRLQLNKRKYQAIRLQTSTPIVEIFKNNKDAVDPPNHTRSSGNNLSNANVKTLSAPVGEHSRSN--N 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  164 SLNSNNCLDLDNSSLVHTDSYIQDLNDDHILLNKRVSRRssrisAVTATSTtikQRRNTQdsnLPnipfhASKHSqilPM 243
Cdd:COG5253 145 PPNLDQNLDTEPESSISQWGELQLNPSGKTLSSQPSRKP-----TSENPKS---ESDNSK---LP-----TSVNS---PL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  244 DDSDVIKLANGDTSMKPNSATKISHSMTSLPLHPLPQPSQKSKQYHMISKSTTSLPPENDHYYQHSRGtnhnhaanaaav 323
Cdd:COG5253 206 PDKSLLKRTLSNFWAERNSYNWKPLVYPSCPSEHIFSDSDVIIREDEPSSLIAFCLSTSDYRNKMMRL------------ 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  324 nnntttttaatglkrsesataeikkmrqsllhkremkRKRKTflvDDDRVLIGNKVSEGHVNFIIAYNMLTGIRVAVSRC 403
Cdd:COG5253 274 -------------------------------------RDSET---MDERLLNGMPLEGGHRNPQESYNMLTGIRVTLSRI 313
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  404 SGIMKPLTpadfrftkklafDYHGNELTPSSQYAFKFKDYCPEVFRELRALFGLDPAdyLVSLTSKYILSELNsPGKSGS 483
Cdd:COG5253 314 EEIMIKKT------------DTHLNEQFEEGLYEFSCKDYFPEVFRELRALCGCDEA--LVSLLSRYILWESN-GGKSGS 378
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  484 FFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISFQnKIKHRKIYFLVMNNLFPPHLd 563
Cdd:COG5253 379 FFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNPLTLLCKIFGFYRVKSRSSIS-SSKSRKIYFIVMENLFYPHG- 456
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  564 IHITYDLKGSTWGRftnlDKERLAKDRSYRPVMKDLNWLEEGQKIKFGpLKKKTFLTQLKKDVELLAKLNTMDYSLLIGI 643
Cdd:COG5253 457 IHRIFDLKGSMRNR----HVERTGKSMSVLLDMNDVEWIRESPKIVFG-LKKKLLLSQVWNDVLFLSKLNIMDYSLLVGI 531
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  644 HDInkakeddLQLADTASIEEQPQTQgpirtgtgtvvrhffrefeggirasdqfnNDVDLIYYVGIIDFLTNYSVMKkle 723
Cdd:COG5253 532 DDE-------REEASVGLIIDFIRTR-----------------------------MTGDKKLESGIKDKLTVGSFTK--- 572
                       730       740       750       760
                ....*....|....*....|....*....|....*....|....*....
gi 6320414  724 tfwrslrhdTKLVSAIPPRDYANRFYEFIEDSVDPLPQKKTQSSYRDDP 772
Cdd:COG5253 573 ---------RKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEGFKTNP 612
 
Name Accession Description Interval E-value
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
4-772 0e+00

