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Conserved domains on  [gi|767996101|ref|XP_011523629|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 beta isoform X2 [Homo sapiens]

Protein Classification

phosphatidylinositol phosphate kinase family protein( domain architecture ID 1000257)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc super family cl28923
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
1-376 0e+00

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family includes phosphatidylinositol 5-phosphate 4-kinases (PIP5Ks) and similar proteins. PIP5Ks catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. The family includes type I and II PIP5Ks (-alpha, -beta, and -gamma) kinases. Signalling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling.


The actual alignment was detected with superfamily member cd17310:

Pssm-ID: 475131  Cd Length: 311  Bit Score: 570.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   1 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 80
Cdd:cd17310   36 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETY 160
Cdd:cd17310  116 RRFVIKTVSSEDVAEMHNILKKYHQ---------------------------FIVECHGNTLLPQFLGMYRLTVDGVETY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 161 MVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 240
Cdd:cd17310  169 MVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 241 DYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshess 320
Cdd:cd17310  249 DYSLLVGIHDV--------------------------------------------------------------------- 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996101 321 pkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17310  260 ----VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1-376 0e+00

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: 570.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   1 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 80
Cdd:cd17310   36 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETY 160
Cdd:cd17310  116 RRFVIKTVSSEDVAEMHNILKKYHQ---------------------------FIVECHGNTLLPQFLGMYRLTVDGVETY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 161 MVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 240
Cdd:cd17310  169 MVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 241 DYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshess 320
Cdd:cd17310  249 DYSLLVGIHDV--------------------------------------------------------------------- 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996101 321 pkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17310  260 ----VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
3-378 1.18e-119

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 350.14  E-value: 1.18e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101     3 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 78
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101    79 YDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHgNTLLPQFLGMYRLTVDG-- 156
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYE---------------------------HIVQNP-NTLLPKFFGLYRVKVKGgt 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   157 -VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFL 234
Cdd:smart00330 132 eKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   235 AQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAM 314
Cdd:smart00330 211 ESLKIMDYSLLVGIHDIERGQREEIELPPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAI 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996101   315 KSHEsspkkEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 378
Cdd:smart00330 285 RARR-----VVLYLGIIDILQTYTWDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
67-377 4.80e-73

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: 226.96  E-value: 4.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   67 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVEcHGNTLLPQF 146
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYE---------------------------HVKQ-NPNTLLPRF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  147 LGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLE 225
Cdd:pfam01504  64 YGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  226 KLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgef 305
Cdd:pfam01504 144 QLERDCEFLESLNIMDYSLLLGIHDLD----------------------------------------------------- 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996101  306 dpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 377
Cdd:pfam01504 171 --------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
29-377 1.58e-36

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 140.74  E-value: 1.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  29 FKFKEYCPMVFRNLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMa 107
Cdd:PLN03185 404 FKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH- 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 108 gslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVA 186
Cdd:PLN03185 483 ---------------------------VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLG 535
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 187 REAsDKEKAKDLPTFKDNDfLNegQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAE 266
Cdd:PLN03185 536 RSA-DKVEIDENTTLKDLD-LN--YSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPY 607
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 267 DEECENDGVG-----------------GNLLCSYGTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYA 313
Cdd:PLN03185 608 SRSITADGLEvvaeedtiedeelsypeGLVLVPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNM 687
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996101 314 MKSHESSPKKE-------------VYFMAIIDILTPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 377
Cdd:PLN03185 688 PARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
14-250 7.40e-33

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 129.68  E-value: 7.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  14 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSs 90
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTIS- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  91 edvaemHNILKKYHQMagslaclcilslpcgipISGWQKRCKFivecHGNTLLPQFLGMYRL-------TVDGVETYMVV 163
Cdd:COG5253  395 ------HSEHICFRPM-----------------IFEYYVHVLF----NPLTLLCKIFGFYRVksrssisSSKSRKIYFIV 447
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 164 TRNVFSHRLtVHRKYDLKGSTVAREASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDY 242
Cdd:COG5253  448 MENLFYPHG-IHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDY 525

