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Conserved domains on  [gi|1958805099|ref|XP_038940525|]
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1-phosphatidylinositol 3-phosphate 5-kinase isoform X12 [Rattus norvegicus]

Protein Classification

1-phosphatidylinositol-3-phosphate 5-kinase( domain architecture ID 13066872)

1-phosphatidylinositol-3-phosphate 5-kinase is part of a complex that 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
 1032-1298 1.63e-156

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: 470.07  E-value: 1.63e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1032 AKFYCRLYYAGEFHKMREVILGSsEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17300      1 TKFTCTIYFAEQFHALRSLYCGG-EDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTdtgKESCDVVLLDE 1191
Cdd:cd17300     80 MAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRNRYVNV---AEDEDSVLLDE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1192 NLLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGIL 1271
Cdd:cd17300    157 NFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGIL 236

                          250       260
                   ....*....|....*....|....*..
gi 1958805099 1272 GGQGkMPTVVSPELYRTRFCEAMDKYF 1298
Cdd:cd17300    237 GGGG-EPTVISPELYKKRFREAMDKYF 262
chaperonin_like super family cl02777
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 1-92 1.31e-41

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


The actual alignment was detected with superfamily member cd03334:

Pssm-ID: 351886 [Multi-domain]  Cd Length: 261  Bit Score: 153.92  E-value: 1.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099    1 MTQGDLVVSMDQLLTKPHLGTCHKFYMQLFQLPNEQTKTLMFFEGCAQHLGCTIKLRGGSDYELARVKEILIFMICVAYH 80
Cdd:cd03334    170 CTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYH 249

                           90
                   ....*....|..
gi 1958805099   81 SQLEISFLMDEF 92
Cdd:cd03334    250 LKLETSFLADEF 261
 
Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
 1032-1298 1.63e-156

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: 470.07  E-value: 1.63e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1032 AKFYCRLYYAGEFHKMREVILGSsEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17300      1 TKFTCTIYFAEQFHALRSLYCGG-EDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTdtgKESCDVVLLDE 1191
Cdd:cd17300     80 MAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRNRYVNV---AEDEDSVLLDE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1192 NLLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGIL 1271
Cdd:cd17300    157 NFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGIL 236

                          250       260
                   ....*....|....*....|....*..
gi 1958805099 1272 GGQGkMPTVVSPELYRTRFCEAMDKYF 1298
Cdd:cd17300    237 GGGG-EPTVISPELYKKRFREAMDKYF 262
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1005-1298 4.59e-105

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 336.28  E-value: 4.59e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1005 QDEVDGGDTQKKQLTNPHVELQFSDANAKFYCRLYYAGEFHKMREvILGSSEEDFIRSLSHSSP-WQARGGKSGAAFYAT 1083
Cdd:smart00330    1 LPSDFKATEKIKFPTPGHLELTPSHGSADFKFKDYCPEVFRNLRE-LFGIDPADYLRSLCRSPPlELSSGGKSGSFFYLS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1084 EDDRFILKQMPRLEVQSFLdfaPHYFNYITNAVQQKrPTALAKILGVYRIGYKNSqnnTEKKLDLLVMENLFY-GRKMAQ 1162
Cdd:smart00330   80 LDDRFIIKTVSKSEIKSLL---PMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGG---TEKKIYFLVMENLFYsDLKVHR 152

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1163 VFDLKGSLRNRNVktDTGKESCDVVLLDENLLKMvRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSN 1242
Cdd:smart00330  153 KYDLKGSTRGREA--DKKKVKELPVLKDLDLVEM-WNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIER 229

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1243 ------------------------------------------------------------ELVVGIIDYIRTFTWDKKLE 1262
Cdd:smart00330  230 gqreeielppvygsdespssessnggkapditgnllvsnspdgdgpfggiparairarrvVLYLGIIDILQTYTWDKKLE 309

                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 1958805099  1263 MVVKSTGILggqGKMPTVVSPELYRTRFCEAMDKYF 1298
Cdd:smart00330  310 HWVKSIGHD---GKTISVVHPEQYAKRFRDFMDKYF 342
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1016-1307 3.12e-66

