|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
66-768 |
0e+00 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 792.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 66 ERVLPNGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSGDAYK 145
Cdd:PLN03185 2 ELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 146 GQWVMNLKHGHGVKSFANGDAYDGEWRRGLQEGQGKYQWSDGSYYIGEWKNGTICGKGSFVWTNGNRYDGFWDEGFPRGN 225
Cdd:PLN03185 82 GRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 226 GTFKWDNGSFYVGHWSKDPEEMNGTYYPSGNE--GNLEWDPK---------DLFNNLSEYTICSGERVPTLPSQKKLSV- 293
Cdd:PLN03185 162 GVYTWSDGGCYVGTWTRGLKDGKGVFYPAGSRvpAVQEFYLNalrkrgvlpDLRRQNQVLSSHNSEQLSRGVSSDKLSKg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 294 ------WNSSKRIEKPRRTSVDGRVSVGVDRAFEKMNMWGNEIGEGgadmrKELDAELMRLDAEGLQSLKSSPV------ 361
Cdd:PLN03185 242 sllpleQSRNRNVSLERRWSLEVSIEKVIGHDYSGSSSAVLDEGSE-----VEYKANRPILEREYMQGVLISELvlnnsf 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 362 ----------PMKLPKAGRKQGETISKGHRNYELMLNLQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWRRFPREGTKYT 431
Cdd:PLN03185 317 sstsrrakrrQKKLVKEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMNFPKAGSQLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 432 PPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLSICGNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGML 511
Cdd:PLN03185 397 PSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRML 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 512 AAYYNHVRAFENSLVIRFFGLHCVKLNGptQKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKpeSEIDSNTILKDL 591
Cdd:PLN03185 477 PDYHHHVKTYENTLITKFFGLHRIKPSS--GQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADK--VEIDENTTLKDL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 592 DLNFIFRLQKAWYQEFIRQIDKDCEFLEQERIMDYSLLVGIHFREASVAGELIP---SGARTPIGESEEES--------- 659
Cdd:PLN03185 553 DLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPysrSITADGLEVVAEEDtiedeelsy 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 660 ------------------GP--RLSR--------AEVDELLSDPSRwASIRLGTNMPARAERTMRKNDSELQLVGEPtge 711
Cdd:PLN03185 633 peglvlvprgaddgstvpGPhiRGSRlrasaagdEEVDLLLPGTAR-LQIQLGVNMPARAERIPGREDKEKQSFHEV--- 708
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 15227305 712 fYEVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIFKVF 768
Cdd:PLN03185 709 -YDVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFIQKVF 764
|
|
| PIPKc_AtPIP5K_like |
cd17302 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ... |
382-767 |
0e+00 |
|
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: 608.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 382 NYELMLNLQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWRRFPREGTKYtPPHQSTEFKWKDYCPLVFRSLRKLFKVDPA 461
Cdd:cd17302 1 SYDLMLNLQLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTP-PPHQSSDFKWKDYCPMVFRNLRELFGIDAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 462 DYMLSICGNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGpt 541
Cdd:cd17302 80 DYMLSLCGDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVKPVG-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 542 QKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTILKDLDLNFIFRLQKAWYQEFIRQIDKDCEFLEQE 621
Cdd:cd17302 158 GRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTTLKDLDLDFKFRLEKGWRDALMRQIDADCAFLEAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 622 RIMDYSLLVGIHFREasvagelipsgartpigeseeesgprlsraevdellsdpsrwasirlgtnmparaertmrkndse 701
Cdd:cd17302 238 RIMDYSLLLGVHFRA----------------------------------------------------------------- 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227305 702 lqlvGEPTGEFYEVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIFKV 767
Cdd:cd17302 253 ----GDSTGEPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIRKV 314
|
|
| PIPKc |
smart00330 |
Phosphatidylinositol phosphate kinases; |
410-768 |
1.46e-157 |
|
Phosphatidylinositol phosphate kinases;
Pssm-ID: 214623 [Multi-domain] Cd Length: 342 Bit Score: 461.08 E-value: 1.46e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 410 PSAFDPKDKIWRRFPREgTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLSICGNDaLRELSSPGKSGSFFYLT 489
Cdd:smart00330 2 PSDFKATEKIKFPTPGH-LELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSP-PLELSSGGKSGSFFYLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 490 NDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGPTQKKVRFVIMGNLFCSKYSVHRRFDLKGS 569