                 ....*...
gi 767996101 243 SLLVGIHD 250
Cdd:COG5253  526 SLLVGIDD 533
 
Name Accession Description Interval E-value
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1-376 0e+00

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: 570.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   1 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 80
Cdd:cd17310   36 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETY 160
Cdd:cd17310  116 RRFVIKTVSSEDVAEMHNILKKYHQ---------------------------FIVECHGNTLLPQFLGMYRLTVDGVETY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 161 MVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 240
Cdd:cd17310  169 MVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 241 DYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshess 320
Cdd:cd17310  249 DYSLLVGIHDV--------------------------------------------------------------------- 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996101 321 pkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17310  260 ----VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
1-376 0e+00

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II phosphatidylinositol 5-phosphate 4-kinase (PIP5KII) and similar proteins; PIP5KIIs, also known as PIPKIIs, or PI4P5KIIs, are responsible for the synthesis of phosphatidylinositol-4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes, from phosphatidylinositol-5-phosphate (PtdIns5P). Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K2A, PIP5K2B, and PIP5K2C isoforms.


Pssm-ID: 340442  Cd Length: 300  Bit Score: 519.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   1 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 80
Cdd:cd17305   25 MLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNSLTRSQPLASDSPGRSGSRFLVSYD 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETY 160
Cdd:cd17305  105 KKYVIKTISSEEVAQMHHILKQYHQ---------------------------YIVERHGKTLLPQYLGMYRITVNGVETY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 161 MVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 240
Cdd:cd17305  158 LVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 241 DYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshess 320
Cdd:cd17305  238 DYSLLVGIHDC--------------------------------------------------------------------- 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996101 321 pkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17305  249 ----IYFMAIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1-376 1.14e-174

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: 488.33  E-value: 1.14e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   1 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYD 80
Cdd:cd17309   34 MLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETY 160
Cdd:cd17309  114 KRYIIKTITSEDVAEMHNILKKYHQ---------------------------YIVECHGNTLLPQFLGMYRLTVDGVETY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 161 MVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 240
Cdd:cd17309  167 MIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLM 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 241 DYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshess 320
Cdd:cd17309  247 DYSLLVGIHDV--------------------------------------------------------------------- 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996101 321 pkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17309  258 ----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1-376 1.73e-147

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: 419.27  E-value: 1.73e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   1 MLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGrcGTRFLTTYD 80
Cdd:cd17311   25 MLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSPPYSESEGS--DGRFLLSYD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHGNTLLPQFLGMYRLTVDGVETY 160
Cdd:cd17311  103 RTLVIKEISSEDVADMHSILSHYHQ---------------------------YIVKCHGNTLLPQFLGMYRLSVDNEDSY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 161 MVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIM 240
Cdd:cd17311  156 MLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIM 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 241 DYSLLVGIHDVdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshess 320
Cdd:cd17311  236 DYSLLLGIHDV--------------------------------------------------------------------- 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767996101 321 pkkeVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17311  247 ----VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
3-378 1.18e-119

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 350.14  E-value: 1.18e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101     3 MPDDFKAYSKIKVDNHLfNKENLPS----RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTT 78
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPShgsaDFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101    79 YDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVECHgNTLLPQFLGMYRLTVDG-- 156
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYE---------------------------HIVQNP-NTLLPKFFGLYRVKVKGgt 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   157 -VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAsDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFL 234
Cdd:smart00330 132 eKKIYFLVMENLFYSDLKVHRKYDLKGSTRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   235 AQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGgnllcSYGTPPDSPGNLLSFPRFFGPGEFDpSVDVYAM 314
Cdd:smart00330 211 ESLKIMDYSLLVGIHDIERGQREEIELPPVYGSDESPSSESS-----NGGKAPDITGNLLVSNSPDGDGPFG-GIPARAI 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767996101   315 KSHEsspkkEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 378
Cdd:smart00330 285 RARR-----VVLYLGIIDILQTYTWDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
28-376 2.66e-83