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 236.38  E-value: 3.12e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1016 KQLTNPHVELQFSDANAKFYCRLYYAGEFHKMREviLGSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPR 1095
Cdd:COG5253    318 IKKTDTHLNEQFEEGLYEFSCKDYFPEVFRELRA--LCGCDEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISH 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1096 LEvqsFLDFAPHYFNYItNAVQQKRPTALAKILGVYRIGYKNS-QNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRN 1174
Cdd:COG5253    396 SE---HICFRPMIFEYY-VHVLFNPLTLLCKIFGFYRVKSRSSiSSSKSRKIYFIVMENLFYPHGIHRIFDLKGSMRNRH 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1175 VKtDTGKesCDVVLLDENLLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVG-IIDYIR 1253
Cdd:COG5253    472 VE-RTGK--SMSVLLDMNDVEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGlIIDFIR 548

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805099 1254 T-FTWDKKLEMVVKSTGILGG--QGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTG 1307
Cdd:COG5253    549 TrMTGDKKLESGIKDKLTVGSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQ 605
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 1074-1297 9.27e-50

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: 176.12  E-value: 9.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1074 GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIgyKNSQnnteKKLDLLVMEN 1153
Cdd:pfam01504   14 GKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEH----VKQNPNTLLPRFYGLHRV--KPGG----KKIYFVVMNN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1154 LFY-GRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKmvRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYS 1232
Cdd:pfam01504   84 LFPtDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFLE--RKLKLRLGPEKREALLKQLERDCEFLESLNIMDYS 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958805099 1233 LLVG---RDDTSNELV-VGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMDKY 1297
Cdd:pfam01504  162 LLLGihdLDEDGKEIYyLGIIDILTEYNLKKKLEHAWKS---LVHDGDSISAVPPKEYAERFLKFIEKI 227
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
 1-92 1.31e-41

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 153.92  E-value: 1.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099    1 MTQGDLVVSMDQLLTKPHLGTCHKFYMQLFQLPNEQTKTLMFFEGCAQHLGCTIKLRGGSDYELARVKEILIFMICVAYH 80
Cdd:cd03334    170 CTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYH 249

                           90
                   ....*....|..
gi 1958805099   81 SQLEISFLMDEF 92
Cdd:cd03334    250 LKLETSFLADEF 261
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1017-1236 3.58e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 93.74  E-value: 3.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1017 QLTNPHvelQFSDANAKFYCRLYyageFHKMREV--------ILGSSEEDFIRSLShsSPwqargGKSGAAFYATEDDRF 1088
Cdd:PLN03185   394 QLTPSH---QSEDFKWKDYCPMV----FRNLREMfkidaadyMMSICGNDALRELS--SP-----GKSGSVFFLSQDDRF 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1089 ILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIGYKNSQnntekKLDLLVMENLFYGR-KMAQVFDLK 1167
Cdd:PLN03185   460 MIKTLRKSEVKVLLRMLPDYHHH----VKTYENTLITKFFGLHRIKPSSGQ-----KFRFVVMGNMFCTElRIHRRFDLK 530

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805099 1168 GSLRNRnvktdtgkeSCDVVLLDEN--LLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVG 1236
Cdd:PLN03185   531 GSSLGR---------SADKVEIDENttLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLG 592
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-71 4.73e-05

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 47.58  E-value: 4.73e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805099    1 MTQGDLVVSMDQLlTKPHLGTCHKFYMQLFQlpneqTKTLMFFEGCAQHLGCTIKLRGGSDYELARVKEIL 71
Cdd:pfam00118  291 ATGARAVSSLDDL-TPDDLGTAGKVEEEKIG-----DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSI 355
 
Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
 1032-1298 1.63e-156

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: 470.07  E-value: 1.63e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1032 AKFYCRLYYAGEFHKMREVILGSsEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17300      1 TKFTCTIYFAEQFHALRSLYCGG-EDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTdtgKESCDVVLLDE 1191
Cdd:cd17300     80 MAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRNRYVNV---AEDEDSVLLDE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1192 NLLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGIL 1271
Cdd:cd17300    157 NFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGIL 236

                          250       260
                   ....*....|....*....|....*..
gi 1958805099 1272 GGQGkMPTVVSPELYRTRFCEAMDKYF 1298
Cdd:cd17300    237 GGGG-EPTVISPELYKKRFREAMDKYF 262
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1005-1298 4.59e-105