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 692.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    4 LRSQPPSVVPLHLTtstsrkteqepSLLHSaIIERHQDRSVPNSNSNPDSNHriKKDRNNHTSYHSSSNSESNMESPRLS 83
Cdd:COG5253   1 TEERPPISRSGTGI-----------SMTHD-KSTRPNDRSMSNDSSLCGLNQ--ASDANGNEYSPNNKVSKKDTFSDQLH 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   84 DGESSTPTSIEELNPTINNSRLVKRNYSISIDPLHDNSNNNTDDDHPNTITSPRPNSTSNKEMQKYSFPEGKESKKIttP 163
Cdd:COG5253  67 DALSKEFTLERERDRLQLNKRKYQAIRLQTSTPIVEIFKNNKDAVDPPNHTRSSGNNLSNANVKTLSAPVGEHSRSN--N 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  164 SLNSNNCLDLDNSSLVHTDSYIQDLNDDHILLNKRVSRRssrisAVTATSTtikQRRNTQdsnLPnipfhASKHSqilPM 243
Cdd:COG5253 145 PPNLDQNLDTEPESSISQWGELQLNPSGKTLSSQPSRKP-----TSENPKS---ESDNSK---LP-----TSVNS---PL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  244 DDSDVIKLANGDTSMKPNSATKISHSMTSLPLHPLPQPSQKSKQYHMISKSTTSLPPENDHYYQHSRGtnhnhaanaaav 323
Cdd:COG5253 206 PDKSLLKRTLSNFWAERNSYNWKPLVYPSCPSEHIFSDSDVIIREDEPSSLIAFCLSTSDYRNKMMRL------------ 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  324 nnntttttaatglkrsesataeikkmrqsllhkremkRKRKTflvDDDRVLIGNKVSEGHVNFIIAYNMLTGIRVAVSRC 403
Cdd:COG5253 274 -------------------------------------RDSET---MDERLLNGMPLEGGHRNPQESYNMLTGIRVTLSRI 313
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  404 SGIMKPLTpadfrftkklafDYHGNELTPSSQYAFKFKDYCPEVFRELRALFGLDPAdyLVSLTSKYILSELNsPGKSGS 483
Cdd:COG5253 314 EEIMIKKT------------DTHLNEQFEEGLYEFSCKDYFPEVFRELRALCGCDEA--LVSLLSRYILWESN-GGKSGS 378
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  484 FFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISFQnKIKHRKIYFLVMNNLFPPHLd 563
Cdd:COG5253 379 FFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNPLTLLCKIFGFYRVKSRSSIS-SSKSRKIYFIVMENLFYPHG- 456
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  564 IHITYDLKGSTWGRftnlDKERLAKDRSYRPVMKDLNWLEEGQKIKFGpLKKKTFLTQLKKDVELLAKLNTMDYSLLIGI 643
Cdd:COG5253 457 IHRIFDLKGSMRNR----HVERTGKSMSVLLDMNDVEWIRESPKIVFG-LKKKLLLSQVWNDVLFLSKLNIMDYSLLVGI 531
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  644 HDInkakeddLQLADTASIEEQPQTQgpirtgtgtvvrhffrefeggirasdqfnNDVDLIYYVGIIDFLTNYSVMKkle 723
Cdd:COG5253 532 DDE-------REEASVGLIIDFIRTR-----------------------------MTGDKKLESGIKDKLTVGSFTK--- 572
                       730       740       750       760
                ....*....|....*....|....*....|....*....|....*....
gi 6320414  724 tfwrslrhdTKLVSAIPPRDYANRFYEFIEDSVDPLPQKKTQSSYRDDP 772
Cdd:COG5253 573 ---------RKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEGFKTNP 612
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
386-754 0e+00

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: 559.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  386 FIIAYNMLTGIRVAVSRCSGIMK-PLTPADFRFTKKLAFDYHGNELTPSSQYAFKFKDYCPEVFRELRALFGLDPADYLV 464
Cdd:cd17303   1 YVLMYNMLTGIRVAVSRCAAKVDrELTDADFKAVHKFSFDITGNELTPSSKYDFKFKDYAPWVFRFLRELFGIDPADYLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  465 SLTSKYILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPisfqnki 544
Cdd:cd17303  81 SLTGKYILSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKMP------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  545 KHRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNLDKERlakdRSYRPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKK 624
Cdd:cd17303 154 RGRKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPEDKLA----KGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKR 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  625 DVELLAKLNTMDYSLLIGIHDInkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefEGGIRASDQFNNDVDLI 704
Cdd:cd17303 230 DVEFLASLNIMDYSLLVGIHDL-----------------------------------------DGGFQATDENNEPGDEI 268
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6320414  705 YYVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIED 754
Cdd:cd17303 269 YYLGIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
411-756 5.63e-141

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 418.71  E-value: 5.63e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     411 TPADFRFTKKLAFDYHGN-ELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYiLSELNSPGKSGSFFYYS 488
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSAdFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSP-PLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     489 RDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISfqnkiKHRKIYFLVMNNLFPPHLDIHITY 568
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGG-----TEKKIYFLVMENLFYSDLKVHRKY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     569 DLKGSTWGRFTNLDKERlakdrsYRPVMKDLNWLEE-GQKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDIN 647
Cdd:smart00330 155 DLKGSTRGREADKKKVK------ELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     648 KAKEDDLQLADTASIEEQPQ-----------TQGPIRTGTGTVVRHFFRE-FEGGIRASdqfnndvDLIYYVGIIDFLTN 715
Cdd:smart00330 229 RGQREEIELPPVYGSDESPSsessnggkapdITGNLLVSNSPDGDGPFGGiPARAIRAR-------RVVLYLGIIDILQT 301
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 6320414     716 YSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIEDSV 756
Cdd:smart00330 302 YTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
466-754 3.49e-116