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: 254.03  E-value: 2.66e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  28 RFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSD--SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQ 105
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 106 magslaclcilslpcgipisgwqkrckFIVEcHGNTLLPQFLGMYRLTV-DGVETYMVVTRNVFSHRLTVHRKYDLKGST 184
Cdd:cd00139   82 ---------------------------HIKK-NPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGST 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 185 VAREAS-DKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVdraeqeemevee 263
Cdd:cd00139  134 VGRRVSkEKEKKKGLKVLKDLDFLEKGEKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL------------ 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 264 raedeecendgvggnllcsygtppdspgnllsfprffgpgefdpsvdvyamkshesspkkeVYFMAIIDILTPYDTKKKA 343
Cdd:cd00139  202 -------------------------------------------------------------VYYLGIIDILQEYNLRKKL 220
                        330       340       350
                 ....*....|....*....|....*....|...
gi 767996101 344 AHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd00139  221 ERFLKSLLYGKDSGISCVPPDEYAERFLKFMES 253
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
67-377 4.80e-73

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: 226.96  E-value: 4.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   67 SQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQmagslaclcilslpcgipisgwqkrckFIVEcHGNTLLPQF 146
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYE---------------------------HVKQ-NPNTLLPRF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  147 LGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPT-FKDNDFLNEGQKLHVGEESKKNFLE 225
Cdd:pfam01504  64 YGLHRVKPGGKKIYFVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  226 KLKRDVEFLAQLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfprffgpgef 305
Cdd:pfam01504 144 QLERDCEFLESLNIMDYSLLLGIHDLD----------------------------------------------------- 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996101  306 dpsvdvyamkshesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSNI 377
Cdd:pfam01504 171 --------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
2-376 2.25e-68

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: 217.93  E-value: 2.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   2 LMPDDFKAYSKIKVDnHLFNKENLPSR--FKFKEYCPMVFRNLRERFGIDDQDYQNSVTrSAPINS--DSQGRCGTRFLT 77
Cdd:cd17303   26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLT-GKYILSelGSPGKSGSFFYF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  78 TYDRRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLTV-DG 156
Cdd:cd17303  104 SRDYRFIIKTIHHSEHKFLRKILPDYYNH----------------------------VKENPNTLLSQFYGLHRVKMpRG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 157 VETYMVVTRNVFSHRLTVHRKYDLKGSTVAREAS-DKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLA 235
Cdd:cd17303  156 RKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 236 QLKIMDYSLLVGIHDVDraeqeemeveeraedeecendgvGGnllcsygtppdspgnllsfprFFGPGEFDpsvdvyamk 315
Cdd:cd17303  236 SLNIMDYSLLVGIHDLD-----------------------GG---------------------FQATDENN--------- 262
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767996101 316 shesSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17303  263 ----EPGDEIYYLGIIDILTPYNAKKKLEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
29-377 2.81e-51

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) and similar proteins; PIP5K (EC 2.7.1.68), also known as PtdIns(4)P-5-kinase, or diphosphoinositide kinase, phosphorylates phosphatidylinositol-4-phosphate to produce phosphatidylinositol-4,5-bisphosphate as a precursor of two second messengers, inositol-1,4,5-triphosphate and diacylglycerol, and as a regulator of many cellular proteins involved in signal transduction and cytoskeletal organization. The family includes several PIP5Ks from Arabidopsis thaliana. AtPIP5K1 is involved in water-stress signal transduction. AtPIP5K2 acts as an interactor of all five Arabidopsis RAB-E proteins but not with other Rab subclasses residing at the Golgi or trans-Golgi network. AtPIP5K3 is a key regulator of root hair tip growth. AtPIP5K4 and AtPIP5K5 are type B PI4P 5-kinases expressed in pollen and have important functions in pollen germination and in pollen tube growth. AtPIP5K6 regulates clathrin-dependent endocytosis in pollen tubes. AtPIP5K9 interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth.