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 336.28  E-value: 4.59e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1005 QDEVDGGDTQKKQLTNPHVELQFSDANAKFYCRLYYAGEFHKMREvILGSSEEDFIRSLSHSSP-WQARGGKSGAAFYAT 1083
Cdd:smart00330    1 LPSDFKATEKIKFPTPGHLELTPSHGSADFKFKDYCPEVFRNLRE-LFGIDPADYLRSLCRSPPlELSSGGKSGSFFYLS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1084 EDDRFILKQMPRLEVQSFLdfaPHYFNYITNAVQQKrPTALAKILGVYRIGYKNSqnnTEKKLDLLVMENLFY-GRKMAQ 1162
Cdd:smart00330   80 LDDRFIIKTVSKSEIKSLL---PMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGG---TEKKIYFLVMENLFYsDLKVHR 152

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1163 VFDLKGSLRNRNVktDTGKESCDVVLLDENLLKMvRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSN 1242
Cdd:smart00330  153 KYDLKGSTRGREA--DKKKVKELPVLKDLDLVEM-WNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIER 229

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  1243 ------------------------------------------------------------ELVVGIIDYIRTFTWDKKLE 1262
Cdd:smart00330  230 gqreeielppvygsdespssessnggkapditgnllvsnspdgdgpfggiparairarrvVLYLGIIDILQTYTWDKKLE 309

                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 1958805099  1263 MVVKSTGILggqGKMPTVVSPELYRTRFCEAMDKYF 1298
Cdd:smart00330  310 HWVKSIGHD---GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 1033-1296 1.19e-69

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: 234.00  E-value: 1.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1033 KFYCRLYYAGEFHKMREvILGSSEEDFIRSLSHSSPW---QARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYF 1109
Cdd:cd00139      2 KFKFKDYAPEVFRKLRE-LFGISEEDYLESLSPEENLrelKESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1110 NYItnavQQKRPTALAKILGVYRIGYKNSqnnteKKLDLLVMENLFY-GRKMAQVFDLKGSLRNRNVKTDTGKESCDVVL 1188
Cdd:cd00139     81 EHI----KKNPNSLLTRFYGLYSIKLQKG-----KKVYFVVMENVFPtDLKIHERYDLKGSTVGRRVSKEKEKKKGLKVL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1189 LDENLLKMVRDnpLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDtsNELVVGIIDYIRTFTWDKKLEMVVKSt 1268
Cdd:cd00139    152 KDLDFLEKGEK--IILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHR--LVYYLGIIDILQEYNLRKKLERFLKS- 226

                          250       260
                   ....*....|....*....|....*...
gi 1958805099 1269 gILGGQGKMPTVVSPELYRTRFCEAMDK 1296
Cdd:cd00139    227 -LLYGKDSGISCVPPDEYAERFLKFMES 253
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1016-1307 3.12e-66

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 236.38  E-value: 3.12e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1016 KQLTNPHVELQFSDANAKFYCRLYYAGEFHKMREviLGSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPR 1095
Cdd:COG5253    318 IKKTDTHLNEQFEEGLYEFSCKDYFPEVFRELRA--LCGCDEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISH 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1096 LEvqsFLDFAPHYFNYItNAVQQKRPTALAKILGVYRIGYKNS-QNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRN 1174
Cdd:COG5253    396 SE---HICFRPMIFEYY-VHVLFNPLTLLCKIFGFYRVKSRSSiSSSKSRKIYFIVMENLFYPHGIHRIFDLKGSMRNRH 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1175 VKtDTGKesCDVVLLDENLLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVG-IIDYIR 1253
Cdd:COG5253    472 VE-RTGK--SMSVLLDMNDVEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGlIIDFIR 548

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805099 1254 T-FTWDKKLEMVVKSTGILGG--QGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTG 1307
Cdd:COG5253    549 TrMTGDKKLESGIKDKLTVGSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQ 605
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 1074-1297 9.27e-50

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: 176.12  E-value: 9.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1074 GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIgyKNSQnnteKKLDLLVMEN 1153
Cdd:pfam01504   14 GKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEH----VKQNPNTLLPRFYGLHRV--KPGG----KKIYFVVMNN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1154 LFY-GRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKmvRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYS 1232
Cdd:pfam01504   84 LFPtDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFLE--RKLKLRLGPEKREALLKQLERDCEFLESLNIMDYS 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958805099 1233 LLVG---RDDTSNELV-VGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMDKY 1297
Cdd:pfam01504  162 LLLGihdLDEDGKEIYyLGIIDILTEYNLKKKLEHAWKS---LVHDGDSISAVPPKEYAERFLKFIEKI 227
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
 1-92 1.31e-41