Cdd:smart00330 80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGTEKKIYFLVMENLFYSDLKVHRKYDLKGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 570 SLGRTTDKpeSEIDSNTILKDLDL----NFIFRLQKAWYQEFIRQIDKDCEFLEQERIMDYSLLVGIHFREASVAGELIP 645
Cdd:smart00330 160 TRGREADK--KKVKELPVLKDLDLvemwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 646 SGARTPIGESEEESGPRLSRAEV-DELLSDPSRWASIRLGTnMPARAERTMRkndselqlvgeptgefyeVVMIFGIIDI 724
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDItGNLLVSNSPDGDGPFGG-IPARAIRARR------------------VVLYLGIIDI 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15227305 725 LQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIFKVF 768
Cdd:smart00330 299 LQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
|
|
| PIP5K |
pfam01504 |
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ... |
467-767 |
1.74e-117 |
|
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: 353.31 E-value: 1.74e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 467 ICGNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGptqKKVR 546
Cdd:pfam01504 1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGG---KKIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 547 FVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTILKDLDLNFI---FRLQKAWYQEFIRQIDKDCEFLEQERI 623
Cdd:pfam01504 78 FVVMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFLERklkLRLGPEKREALLKQLERDCEFLESLNI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 624 MDYSLLVGIHFREasvagelipsgartpigeseeesgprlsraevdellsdpsrwasirlgtnmparaertmrkndselq 703
Cdd:pfam01504 158 MDYSLLLGIHDLD------------------------------------------------------------------- 170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227305 704 lvgeptgEFYEVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIFKV 767
Cdd:pfam01504 171 -------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
|
|
| PIPKc_PIP5K_yeast_like |
cd17303 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ... |
383-766 |
1.70e-101 |
|
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: 315.39 E-value: 1.70e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 383 YELMLNLQLGIRHSVGRQAPAASLDLKPSAFDPKDKiwRRFPREGTKYTPPHQStEFKWKDYCPLVFRSLRKLFKVDPAD 462
Cdd:cd17303 1 YVLMYNMLTGIRVAVSRCAAKVDRELTDADFKAVHK--FSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 463 YMLSICGNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLngPTQ 542
Cdd:cd17303 78 YLMSLTGKYILSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKM--PRG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 543 KKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTILKdlDLNFIfRLQKAWY------QEFIRQIDKDCE 616
Cdd:cd17303 156 RKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRETPEDKLAKGPRATLK--DLNWL-RRKRKLAlgpekrKQFLTQLKRDVE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 617 FLEQERIMDYSLLVGIHFREasvagelipsGARTPIGESeeesgprlsraevdellsdpsrwasirlgtnmparaertmr 696
Cdd:cd17303 233 FLASLNIMDYSLLVGIHDLD----------GGFQATDEN----------------------------------------- 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 697 kndselqlvGEPTGEFYEVvmifGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIFK 766
Cdd:cd17303 262 ---------NEPGDEIYYL----GIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
|
|
| PIPKc |
cd00139 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ... |
438-766 |
5.03e-98 |
|
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: 304.11 E-value: 5.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 438 EFKWKDYCPLVFRSLRKLFKVDPADYMLSICGNDALREL-SSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYN 516
Cdd:cd00139 2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 517 HVRAFENSLVIRFFGLHCVKLNGptQKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTILKDLDL--- 593
Cdd:cd00139 82 HIKKNPNSLLTRFYGLYSIKLQK--GKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEKEKKKGLKVLKDLDFlek 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 594 NFIFRLQKAWYQEFIRQIDKDCEFLEQERIMDYSLLVGIHFReasvagelipsgartpigeseeesgprlsraevdells 673
Cdd:cd00139 160 GEKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL-------------------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 674 dpsrwasirlgtnmparaertmrkndselqlvgeptgefyevVMIFGIIDILQDYDISKKLEHAYKSIQYD-PSSISAVD 752
Cdd:cd00139 202 ------------------------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGkDSGISCVP 239
|
330
....*....|....