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: 350.23  E-value: 3.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    466 LTSKYILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMpisfqnkiK 545
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKP--------G 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    546 HRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNlDKERLAKDrsyRPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKKD 625
Cdd:pfam01504  73 GKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAK-KKEREKDE---PTTLKDLDFLERKLKLRLGPEKREALLKQLERD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    626 VELLAKLNTMDYSLLIGIHDInkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggirasdqfNNDVDLIY 705
Cdd:pfam01504 149 CEFLESLNIMDYSLLLGIHDL---------------------------------------------------DEDGKEIY 177
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 6320414    706 YVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIED 754
Cdd:pfam01504 178 YLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEK 226
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
336-753 1.10e-64

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 230.10  E-value: 1.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   336 LKRSESATAEIKKMRQSLlHKREMKRKrktflvdddrvliGNKVSEGHVNFIIAYNMLTGIRVAVSRCSGIMK-PLTPAD 414
Cdd:PLN03185 312 LNNSFSSTSRRAKRRQKK-LVKEIKRP-------------GETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRrEVRPSD 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   415 F--RFTKKLAFDYHGNELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILSELNSPGKSGSFFYYSRDY 491
Cdd:PLN03185 378 FgpRASFWMNFPKAGSQLTPSHQSEdFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDD 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   492 KYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKmPISFQnkikhrKIYFLVMNNLFPPHLDIHITYDLK 571
Cdd:PLN03185 458 RFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIK-PSSGQ------KFRFVVMGNMFCTELRIHRRFDLK 530
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   572 GSTWGRFTN---LDKERLAKDRsyrpvmkDLNWleegqKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIH---- 644
Cdd:PLN03185 531 GSSLGRSADkveIDENTTLKDL-------DLNY-----SFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrap 598
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   645 -------DINKAKEDD----LQLADTASIEEQPQTQGPI------RTGTGTVVRHffreFEGG-IRASDQFNNDVDL--- 703
Cdd:PLN03185 599 qhlrsllPYSRSITADglevVAEEDTIEDEELSYPEGLVlvprgaDDGSTVPGPH----IRGSrLRASAAGDEEVDLllp 674
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   704 -------------------------------------IYYVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYAN 746
Cdd:PLN03185 675 gtarlqiqlgvnmparaeripgredkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSK 754

                 ....*..
gi 6320414   747 RFYEFIE 753
Cdd:PLN03185 755 RFLEFIQ 761
 
Name Accession Description Interval E-value
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
4-772 0e+00

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 692.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    4 LRSQPPSVVPLHLTtstsrkteqepSLLHSaIIERHQDRSVPNSNSNPDSNHriKKDRNNHTSYHSSSNSESNMESPRLS 83
Cdd:COG5253   1 TEERPPISRSGTGI-----------SMTHD-KSTRPNDRSMSNDSSLCGLNQ--ASDANGNEYSPNNKVSKKDTFSDQLH 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   84 DGESSTPTSIEELNPTINNSRLVKRNYSISIDPLHDNSNNNTDDDHPNTITSPRPNSTSNKEMQKYSFPEGKESKKIttP 163
Cdd:COG5253  67 DALSKEFTLERERDRLQLNKRKYQAIRLQTSTPIVEIFKNNKDAVDPPNHTRSSGNNLSNANVKTLSAPVGEHSRSN--N 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  164 SLNSNNCLDLDNSSLVHTDSYIQDLNDDHILLNKRVSRRssrisAVTATSTtikQRRNTQdsnLPnipfhASKHSqilPM 243
Cdd:COG5253 145 PPNLDQNLDTEPESSISQWGELQLNPSGKTLSSQPSRKP-----TSENPKS---ESDNSK---LP-----TSVNS---PL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  244 DDSDVIKLANGDTSMKPNSATKISHSMTSLPLHPLPQPSQKSKQYHMISKSTTSLPPENDHYYQHSRGtnhnhaanaaav 323
Cdd:COG5253 206 PDKSLLKRTLSNFWAERNSYNWKPLVYPSCPSEHIFSDSDVIIREDEPSSLIAFCLSTSDYRNKMMRL------------ 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  324 nnntttttaatglkrsesataeikkmrqsllhkremkRKRKTflvDDDRVLIGNKVSEGHVNFIIAYNMLTGIRVAVSRC 403
Cdd:COG5253 274 -------------------------------------RDSET---MDERLLNGMPLEGGHRNPQESYNMLTGIRVTLSRI 313
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  404 SGIMKPLTpadfrftkklafDYHGNELTPSSQYAFKFKDYCPEVFRELRALFGLDPAdyLVSLTSKYILSELNsPGKSGS 483
Cdd:COG5253 314 EEIMIKKT------------DTHLNEQFEEGLYEFSCKDYFPEVFRELRALCGCDEA--LVSLLSRYILWESN-GGKSGS 378
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  484 FFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISFQnKIKHRKIYFLVMNNLFPPHLd 563
Cdd:COG5253 379 FFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNPLTLLCKIFGFYRVKSRSSIS-SSKSRKIYFIVMENLFYPHG- 456
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  564 IHITYDLKGSTWGRftnlDKERLAKDRSYRPVMKDLNWLEEGQKIKFGpLKKKTFLTQLKKDVELLAKLNTMDYSLLIGI 643
Cdd:COG5253 457 IHRIFDLKGSMRNR----HVERTGKSMSVLLDMNDVEWIRESPKIVFG-LKKKLLLSQVWNDVLFLSKLNIMDYSLLVGI 531
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  644 HDInkakeddLQLADTASIEEQPQTQgpirtgtgtvvrhffrefeggirasdqfnNDVDLIYYVGIIDFLTNYSVMKkle 723
Cdd:COG5253 532 DDE-------REEASVGLIIDFIRTR-----------------------------MTGDKKLESGIKDKLTVGSFTK--- 572
                       730       740       750       760
                ....*....|....*....|....*....|....*....|....*....
gi 6320414  724 tfwrslrhdTKLVSAIPPRDYANRFYEFIEDSVDPLPQKKTQSSYRDDP 772
Cdd:COG5253 573 ---------RKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEGFKTNP 612
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
386-754 0e+00