Pssm-ID: 340439  Cd Length: 314  Bit Score: 173.63  E-value: 2.81e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  29 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMa 107
Cdd:cd17302   57 FKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 108 gslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLT-VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVA 186
Cdd:cd17302  136 ---------------------------VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 187 REASDKEKAKDLPT-FKDNDFlneGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveera 265
Cdd:cd17302  189 RTTGKPESEIDPNTtLKDLDL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH---------------- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 266 edeecendgvggnllcsygtppdspgnllsfprFFGPGEFDPSVDVyamkshesspkkeVYFMAIIDILTPYDTKKKAAH 345
Cdd:cd17302  250 ---------------------------------FRAGDSTGEPYDV-------------VLYFGIIDILQEYNISKKLEH 283
                        330       340       350
                 ....*....|....*....|....*....|..
gi 767996101 346 AAKTVKHGAGAeISTVNPEQYSKRFNEFMSNI 377
Cdd:cd17302  284 AYKSLQYDPAS-ISAVDPKLYSRRFRDFIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
27-376 2.86e-48

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: 165.88  E-value: 2.86e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  27 SRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKY--- 103
Cdd:cd17301   53 SDFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYymn 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 104 -HQmagslaclcilslpcgipisgwqkrckfivecHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKG 182
Cdd:cd17301  133 lNQ--------------------------------NPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 183 STVAREASDKEKAKDLPTFKDNDFLN---EGQKLhvgEESKKNFLEK-LKRDVEFLAQLKIMDYSLLVGIHDvdraeqee 258
Cdd:cd17301  181 STYKRKASKKERQKKSPTLKDLDFMEdhpEGILL---EPDTYDALLKtIQRDCRVLESFKIMDYSLLLGVHN-------- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 259 meveeraedeecendgVGGnllcsygtppdspgnllsfprffgpgefdpsvdvyaMKSHESSPKKEVYFMAIIDILTPYD 338
Cdd:cd17301  250 ----------------LGG------------------------------------IPARNSKGERLLLFIGIIDILQSYR 277
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 767996101 339 TKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17301  278 LKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMAN 314
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
29-249 1.18e-40

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: 145.90  E-value: 1.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  29 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMAG 108
Cdd:cd17307   55 FRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 109 SlaclcilslpcgipisgwqkrckfivecHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVARE 188
Cdd:cd17307  135 Q----------------------------NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRR 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996101 189 ASDKEKAKDLPTFKDNDFLNEGQK-LHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIH 249
Cdd:cd17307  187 ASRKEREKSCPTYKDLDFLQDMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
29-378 1.55e-37

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1gamma) and similar proteins; PIP5K1gamma(EC 2.7.1.68), also known as PtdIns(4)P-5-kinase 1 gamma, or PIP5K1gamma, or PIPKIgamma, or PtdInsPKI gamma, is a phosphatidylinositol-4-phosphate 5-kinase that catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), which is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. PIP5K1gamma is required for epidermal growth factor (EGF)-stimulated directional cell migration. It also modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin.


Pssm-ID: 340445  Cd Length: 323  Bit Score: 137.82  E-value: 1.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  29 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMAG 108
Cdd:cd17308   56 FRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 109 SlaclcilslpcgipisgwqkrckfivecHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVARE 188
Cdd:cd17308  136 Q----------------------------NPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRR 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 189 ASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvdraeqeemeveeraed 267
Cdd:cd17308  188 ASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVH------------------ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 268 eecendgvggnllcsygtppdspgNLLSFPRFFGPGEfdpsvdvyamkshesspkKEVYFMAIIDILTPYDTKKKAAHAA 347
Cdd:cd17308  250 ------------------------NIGGIPAVNGKGE------------------RLLLYIGIIDILQSYRLIKKLEHTW 287
                        330       340       350
                 ....*....|....*....|....*....|.
gi 767996101 348 KTVKHGaGAEISTVNPEQYSKRFNEFMSNIL 378
Cdd:cd17308  288 KALVHD-GDTVSVHRPSFYAERFFKFMSNTV 317
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
29-377 1.58e-36