gi 15227305 753 PRQYSRRFRDFIFK 766
Cdd:cd00139 240 PDEYAERFLKFMES 253
|
|
| PIPKc_PIP5KI |
cd17301 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ... |
383-768 |
1.05e-95 |
|
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: 300.32 E-value: 1.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 383 YELMLNLQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWrrFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPAD 462
Cdd:cd17301 1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVF--FPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 463 YMLSICgNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGptq 542
Cdd:cd17301 79 YLLSLC-NEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 543 KKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTiLKDLDLNFIFR----LQKAWYQEFIRQIDKDCEFL 618
Cdd:cd17301 155 KNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPT-LKDLDFMEDHPegilLEPDTYDALLKTIQRDCRVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 619 EQERIMDYSLLVGIHFreasVAGelIPsgARTPIGESeeesgprlsraevdellsdpsrwasirlgtnmparaertmrkn 698
Cdd:cd17301 234 ESFKIMDYSLLLGVHN----LGG--IP--ARNSKGER------------------------------------------- 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227305 699 dselqlvgeptgefyevVMIF-GIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIF-KVF 768
Cdd:cd17301 263 -----------------LLLFiGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMAnTVF 317
|
|
| PIPKc_PIP5K1B |
cd17307 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
389-768 |
4.36e-62 |
|
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: 211.39 E-value: 4.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 389 LQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWrrFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLSIC 468
Cdd:cd17307 7 IQLGIGYTVGNLTSKPDRDVLMQDFYVVESVF--LPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSIC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 469 gNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGptqKKVRFV 548
Cdd:cd17307 85 -SEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGG---INIRIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 549 IMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEiDSNTILKDLDlnFIFRLQKAW------YQEFIRQIDKDCEFLEQER 622
Cdd:cd17307 161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKERE-KSCPTYKDLD--FLQDMHDGLyfdpetYNALMKTLQRDCRVLESFK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 623 IMDYSLLVGIHFreasvagelipsgartpigeseeesgprlsraevdellsdpsrwasirLGtNMPARAERTMRkndsel 702
Cdd:cd17307 238 IMDYSLLLGIHV------------------------------------------------LG-GIPAKNHKGEK------ 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227305 703 qlvgeptgefyeVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFI-FKVF 768
Cdd:cd17307 263 ------------LLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMnSRVF 317
|
|
| PIPKc_PIP5K1A_like |
cd17306 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
389-764 |
4.49e-60 |
|
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: 206.39 E-value: 4.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 389 LQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWrrFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLSIC 468
Cdd:cd17306 10 IQLGITHTVGSLSTKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 469 gNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGptqKKVRFV 548
Cdd:cd17306 88 -SEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGG---KNIRIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 549 IMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTiLKDLDlnFI------FRLQKAWYQEFIRQIDKDCEFLEQER 622
Cdd:cd17306 164 VMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPT-YKDLD--FLqdipdgLFLDSDMYNALCKTLQRDCLVLQSFK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 623 IMDYSLLVGIHFREASVAGELipsgartpigESEEESGprlsraevdellsdpsrwasirlgtNMPARAERTMRkndsel 702
Cdd:cd17306 241 IMDYSLLVGIHNIDARRGGTI----------ETDDQMG-------------------------GIPARNSKGER------ 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227305 703 qlvgeptgefyeVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFI 764
Cdd:cd17306 280 ------------LLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFM 329
|
|
| PIPKc_PIP5K1C |
cd17308 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
389-764 |
1.92e-59 |
|