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: 559.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  386 FIIAYNMLTGIRVAVSRCSGIMK-PLTPADFRFTKKLAFDYHGNELTPSSQYAFKFKDYCPEVFRELRALFGLDPADYLV 464
Cdd:cd17303   1 YVLMYNMLTGIRVAVSRCAAKVDrELTDADFKAVHKFSFDITGNELTPSSKYDFKFKDYAPWVFRFLRELFGIDPADYLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  465 SLTSKYILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPisfqnki 544
Cdd:cd17303  81 SLTGKYILSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKMP------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  545 KHRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNLDKERlakdRSYRPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKK 624
Cdd:cd17303 154 RGRKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPEDKLA----KGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKR 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  625 DVELLAKLNTMDYSLLIGIHDInkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefEGGIRASDQFNNDVDLI 704
Cdd:cd17303 230 DVEFLASLNIMDYSLLVGIHDL-----------------------------------------DGGFQATDENNEPGDEI 268
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6320414  705 YYVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIED 754
Cdd:cd17303 269 YYLGIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
411-756 5.63e-141

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 418.71  E-value: 5.63e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     411 TPADFRFTKKLAFDYHGN-ELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYiLSELNSPGKSGSFFYYS 488
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSAdFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSP-PLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     489 RDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISfqnkiKHRKIYFLVMNNLFPPHLDIHITY 568
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGG-----TEKKIYFLVMENLFYSDLKVHRKY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     569 DLKGSTWGRFTNLDKERlakdrsYRPVMKDLNWLEE-GQKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDIN 647
Cdd:smart00330 155 DLKGSTRGREADKKKVK------ELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414     648 KAKEDDLQLADTASIEEQPQ-----------TQGPIRTGTGTVVRHFFRE-FEGGIRASdqfnndvDLIYYVGIIDFLTN 715
Cdd:smart00330 229 RGQREEIELPPVYGSDESPSsessnggkapdITGNLLVSNSPDGDGPFGGiPARAIRAR-------RVVLYLGIIDILQT 301
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 6320414     716 YSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIEDSV 756
Cdd:smart00330 302 YTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
466-754 3.49e-116

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: 350.23  E-value: 3.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    466 LTSKYILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMpisfqnkiK 545
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKP--------G 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    546 HRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNlDKERLAKDrsyRPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKKD 625
Cdd:pfam01504  73 GKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAK-KKEREKDE---PTTLKDLDFLERKLKLRLGPEKREALLKQLERD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414    626 VELLAKLNTMDYSLLIGIHDInkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggirasdqfNNDVDLIY 705
Cdd:pfam01504 149 CEFLESLNIMDYSLLLGIHDL---------------------------------------------------DEDGKEIY 177
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 6320414    706 YVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIED 754
Cdd:pfam01504 178 YLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEK 226
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
436-754 5.64e-106