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 153.92  E-value: 1.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099    1 MTQGDLVVSMDQLLTKPHLGTCHKFYMQLFQLPNEQTKTLMFFEGCAQHLGCTIKLRGGSDYELARVKEILIFMICVAYH 80
Cdd:cd03334    170 CTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYH 249

                           90
                   ....*....|..
gi 1958805099   81 SQLEISFLMDEF 92
Cdd:cd03334    250 LKLETSFLADEF 261
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
 987-1296 1.30e-28

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: 117.78  E-value: 1.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099  987 YQVGQTGKEgmESQGLEPQDevdgGDTQKKQLTN---------PHvelQFSDANAKFYCRLYyageFHKMREViLGSSEE 1057
Cdd:cd17302     14 YSVGKIAPV--ARRDLKPSD----FDPKAKQWFPfpgsgstppPH---QSSDFKWKDYCPMV----FRNLREL-FGIDAA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1058 DFIRSLSH-------SSPwqargGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGV 1130
Cdd:cd17302     80 DYMLSLCGddalrelSSP-----GKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH----VKAYENTLLTKFFGV 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1131 YRIGYKNSqnnteKKLDLLVMENLFYGR-KMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENL-LKMVRDnplyiRSHS 1208
Cdd:cd17302    151 HRVKPVGG-----RKVRFVVMGNLFCTElRIHRRFDLKGSTHGRTTGKPESEIDPNTTLKDLDLdFKFRLE-----KGWR 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1209 KSVLRTsIHSDAHFLSSHLIIDYSLLVG-------RDDTSNELVV--GIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPT 1279
Cdd:cd17302    221 DALMRQ-IDADCAFLEALRIMDYSLLLGvhfragdSTGEPYDVVLyfGIIDILQEYNISKKLEHAYKS---LQYDPASIS 296

                          330
                   ....*....|....*..
gi 1958805099 1280 VVSPELYRTRFCEAMDK 1296
Cdd:cd17302    297 AVDPKLYSRRFRDFIRK 313
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1039-1295 3.03e-28

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: 117.07  E-value: 3.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1039 YYAGE-FHKMREvILGSSEEDFIRSLSHSSPWQA--RGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYItna 1115
Cdd:cd17304     53 TYAGPvFATLRQ-SLGISEKEYQNSLSPDEPYLQfiSNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL--- 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1116 vqQKRP-TALAKILGVYRIGYKNsqnntEKKLDLLVMENLFY-GRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENL 1193
Cdd:cd17304    129 --ENYPhSLLVKFLGVHSIKLPG-----KKKKYFIVMQSVFYpDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNF 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1194 LkmvrDNPLYIRsHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRD------------DTSNEL----------VVGIIDY 1251
Cdd:cd17304    202 E----GNSINLG-QQRSWFLRQVEIDTEFLKGLNVLDYSLLVGFQplhsdenrrllpNYKNALhvvdgpeyryFVGIIDI 276

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958805099 1252 IRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMD 1295
Cdd:cd17304    277 FTVYGLRKRLEHLWKS---LRYPGQSFSTVSPEKYARRFCQWVE 317
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
 1033-1296 2.90e-24

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: 104.66  E-value: 2.90e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1033 KFYCRLYyageFHKMREViLGSSEEDFIRSLSHSSP-WQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17305     56 KEYCPLV----FRNLRER-FGIDDDDYLNSLTRSQPlASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQY 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ItnaVQQKRPTALAKILGVYRIgyknSQNNTEKKLdlLVMENLFYGR-KMAQVFDLKGSLRNRnVKTDTGKESCDVVLLD 1190
Cdd:cd17305    131 I---VERHGKTLLPQYLGMYRI----TVNGVETYL--VVMRNVFSPRlPIHKKYDLKGSTVDR-QASDKEKAKDLPTLKD 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1191 ENLLKMVRDnpLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDtsnelVV---GIIDYIRTFTWDKKLEMVVKS 1267
Cdd:cd17305    201 NDFLNDGTK--IYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHD-----CIyfmAIIDILTHYGAKKRAAHAAKT 273