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: 204.46 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 389 LQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWrrFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLSIC 468
Cdd:cd17308 8 IQLGIGYTVGNLSSKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDYLYSLC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 469 gNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGptqKKVRFV 548
Cdd:cd17308 86 -NEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGG---KNIRVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 549 IMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEiDSNTILKDLDLNFIF----RLQKAWYQEFIRQIDKDCEFLEQERIM 624
Cdd:cd17308 162 VMNNILPRVVKMHLKFDLKGSTYKRRASKKERE-KSKPTFKDLDFMQDMpeglMLDADTFSALVKTLQRDCLVLESFKIM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 625 DYSLLVGIHfreaSVAGelIPSgartpigeseeesgprlsraevdellsdpsrwasirlgtnMPARAERtmrkndselql 704
Cdd:cd17308 241 DYSLLLGVH----NIGG--IPA----------------------------------------VNGKGER----------- 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 705 vgeptgefyeVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFI 764
Cdd:cd17308 264 ----------LLLYIGIIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFM 313
|
|
| PIPKc_PIP5KII |
cd17305 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ... |
432-764 |
1.01e-51 |
|
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: 182.47 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 432 PPHqsteFKWKDYCPLVFRSLRKLFKVDPADYMLSICGNDALrELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGML 511
Cdd:cd17305 50 PSH----FKVKEYCPLVFRNLRERFGIDDDDYLNSLTRSQPL-ASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHIL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 512 AAYYNH-VRAFENSLVIRFFGLHCVKLNGptqKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGR-TTDKpESEIDSNTiLK 589
Cdd:cd17305 125 KQYHQYiVERHGKTLLPQYLGMYRITVNG---VETYLVVMRNVFSPRLPIHKKYDLKGSTVDRqASDK-EKAKDLPT-LK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 590 DLDlnFIFRLQKAWY-----QEFIRQIDKDCEFLEQERIMDYSLLVGIHfreasvagelipsgartpigeseeesgprls 664
Cdd:cd17305 200 DND--FLNDGTKIYIgdeakAKLLETLKRDVEFLAKLNLMDYSLLVGIH------------------------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 665 raevdellsdpsrwasirlgtnmparaertmrkndselqlvgeptgefyEVVMIFGIIDILQDYDISKKLEHAYKSIQYD 744
Cdd:cd17305 247 -------------------------------------------------DCIYFMAIIDILTHYGAKKRAAHAAKTVKHG 277
|
330 340
....*....|....*....|.
gi 15227305 745 PSS-ISAVDPRQYSRRFRDFI 764
Cdd:cd17305 278 AGAeISTVKPEQYAKRFLEFI 298
|
|
| PIPKc_PIP5KL1 |
cd17304 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
380-764 |
2.01e-51 |
|
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: 182.17 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 380 HRNYELMLNLQLGIRHSVgRQAPAASLDLKPSAFDPKDKIwrrfpregTKYTPPHQSTEFKwkDYCPLVFRSLRKLFKVD 459
Cdd:cd17304 1 HEFYSLTCMMKEGLRAAI-QNSIDVPPKESLSDDDYTEVL--------TQVIPKHKGFEFR--TYAGPVFATLRQSLGIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 460 PADYMLSICGNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLng 539
Cdd:cd17304 70 EKEYQNSLSPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 540 PTQKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDkPESEiDSN--TILKDLDL--NFI-FRLQKAWyqeFIRQIDKD 614
Cdd:cd17304 148 PGKKKKYFIVMQSVFYPDERINERYDIKGCQVSRYTD-PEPE-GSQiiVVLKDLNFegNSInLGQQRSW---FLRQVEID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 615 CEFLEQERIMDYSLLVGIHfreasvagelipsgartpigeseeesgprlsraevdELLSDPSRwasiRLGTNMParaert 694
Cdd:cd17304 223 TEFLKGLNVLDYSLLVGFQ------------------------------------PLHSDENR----RLLPNYK------ 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 695 mrkndSELQLVGEPTGEFYevvmiFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFI 764
Cdd:cd17304 257 -----NALHVVDGPEYRYF-----VGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWV 316
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
66-242 |
9.18e-46 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 164.74 E-value: 9.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 66 ERVLPNGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSGDAYK 145
Cdd:COG4642 95 EGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 146 GQWVMNLKHGHGVKSFANGDAYDGEWRRGLQEGQGKYQWSDGSYYIGEWKNGTICGKGSFVWTNGNRYDGFWDEGFPRGN 225
Cdd:COG4642 175 GEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQ 254
|
170
....*....|....*..