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: 324.91  E-value: 5.64e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  436 YAFKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILSEL-NSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYY 514
Cdd:cd00139   1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  515 NHVRDNPNTLICQFYGLHRVKMPisfqnkiKHRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNLDKERLAKDrsyrP 594
Cdd:cd00139  81 EHIKKNPNSLLTRFYGLYSIKLQ-------KGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEKEKKKGL----K 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  595 VMKDLNWLEEGQKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHdinkakeddlqladtasieeqpqtqgpirt 674
Cdd:cd00139 150 VLKDLDFLEKGEKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH------------------------------ 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  675 gtgtvvrhffrefeggirasdqfnndvDLIYYVGIIDFLTNYSVMKKLETFWRSLRHDTK-LVSAIPPRDYANRFYEFIE 753
Cdd:cd00139 200 ---------------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKDsGISCVPPDEYAERFLKFME 252

                .
gi 6320414  754 D 754
Cdd:cd00139 253 S 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
391-754 1.12e-89

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: 284.57  E-value: 1.12e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  391 NMLTGIRVAVSRCSGIM-KPLTPADFRFTKKLAFDYHGNELTPSSQYA--FKFKDYCPEVFRELRALFGLDPADYLVSLT 467
Cdd:cd17302   7 NLQLGIRYSVGKIAPVArRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSsdFKWKDYCPMVFRNLRELFGIDAADYMLSLC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  468 SKYILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISfqnkikhR 547
Cdd:cd17302  87 GDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVKPVGG-------R 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  548 KIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTnlDKERLAKDRsyRPVMKDLNWleeGQKIKFGPLKKKTFLTQLKKDVE 627
Cdd:cd17302 160 KVRFVVMGNLFCTELRIHRRFDLKGSTHGRTT--GKPESEIDP--NTTLKDLDL---DFKFRLEKGWRDALMRQIDADCA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  628 LLAKLNTMDYSLLIGIHdinkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggIRASDQFNNDVDLIYYV 707
Cdd:cd17302 233 FLEALRIMDYSLLLGVH----------------------------------------------FRAGDSTGEPYDVVLYF 266
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 6320414  708 GIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIED 754
Cdd:cd17302 267 GIIDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIRK 313
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
410-754 9.75e-68

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: 226.00  E-value: 9.75e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  410 LTPADFRFTKKLAFDYHG--NELTPSSqyaFKFKDYCPEVFRELRALFGLDPADYLVSLTsKYILSELNSPGKSGSFFYY 487
Cdd:cd17305  26 LMPDDFKAYSKIKVDNHLfnKENLPSH---FKVKEYCPLVFRNLRERFGIDDDDYLNSLT-RSQPLASDSPGRSGSRFLV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  488 SRDYKYIIKTIHHSEHIHLRKHIQEYYNH-VRDNPNTLICQFYGLHRVKmpisfqnkIKHRKIYFLVMNNLFPPHLDIHI 566
Cdd:cd17305 102 SYDKKYVIKTISSEEVAQMHHILKQYHQYiVERHGKTLLPQYLGMYRIT--------VNGVETYLVVMRNVFSPRLPIHK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  567 TYDLKGSTWGRFTNlDKERlAKDRsyrPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDI 646
Cdd:cd17305 174 KYDLKGSTVDRQAS-DKEK-AKDL---PTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDC 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  647 nkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggirasdqfnndvdlIYYVGIIDFLTNYSVMKKLETFW 726
Cdd:cd17305 249 ---------------------------------------------------------IYFMAIIDILTHYGAKKRAAHAA 271
                       330       340
                ....*....|....*....|....*....
gi 6320414  727 RSLRHDTKL-VSAIPPRDYANRFYEFIED 754
Cdd:cd17305 272 KTVKHGAGAeISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
409-756 7.10e-66

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: 221.74  E-value: 7.10e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  409 PLTPADFRFTKKLAFDYHGNELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKyILSELNSPGKSGSFFYY 487
Cdd:cd17301  25 DVLMQDFEVVESVFFPSEGSTLTPAHHYSdFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNE-PLRELSNPGASGSLFYL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  488 SRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMpisfqnkiKHRKIYFLVMNNLFPPHLDIHIT 567
Cdd:cd17301 104 THDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQS--------GGKNIRFVVMNNLLPSNIKMHEK 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  568 YDLKGSTWGRFTNlDKERLAKDrsyrPVMKDLNWLEEGQK-IKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDI 646
Cdd:cd17301 176 YDLKGSTYKRKAS-KKERQKKS----PTLKDLDFMEDHPEgILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGVHNL 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  647 nkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeGGIRASDqfNNDVDLIYYVGIIDFLTNYSVMKKLETFW 726
Cdd:cd17301 251 ------------------------------------------GGIPARN--SKGERLLLFIGIIDILQSYRLKKKLEHTW 286
                       330       340       350
                ....*....|....*....|....*....|
gi 6320414  727 RSLRHDTKLVSAIPPRDYANRFYEFIEDSV 756
Cdd:cd17301 287 KSVVHDGDTVSVHRPSFYAERFQNFMANTV 316
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
336-753 1.10e-64