                          250       260
                   ....*....|....*....|....*....
gi 1958805099 1268 tgILGGQGKMPTVVSPELYRTRFCEAMDK 1296
Cdd:cd17305    274 --VKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
 1040-1296 3.64e-24

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: 105.07  E-value: 3.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1040 YAGE-FHKMREvILGSSEEDFIRSLSH-------SSPwqargGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17303     59 YAPWvFRFLRE-LFGIDPADYLMSLTGkyilselGSP-----GKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNH 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ITNAVQqkrpTALAKILGVYRIgyknsQNNTEKKLDLLVMENLF-YGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLD 1190
Cdd:cd17303    133 VKENPN----TLLSQFYGLHRV-----KMPRGRKIHFVVMNNLFpPHRDIHQTFDLKGSTVGRETPEDKLAKGPRATLKD 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1191 ENLLKmvRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVG-------------RDDTSNEL-VVGIIDYIRTFT 1256
Cdd:cd17303    204 LNWLR--RKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGihdldggfqatdeNNEPGDEIyYLGIIDILTPYN 281

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958805099 1257 WDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMDK 1296
Cdd:cd17303    282 AKKKLEHFFKS---LRHDRHTISAVPPKEYARRFLKFIED 318
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
 1044-1294 1.52e-22

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: 100.01  E-value: 1.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1044 FHKMREvILGSSEEDFIRSLSHSsPWQ--ARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFnyiTNAVQQKRp 1121
Cdd:cd17301     65 FRYFRE-LFGIKPDDYLLSLCNE-PLRelSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYY---MNLNQNPR- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1122 TALAKILGVYriGYKNSQnnteKKLDLLVMENLF-YGRKMAQVFDLKGS-LRNRNVKTDTGKESCDVVLLDENllkmvRD 1199
Cdd:cd17301    139 TLLPKFYGLY--CYQSGG----KNIRFVVMNNLLpSNIKMHEKYDLKGStYKRKASKKERQKKSPTLKDLDFM-----ED 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1200 NP--LYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVG---------RDDTSNELV--VGIIDYIRTFTWDKKLEMVVK 1266
Cdd:cd17301    208 HPegILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGvhnlggipaRNSKGERLLlfIGIIDILQSYRLKKKLEHTWK 287

                          250       260
                   ....*....|....*....|....*...
gi 1958805099 1267 StgILGGqGKMPTVVSPELYRTRFCEAM 1294
Cdd:cd17301    288 S--VVHD-GDTVSVHRPSFYAERFQNFM 312
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1017-1236 3.58e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 93.74  E-value: 3.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1017 QLTNPHvelQFSDANAKFYCRLYyageFHKMREV--------ILGSSEEDFIRSLShsSPwqargGKSGAAFYATEDDRF 1088
Cdd:PLN03185   394 QLTPSH---QSEDFKWKDYCPMV----FRNLREMfkidaadyMMSICGNDALRELS--SP-----GKSGSVFFLSQDDRF 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1089 ILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIGYKNSQnntekKLDLLVMENLFYGR-KMAQVFDLK 1167
Cdd:PLN03185   460 MIKTLRKSEVKVLLRMLPDYHHH----VKTYENTLITKFFGLHRIKPSSGQ-----KFRFVVMGNMFCTElRIHRRFDLK 530

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805099 1168 GSLRNRnvktdtgkeSCDVVLLDEN--LLKMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVG 1236
Cdd:PLN03185   531 GSSLGR---------SADKVEIDENttLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLG 592
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1033-1294 3.30e-18

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: 87.03  E-value: 3.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1033 KFYCRLYyageFHKMREViLGSSEEDFIRSLSHSSPWQARG-GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17310     67 KEYCPMV----FRNLRER-FGIDDQDYQNSVTRSAPINSDSqGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQF 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ItnaVQQKRPTALAKILGVYRIGYKNSQNNtekkldLLVMENLFYGR-KMAQVFDLKGSLRNRNVktdTGKESC-DVVLL 1189
Cdd:cd17310    142 I---VECHGNTLLPQFLGMYRLTVDGVETY------MVVTRNVFSHRlTVHRKYDLKGSTVSREA---SDKEKAkDLPTF 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1190 DENLLkMVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSneLVVGIIDYIRTFTWDKKLEMVVKStg 1269
Cdd:cd17310    210 KDNDF-LNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVV--YFMAIIDILTPYDAKKKAAHAAKT-- 284