gi 15227305 226 GTFKWDNGSFYVGHWSK 242
Cdd:COG4642 255 GTMTYADGSVYEGEWKN 271
|
|
| MSS4 |
COG5253 |
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms]; |
373-640 |
1.64e-45 |
|
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
Pssm-ID: 227578 [Multi-domain] Cd Length: 612 Bit Score: 172.82 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 373 GETISKGHRNYELMLNLQLGIRHSVGRQapaasldlkpsafdpkDKIWRRFPREGTKYTPPHQSTEFKWKDYCPLVFRSL 452
Cdd:COG5253 286 GMPLEGGHRNPQESYNMLTGIRVTLSRI----------------EEIMIKKTDTHLNEQFEEGLYEFSCKDYFPEVFREL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 453 RKLFKVDPAdyMLSICGNDALRElSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGL 532
Cdd:COG5253 350 RALCGCDEA--LVSLLSRYILWE-SNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNPLTLLCKIFGF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 533 HCVKL-NGPTQKKVR---FVIMGNLFCSKySVHRRFDLKGSSLGRTTdkpESEIDSNTILKDL-DLNFIFRLQKAWY--- 604
Cdd:COG5253 427 YRVKSrSSISSSKSRkiyFIVMENLFYPH-GIHRIFDLKGSMRNRHV---ERTGKSMSVLLDMnDVEWIRESPKIVFglk 502
|
250 260 270
....*....|....*....|....*....|....*....
gi 15227305 605 -QEFIRQIDKDCEFLEQERIMDYSLLVGIHF--REASVA 640
Cdd:COG5253 503 kKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDerEEASVG 541
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
62-219 |
4.00e-44 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 160.12 E-value: 4.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 62 FYHAERVLPNGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSG 141
Cdd:COG4642 114 GGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANG 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227305 142 DAYKGQWVMNLKHGHGVKSFANGDAYDGEWRRGLQEGQGKYQWSDGSYYIGEWKNGTICGKGSFVWTNGNRYDGFWDE 219
Cdd:COG4642 194 DVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEWKN 271
|
|
| PIPKc_PIP5K2A |
cd17309 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ... |
385-764 |
7.29e-41 |
|
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: 152.05 E-value: 7.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 385 LMLNLQLGIRHSVGR----QAPAAsldLKPSAFdpkdKIWRRFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDP 460
Cdd:cd17309 11 LLSVLMWGVNHSINElshvQIPVM---LMPDDF----KAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 461 ADYMLSICGNDALRElSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNH-VRAFENSLVIRFFGLHCVKLNG 539
Cdd:cd17309 84 QDFQNSLTRSAPLAN-DSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYiVECHGNTLLPQFLGMYRLTVDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 540 ptqKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTiLKDLDlnFIFRLQKAWYQE-----FIRQIDKD 614
Cdd:cd17309 163 ---VETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPT-LKDND--FINDGQKIYIDEnnkkmFLEKLKKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 615 CEFLEQERIMDYSLLVGIHfreasvagelipsgartpigeseeesgprlsraevdellsdpsrwasirlgtnmparaert 694
Cdd:cd17309 237 VEFLAQLKLMDYSLLVGIH------------------------------------------------------------- 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227305 695 mrkndselqlvgeptgefyEVVMIFGIIDILQDYDISKKLEHAYKSIQYDP-SSISAVDPRQYSRRFRDFI 764
Cdd:cd17309 256 -------------------DVVYFMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 307
|
|
| PIPKc_PIKfyve |
cd17300 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ... |
444-768 |
1.36e-40 |
|
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: 149.97 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 444 YCPLVFRSLRKLFKVDPADYMLSICgnDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHV-RAFE 522
Cdd:cd17300 8 YFAEQFHALRSLYCGGEDDFIRSLS--RCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMaKALF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 523 N---SLVIRFFGL---HCVKLNGPTQKKVRFVIMGNLFCSKySVHRRFDLKGSSLGRTTDKPESEidsNTILkdLDLNFI 596