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 230.10  E-value: 1.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   336 LKRSESATAEIKKMRQSLlHKREMKRKrktflvdddrvliGNKVSEGHVNFIIAYNMLTGIRVAVSRCSGIMK-PLTPAD 414
Cdd:PLN03185 312 LNNSFSSTSRRAKRRQKK-LVKEIKRP-------------GETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRrEVRPSD 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   415 F--RFTKKLAFDYHGNELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILSELNSPGKSGSFFYYSRDY 491
Cdd:PLN03185 378 FgpRASFWMNFPKAGSQLTPSHQSEdFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDD 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   492 KYIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKmPISFQnkikhrKIYFLVMNNLFPPHLDIHITYDLK 571
Cdd:PLN03185 458 RFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIK-PSSGQ------KFRFVVMGNMFCTELRIHRRFDLK 530
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   572 GSTWGRFTN---LDKERLAKDRsyrpvmkDLNWleegqKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIH---- 644
Cdd:PLN03185 531 GSSLGRSADkveIDENTTLKDL-------DLNY-----SFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrap 598
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   645 -------DINKAKEDD----LQLADTASIEEQPQTQGPI------RTGTGTVVRHffreFEGG-IRASDQFNNDVDL--- 703
Cdd:PLN03185 599 qhlrsllPYSRSITADglevVAEEDTIEDEELSYPEGLVlvprgaDDGSTVPGPH----IRGSrLRASAAGDEEVDLllp 674
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414   704 -------------------------------------IYYVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYAN 746
Cdd:PLN03185 675 gtarlqiqlgvnmparaeripgredkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSK 754

                 ....*..
gi 6320414   747 RFYEFIE 753
Cdd:PLN03185 755 RFLEFIQ 761
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
414-765 1.60e-56

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: 196.37  E-value: 1.60e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  414 DFRFTKKLAFDYHGNELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILsELNSPGKSGSFFYYSRDYK 492
Cdd:cd17307  30 DFYVVESVFLPSEGSNLTPAHHYPdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLI-ELSNPGASGSLFYVTSDDE 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  493 YIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMPISfqnkikhrKIYFLVMNNLFPPHLDIHITYDLKG 572
Cdd:cd17307 109 FIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGI--------NIRIVVMNNVLPRSVKMHYKYDLKG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  573 STWGRFTNlDKERlakdRSYRPVMKDLNWLEEGQK-IKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDInkake 651
Cdd:cd17307 181 STYKRRAS-RKER----EKSCPTYKDLDFLQDMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIHVL----- 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  652 ddlqladtasieeqpqtqgpirtgtgtvvrhffrefeGGIRASDqfNNDVDLIYYVGIIDFLTNYSVMKKLETFWRSLRH 731
Cdd:cd17307 251 -------------------------------------GGIPAKN--HKGEKLLLFMGIIDILQSYRLMKKLEHSWKALVY 291
                       330       340       350
                ....*....|....*....|....*....|....
gi 6320414  732 DTKLVSAIPPRDYANRFYEFIEDSVdplpQKKTQ 765
Cdd:cd17307 292 DGDTVSVHRPSFYADRFLKFMNSRV----FKKVQ 321
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
414-756 1.50e-54

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: 190.98  E-value: 1.50e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  414 DFRFTKKLAFDYHGNELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILsELNSPGKSGSFFYYSRDYK 492
Cdd:cd17308  31 DFYVVESIFFPSEGSNLTPAHHYPdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLI-ELSNPGASGSLFYVTSDDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  493 YIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMpisfqnkiKHRKIYFLVMNNLFPPHLDIHITYDLKG 572
Cdd:cd17308 110 FIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQS--------GGKNIRVVVMNNILPRVVKMHLKFDLKG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  573 STWGRFTNlDKERLAKdrsyRPVMKDLNWLE---EGQKIK---FGPLKKKtfltqLKKDVELLAKLNTMDYSLLIGIHDI 646
Cdd:cd17308 182 STYKRRAS-KKEREKS----KPTFKDLDFMQdmpEGLMLDadtFSALVKT-----LQRDCLVLESFKIMDYSLLLGVHNI 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  647 nkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeGGIRASDqfNNDVDLIYYVGIIDFLTNYSVMKKLETFW 726
Cdd:cd17308 252 ------------------------------------------GGIPAVN--GKGERLLLYIGIIDILQSYRLIKKLEHTW 287
                       330       340       350
                ....*....|....*....|....*....|
gi 6320414  727 RSLRHDTKLVSAIPPRDYANRFYEFIEDSV 756
Cdd:cd17308 288 KALVHDGDTVSVHRPSFYAERFFKFMSNTV 317
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
414-756 7.48e-54