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 140.74  E-value: 1.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  29 FKFKEYCPMVFRNLRERFGIDDQDYQNSVT-RSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQMa 107
Cdd:PLN03185 404 FKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH- 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 108 gslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLTVDGVETY-MVVTRNVFSHRLTVHRKYDLKGSTVA 186
Cdd:PLN03185 483 ---------------------------VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLKGSSLG 535
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 187 REAsDKEKAKDLPTFKDNDfLNegQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHdvDRAeqEEMEVEERAE 266
Cdd:PLN03185 536 RSA-DKVEIDENTTLKDLD-LN--YSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRA--PQHLRSLLPY 607
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 267 DEECENDGVG-----------------GNLLCSYGTPPDS--PGNLLSFPRFFGPGEFDPSVD--------------VYA 313
Cdd:PLN03185 608 SRSITADGLEvvaeedtiedeelsypeGLVLVPRGADDGStvPGPHIRGSRLRASAAGDEEVDlllpgtarlqiqlgVNM 687
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996101 314 MKSHESSPKKE-------------VYFMAIIDILTPYDTKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFMSNI 377
Cdd:PLN03185 688 PARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-252 8.23e-36

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: 133.58  E-value: 8.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  27 SRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQM 106
Cdd:cd17306   56 NDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 107 agslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVA 186
Cdd:cd17306  136 ----------------------------LNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYK 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996101 187 REASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVD 252
Cdd:cd17306  188 RRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNID 254
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
14-250 7.40e-33

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 129.68  E-value: 7.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  14 KVDNHLfnKENLPS---RFKFKEYCPMVFRNLRERFGIDDQDYqnSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSs 90
Cdd:COG5253  320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCDEALV--SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTIS- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  91 edvaemHNILKKYHQMagslaclcilslpcgipISGWQKRCKFivecHGNTLLPQFLGMYRL-------TVDGVETYMVV 163
Cdd:COG5253  395 ------HSEHICFRPM-----------------IFEYYVHVLF----NPLTLLCKIFGFYRVksrssisSSKSRKIYFIV 447
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 164 TRNVFSHRLtVHRKYDLKGSTVAREASDKEKAKD-LPTFKDNDFLNEGQKlHVGEESKKNFLEKLKRDVEFLAQLKIMDY 242
Cdd:COG5253  448 MENLFYPHG-IHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWIRESPK-IVFGLKKKLLLSQVWNDVLFLSKLNIMDY 525

                 ....*...
gi 767996101 243 SLLVGIHD 250
Cdd:COG5253  526 SLLVGIDD 533
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
2-376 6.24e-31

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: 119.77  E-value: 6.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101   2 LMPDDFKAyskiKVDNHLFNKENlpsrFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAP-INSDSQGRCGTRFLTTYD 80
Cdd:cd17304   30 LSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPyLQFISNSKSGQDFFLTND 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  81 RRFVIKTVSSEDVAEMHNILKKYHQMagslaclcilslpcgipisgwqkrckfiVECHGNTLLPQFLGMYRLTVDGV-ET 159
Cdd:cd17304  102 KRFFLKTQTKREAKFLLSILRKYVQH----------------------------LENYPHSLLVKFLGVHSIKLPGKkKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 160 YMVVTRNVFSHRLTVHRKYDLKGSTVAR-EASDKEKAKDLPTFKDNDFlnEGQKLHVGEEsKKNFLEKLKRDVEFLAQLK 238
Cdd:cd17304  154 YFIVMQSVFYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQ-RSWFLRQVEIDTEFLKGLN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 239 IMDYSLLVGI----HDVDRaeqeemeveeraedeecendgvggNLLcsygtpPDSPGNLlsfprffgpgefdpsvdvyam 314
Cdd:cd17304  231 VLDYSLLVGFqplhSDENR------------------------RLL------PNYKNAL--------------------- 259
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996101 315 ksHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFNEFMSN 376
Cdd:cd17304  260 --HVVDGPEYRYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWVED 318
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
39-248 7.31e-28

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: 110.29  E-value: 7.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101  39 FRNLRERFGIDDQDYQNSVTRSAPINSdSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKY-HQMAGSLaclcils 117
Cdd:cd17300   13 FHALRSLYCGGEDDFIRSLSRCVKWDA-SGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfEYMAKAL------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996101 118 lpcgipisgwqkrckfivECHGNTLLPQFLGMYRLTVDGVET------YMVVTRNVFsHRLTVHRKYDLKGSTVAREASD 191
Cdd:cd17300   85 ------------------FHKRPSLLAKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNV 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767996101 192 KEKakDLPTFKDNDFLNE--GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGI 248
Cdd:cd17300  146 AED--EDSVLLDENFLEYtkGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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