Cdd:cd17300 86 HkrpSLLAKILGVyriSVKNSTTNKTSKQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDE---DSVL--LDENFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 597 -------FRLQKAWYQEFIRQIDKDCEFLEQERIMDYSLLVGIhfreasvagelipsgartpigeseeesgprlsraevd 669
Cdd:cd17300 160 eytkgspLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI------------------------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 670 ellsdpsrwasirlgtnmparaertmrkNDSELQLVgeptgefyevvmiFGIIDILQDYDISKKLEHAYKSI-----QYD 744
Cdd:cd17300 203 ----------------------------DEEKKELV-------------VGIIDYIRTYTWDKKLESWVKSLgilggGGE 241
|
330 340
....*....|....*....|....
gi 15227305 745 PSSISavdPRQYSRRFRDFIFKVF 768
Cdd:cd17300 242 PTVIS---PELYKKRFREAMDKYF 262
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
71-255 |
2.63e-40 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 149.34 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 71 NGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSGDAYKGQWVM 150
Cdd:COG4642 77 GGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 151 NLKHGHGVKSFANGDAYDGEWRRGLQEGQGKYQWSDGSYYIGEWKNGTICGKGSFVWTNGNRYDGFWDEGFPRGNGTFKW 230
Cdd:COG4642 157 GKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTY 236
|
170 180
....*....|....*....|....*.
gi 15227305 231 DNGSFYVGHWSKDPEEMNGTY-YPSG 255
Cdd:COG4642 237 ADGDRYEGEFKNGKRHGQGTMtYADG 262
|
|
| PIPKc_PIP5K2B |
cd17310 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ... |
389-764 |
3.05e-38 |
|
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: 144.81 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 389 LQLGIRHSVGR--QAPAASLdLKPSAFdpkdKIWRRFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLS 466
Cdd:cd17310 17 LMWGVNHTINElsNVPVPVM-LMPDDF----KAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 467 ICGNDALRElSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNH-VRAFENSLVIRFFGLHCVKLNGptqKKV 545
Cdd:cd17310 92 VTRSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFiVECHGNTLLPQFLGMYRLTVDG---VET 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 546 RFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTiLKDLDlnFIFRLQKAWYQE-----FIRQIDKDCEFLEQ 620
Cdd:cd17310 168 YMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPT-FKDND--FLNEGQKLHVGEeskknFLEKLKRDVEFLAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 621 ERIMDYSLLVGIHfreasvagelipsgartpigeseeesgprlsraevdellsdpsrwasirlgtnmparaertmrknds 700
Cdd:cd17310 245 LKIMDYSLLVGIH------------------------------------------------------------------- 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227305 701 elqlvgeptgefyEVVMIFGIIDILQDYDISKKLEHAYKSIQYDP-SSISAVDPRQYSRRFRDFI 764
Cdd:cd17310 258 -------------DVVYFMAIIDILTPYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFNEFM 309
|
|
| PIPKc_PIP5K2C |
cd17311 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ... |
392-764 |
1.09e-36 |
|
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: 140.00 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 392 GIRHSVGR--QAPAASLdLKPSAFDPKDKIW---RRFPREGTkytPPHqsteFKWKDYCPLVFRSLRKLFKVDPADYMLS 466
Cdd:cd17311 9 GVNHSINElsQVPVPVM-LLPDDFKANSKIKvnnHLFNRENL---PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 467 ICGNDALRElssPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNH-VRAFENSLVIRFFGLHCVKLNGptqKKV 545
Cdd:cd17311 81 LTRSPPYSE---SEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYiVKCHGNTLLPQFLGMYRLSVDN---EDS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 546 RFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTiLKDLDlnFIFRLQKAWYQE-----FIRQIDKDCEFLEQ 620