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: 189.44  E-value: 7.48e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  414 DFRFTKKLAFDYHGNELTPSSQYA-FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILsELNSPGKSGSFFYYSRDYK 492
Cdd:cd17306  33 DFYVVESIFFPSEGSNLTPAHHYNdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLI-ELSNSGASGSLFYVSSDDE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  493 YIIKTIHHSEHIHLRKHIQEYYNHVRDNPNTLICQFYGLHRVKMpisfqnkiKHRKIYFLVMNNLFPPHLDIHITYDLKG 572
Cdd:cd17306 112 FIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQA--------GGKNIRIVVMNNLLPRSVKMHLKYDLKG 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  573 STWGRFTNLdKERlakdRSYRPVMKDLNWLEE-GQKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDINKAKe 651
Cdd:cd17306 184 STYKRRASQ-KER----EKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNIDARR- 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  652 ddlqladTASIEEQPQTQG-PIRTGTGTvvrhffrefeggirasdqfnndvDLIYYVGIIDFLTNYSVMKKLETFWRSLR 730
Cdd:cd17306 258 -------GGTIETDDQMGGiPARNSKGE-----------------------RLLLYIGIIDILQSYRFVKKLEHSWKALV 307
                       330       340
                ....*....|....*....|....*.
gi 6320414  731 HDTKLVSAIPPRDYANRFYEFIEDSV 756
Cdd:cd17306 308 HDGDTVSVHRPGFYAERFQRFMCNTV 333
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
392-754 1.23e-49

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: 177.16  E-value: 1.23e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  392 MLTGIRVAVSRCSGIMKP--LTPADFRFTKKLAFDYH--GNELTPSSqyaFKFKDYCPEVFRELRALFGLDPADYLVSLT 467
Cdd:cd17310  17 LMWGVNHTINELSNVPVPvmLMPDDFKAYSKIKVDNHlfNKENLPSR---FKFKEYCPMVFRNLRERFGIDDQDYQNSVT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  468 SKYILSElNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRD-NPNTLICQFYGLHRVKmpisfqnkIKH 546
Cdd:cd17310  94 RSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLT--------VDG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  547 RKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNlDKERlAKDRsyrPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKKDV 626
Cdd:cd17310 165 VETYMVVTRNVFSHRLTVHRKYDLKGSTVSREAS-DKEK-AKDL---PTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  627 ELLAKLNTMDYSLLIGIHDInkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggirasdqfnndvdlIYY 706
Cdd:cd17310 240 EFLAQLKIMDYSLLVGIHDV---------------------------------------------------------VYF 262
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6320414  707 VGIIDFLTNYSVMKKLETFWRSLRHDTKL-VSAIPPRDYANRFYEFIED 754
Cdd:cd17310 263 MAIIDILTPYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
391-752 2.53e-47

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: 170.54  E-value: 2.53e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  391 NMLTGIRVAVSRCSGIMKP--LTPADFRFTKKLAFDYH--GNELTPSSqyaFKFKDYCPEVFRELRALFGLDPADYLVSL 466
Cdd:cd17309  14 VLMWGVNHSINELSHVQIPvmLMPDDFKAYSKIKVDNHlfNKENMPSH---FKFKEYCPMVFRNLRERFGIDDQDFQNSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  467 TSKYILSElNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRD-NPNTLICQFYGLHRVKmpisfqnkIK 545
Cdd:cd17309  91 TRSAPLAN-DSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVEcHGNTLLPQFLGMYRLT--------VD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  546 HRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNlDKERlAKDRsyrPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKKD 625
Cdd:cd17309 162 GVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREAS-DKEK-AKEL---PTLKDNDFINDGQKIYIDENNKKMFLEKLKKD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  626 VELLAKLNTMDYSLLIGIHDInkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggirasdqfnndvdlIY 705
Cdd:cd17309 237 VEFLAQLKLMDYSLLVGIHDV---------------------------------------------------------VY 259
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 6320414  706 YVGIIDFLTNYSVMKKLETFWRSLRHDTKL-VSAIPPRDYANRFYEFI 752
Cdd:cd17309 260 FMAIIDILTHYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFLDFI 307
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
438-754 3.46e-46