                          250       260
                   ....*....|....*....|....*
gi 1958805099 1270 ILGGQGKMPTVVSPELYRTRFCEAM 1294
Cdd:cd17310    285 VKHGAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1033-1290 1.45e-17

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: 85.03  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1033 KFYCRLYyageFHKMREViLGSSEEDFIRSLSHSSPWQARG-GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1111
Cdd:cd17309     65 KEYCPMV----FRNLRER-FGIDDQDFQNSLTRSAPLANDSqARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQY 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1112 ItnaVQQKRPTALAKILGVYRIGYKNSQnntekkLDLLVMENLFYGR-KMAQVFDLKGSLRNRNVkTDTGKESCDVVLLD 1190
Cdd:cd17309    140 I---VECHGNTLLPQFLGMYRLTVDGVE------TYMIVTRNVFSHRlSVYRKYDLKGSTVAREA-SDKEKAKELPTLKD 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1191 ENLLKmvRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSneLVVGIIDYIRTFTWDKKLEMVVKStgI 1270
Cdd:cd17309    210 NDFIN--DGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDVV--YFMAIIDILTHYDAKKKAAHAAKT--V 283

                          250       260
                   ....*....|....*....|
gi 1958805099 1271 LGGQGKMPTVVSPELYRTRF 1290
Cdd:cd17309    284 KHGAGAEISTVNPEQYSKRF 303
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1044-1292 2.97e-17

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: 84.15  E-value: 2.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1044 FHKMREViLGSSEEDFIRSLSHSSPwQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYItnaVQQKRPTA 1123
Cdd:cd17311     63 FRNLRER-FGIDDQDYQVSLTRSPP-YSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYI---VKCHGNTL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1124 LAKILGVYRIGYKNSQNNtekkldLLVMENLFYGR-KMAQVFDLKGSLRNRNVkTDTGKESCDVVLLDENLLKmvRDNPL 1202
Cdd:cd17311    138 LPQFLGMYRLSVDNEDSY------MLVMRNMFSHRlPVHRKYDLKGSLVSREA-SDKEKVKELPTLKDMDFLN--KNQKV 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1203 YIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSneLVVGIIDYIRTFTWDKKLEMVVKStgILGGQGKMPTVVS 1282
Cdd:cd17311    209 YVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDVV--YFMGLIDILTQYDAKKKAAHAAKT--VKHGAGAEISTVH 284

                          250
                   ....*....|
gi 1958805099 1283 PELYRTRFCE 1292
Cdd:cd17311    285 PEQYAKRFLD 294
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1013-1295 3.04e-17

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: 84.27  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1013 TQKKQLTNPHvelQFSDANAKFYCRLyyagEFHKMREvILGSSEEDFIRSLSH------SSPwqargGKSGAAFYATEDD 1086
Cdd:cd17307     41 SEGSNLTPAH---HYPDFRFKTYAPL----AFRYFRE-LFGIKPDDYLYSICSeplielSNP-----GASGSLFYVTSDD 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1087 RFILKQMPRLEVQSFLDFAPHYFnyiTNAVQQKRpTALAKILGVYRIGYKNSQnntekkLDLLVMENLF-YGRKMAQVFD 1165
Cdd:cd17307    108 EFIIKTVQHKEAEFLQKLLPGYY---MNLNQNPR-TLLPKFYGLYCMQSGGIN------IRIVVMNNVLpRSVKMHYKYD 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1166 LKGSLRNRNVKTDTGKESCDvVLLDENLLKMVRDNpLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVG--------- 1236
Cdd:cd17307    178 LKGSTYKRRASRKEREKSCP-TYKDLDFLQDMHDG-LYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGihvlggipa 255

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805099 1237 --RDDTSNELVVGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMD 1295
Cdd:cd17307    256 knHKGEKLLLFMGIIDILQSYRLMKKLEHSWKA---LVYDGDTVSVHRPSFYADRFLKFMN 313
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 2-84 8.59e-16