Cdd:cd17311 155 YMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMD--FLNKNQKVYVGEeqkriFLEKLKRDVEFLVQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 621 ERIMDYSLLVGIHfreasvagelipsgartpigeseeesgprlsraevdellsdpsrwasirlgtnmparaertmrknds 700
Cdd:cd17311 232 LKIMDYSLLLGIH------------------------------------------------------------------- 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227305 701 elqlvgeptgefyEVVMIFGIIDILQDYDISKKLEHAYKSIQYDP-SSISAVDPRQYSRRFRDFI 764
Cdd:cd17311 245 -------------DVVYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHPEQYAKRFLDFI 296
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
70-281 |
1.21e-18 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 86.55 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 70 PNGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSGDAYKGQWV 149
Cdd:COG4642 18 LGGGGEGGLAAAGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGDGGGGEGG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 150 mnlkhghgvksFANGDAYDGEWRRGLQEGQGKYQWSDGSYYIGEWKNGTICGKGSFVWTNGNRYDGFWDEGFPRGNGTFK 229
Cdd:COG4642 98 -----------FGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15227305 230 WDNGSFYVGHWSKDpeEMNGT---YYPSGN--EGNLEwdpKDLFNNLSEYTICSGER 281
Cdd:COG4642 167 YADGDRYEGEFKNG--KRHGQgtlTYANGDvyEGEFK---NGQRHGQGTYTYADGDR 218
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
100-256 |
1.28e-08 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 56.89 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 100 GDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSGDAYKGQWVMNLKHGHGVKSFANGDAYDGEWRRGLQEGQ 179
Cdd:COG4642 2 GSVAEDGAGGGGDATALGGGGEGGLAAAGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 180 GKYQWSDGSYYIGEWKNGTIC------------GKGSFVWTNGNRYDGFWDEGFPRGNGTFKWDNGSFYVGHWSKDPEEM 247
Cdd:COG4642 82 GGGKGDGGDGGGGEGGFGGGGgggggkkgggggGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHG 161
|
170
....*....|
gi 15227305 248 NGTY-YPSGN 256
Cdd:COG4642 162 QGTLtYADGD 171
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
167-189 |
5.30e-05 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 40.47 E-value: 5.30e-05
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
75-97 |
5.85e-04 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 37.77 E-value: 5.85e-04
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
190-212 |
6.58e-04 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 37.39 E-value: 6.58e-04
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
144-165 |
6.98e-04 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 37.39 E-value: 6.98e-04
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
165-186 |
9.36e-04 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 36.93 E-value: 9.36e-04
|
| YwqK |
COG2849 |
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms]; |
57-197 |
2.27e-03 |
|
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
Pssm-ID: 442097 [Multi-domain] Cd Length: 163 Bit Score: 39.67 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227305 57 SSLEEFYHAERVLPNGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGA-TYEGEFKSGYMDGIGT 135
Cdd:COG2849 16 LKLKYELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGQlKSEGTYKNGKLEGEWK 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227305 136 YTGPSGD-AYKGQWVMNLKHGHGVKSFANGD-AYDGEWRRGLQEGQGKYQWSDGS-YYIGEWKNG 197
Cdd:COG2849 96 EYYENGKlKSEGNYKNGKLHGEWKEYYENGKlKEEGNYKNGKKDGVWKYYDENGKlVKEEEYKNG 160
|
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
142-163 |
4.81e-03 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 35.01 E-value: 4.81e-03
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
121-142 |
5.42e-03 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 34.69 E-value: 5.42e-03
|
| |