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: 167.53  E-value: 3.46e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  438 FKFKDYCPEVFRELRALFGLDPADYLVSLTSKYILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHV 517
Cdd:cd17304  49 FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  518 RDNPNTLICQFYGLHRVKMPISfqnkikhRKIYFLVMNNLFPPHLDIHITYDLKGSTWGRFTNLDKErlakDRSYRPVMK 597
Cdd:cd17304 129 ENYPHSLLVKFLGVHSIKLPGK-------KKKYFIVMQSVFYPDERINERYDIKGCQVSRYTDPEPE----GSQIIVVLK 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  598 DLNWleEGQKIKFGPlKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDINkakeddlqladtaSIEEQ---PQTQGPIRT 674
Cdd:cd17304 198 DLNF--EGNSINLGQ-QRSWFLRQVEIDTEFLKGLNVLDYSLLVGFQPLH-------------SDENRrllPNYKNALHV 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  675 GTGTVVRhffrefeggirasdqfnndvdliYYVGIIDFLTNYSVMKKLETFWRSLRHDTKLVSAIPPRDYANRFYEFIED 754
Cdd:cd17304 262 VDGPEYR-----------------------YFVGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVED 318
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
410-754 1.29e-42

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: 156.95  E-value: 1.29e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  410 LTPADFRFTKKLAFDYH--GNELTPSSqyaFKFKDYCPEVFRELRALFGLDPADYLVSLTSKyilSELNSPGKSGSFFYY 487
Cdd:cd17311  26 LLPDDFKANSKIKVNNHlfNRENLPSH---FKFKEYCPQVFRNLRERFGIDDQDYQVSLTRS---PPYSESEGSDGRFLL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  488 SRDYKYIIKTIHHSEHIHLRKHIQEYYNH-VRDNPNTLICQFYGLHRVKmpisfqnkIKHRKIYFLVMNNLFPPHLDIHI 566
Cdd:cd17311 100 SYDRTLVIKEISSEDVADMHSILSHYHQYiVKCHGNTLLPQFLGMYRLS--------VDNEDSYMLVMRNMFSHRLPVHR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  567 TYDLKGSTWGRFTNlDKERLAKdrsyRPVMKDLNWLEEGQKIKFGPLKKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDI 646
Cdd:cd17311 172 KYDLKGSLVSREAS-DKEKVKE----LPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  647 nkakeddlqladtasieeqpqtqgpirtgtgtvvrhffrefeggirasdqfnndvdlIYYVGIIDFLTNYSVMKKLETFW 726
Cdd:cd17311 247 ---------------------------------------------------------VYFMGLIDILTQYDAKKKAAHAA 269
                       330       340
                ....*....|....*....|....*....
gi 6320414  727 RSLRHDTKL-VSAIPPRDYANRFYEFIED 754
Cdd:cd17311 270 KTVKHGAGAeISTVHPEQYAKRFLDFITN 298
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
443-753 9.64e-35

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: 133.41  E-value: 9.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  443 YCPEVFRELRALFGLDPADYLVSLTSkyILSELNSPGKSGSFFYYSRDYKYIIKTIHHSEHIHLRKHIQEYYNHVRDNPN 522
Cdd:cd17300   8 YFAEQFHALRSLYCGGEDDFIRSLSR--CVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  523 ----TLICQFYGLHRVKMPISFQNKIKhrKIYFLVMNNLFPPHlDIHITYDLKGSTWGRFTNLDKERLAkdrsyrpVMKD 598
Cdd:cd17300  86 hkrpSLLAKILGVYRISVKNSTTNKTS--KQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDEDS-------VLLD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  599 LNWLEEgqkIKFGPL-----KKKTFLTQLKKDVELLAKLNTMDYSLLIGIHDINKakeddlQLadtasieeqpqtqgpir 673
Cdd:cd17300 156 ENFLEY---TKGSPLylrehSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKK------EL----------------- 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320414  674 tgtgtvvrhffrefeggirasdqfnndvdliyYVGIIDFLTNYSVMKKLETFWRSLrhdTKLVSA-----IPPRDYANRF 748
Cdd:cd17300 210 --------------------------------VVGIIDYIRTYTWDKKLESWVKSL---GILGGGgeptvISPELYKKRF 254

                ....*
gi 6320414  749 YEFIE 753
Cdd:cd17300 255 REAMD 259
 
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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