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 77.51  E-value: 8.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099    2 TQGDLVVSMDQLlTKPHLGTCHKFYMQlfqlpNEQTKTLMFFEGCAQHLGCTIKLRGGSDYELARVKEILIFMICVAYHS 81
Cdd:cd03333    133 TGATIVSSLEDL-TPEDLGTAELVEET-----KIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALCAVRAA 206


                   ...
gi 1958805099   82 QLE 84
Cdd:cd03333    207 VEE 209
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1013-1294 9.82e-16

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: 80.04  E-value: 9.82e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1013 TQKKQLTNPHvelQFSDanakFYCRLYYAGEFHKMREvILGSSEEDFIRSLSHSSPWQ-ARGGKSGAAFYATEDDRFILK 1091
Cdd:cd17308     42 SEGSNLTPAH---HYPD----FRFKTYAPVAFRYFRE-LFGIRPDDYLYSLCNEPLIElSNPGASGSLFYVTSDDEFIIK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1092 QMPRLEVQSFLDFAPHYFnyiTNAVQQKRpTALAKILGVYRIgyknsqNNTEKKLDLLVMENLF-YGRKMAQVFDLKGSL 1170
Cdd:cd17308    114 TVMHKEAEFLQKLLPGYY---MNLNQNPR-TLLPKFYGLYCV------QSGGKNIRVVVMNNILpRVVKMHLKFDLKGST 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1171 RNRNVKTDTGKESC----DVVLLDENLLKMVRDNPLYirshskSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSN---- 1242
Cdd:cd17308    184 YKRRASKKEREKSKptfkDLDFMQDMPEGLMLDADTF------SALVKTLQRDCLVLESFKIMDYSLLLGVHNIGGipav 257

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958805099 1243 -------ELVVGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAM 1294
Cdd:cd17308    258 ngkgerlLLYIGIIDILQSYRLIKKLEHTWKA---LVHDGDTVSVHRPSFYAERFFKFM 313
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1034-1294 1.38e-12

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: 70.80  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1034 FYCRLYYAGEFHKMREvILGSSEEDFIRSLSHSSPWQ-ARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFnyi 1112
Cdd:cd17306     58 FRFKTYAPVAFRYFRE-LFGIRPDDYLYSLCSEPLIElSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYY--- 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1113 TNAVQQKRpTALAKILGVY--RIGYKNsqnntekkLDLLVMENLF-YGRKMAQVFDLKGSLRNRNVKTDTgKESCDVVLL 1189
Cdd:cd17306    134 MNLNQNPR-TLLPKFYGLYcvQAGGKN--------IRIVVMNNLLpRSVKMHLKYDLKGSTYKRRASQKE-REKPLPTYK 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1190 DENLLKMVRDNpLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVG-----------------------RDDTSNELV- 1245
Cdd:cd17306    204 DLDFLQDIPDG-LFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGihnidarrggtietddqmggipaRNSKGERLLl 282

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958805099 1246 -VGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAM 1294
Cdd:cd17306    283 yIGIIDILQSYRFVKKLEHSWKA---LVHDGDTVSVHRPGFYAERFQRFM 329
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-71 4.73e-05

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 47.58  E-value: 4.73e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805099    1 MTQGDLVVSMDQLlTKPHLGTCHKFYMQLFQlpneqTKTLMFFEGCAQHLGCTIKLRGGSDYELARVKEIL 71
Cdd:pfam00118  291 ATGARAVSSLDDL-TPDDLGTAGKVEEEKIG-----DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSI 355
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 14-61 8.50e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239456 [Multi-domain]  Cd Length: 522  Bit Score: 40.35  E-value: 8.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958805099   14 LTKPHLGTCHKFYMQlfQLPNEQTKtlmFFEGCAQHLGCTIKLRGGSD 61
Cdd:cd03340    333 ITDDVLGTCGLFEER--QVGGERYN---IFTGCPKAKTCTIILRGGAE 375
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 7-68 9.56e-03

chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 238189  Cd Length: 464  Bit Score: 40.10  E-value: 9.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958805099    7 VVSMDQLLTKPHLGTCHKFYmqlfqlpneQTKT----LMFFEGCAQHLGCTIKLRGGSDYELARVK 68
Cdd:cd00309    273 IVSRLEDLTPEDLGTAGLVE---------ETKIgdekYTFIEGCKGGKVATILLRGATEVELDEAE 329
 
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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