|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
48-810 |
0e+00 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 1547.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 48 RELVLPDGESYSGSLLGNVPEGPGKYIWSDGCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYVDANKLTY 127
Cdd:PLN03185 1 GELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 128 KGRWRLNLKHGLGYQVYPNGDVFEGSWIQGLGEGPGKYTWANKNVYLGDMKGGKMSGKGTLTWVTGDSYEGSWLNGMMHG 207
Cdd:PLN03185 81 KGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 208 VGVYTWSDGGCYVGTWTRGLKDGKGSFYSAGTRVPVVQEFYLNALRKRGVLPDMRRQNQVASSVNMENLRVGVNRNKLSK 287
Cdd:PLN03185 161 FGVYTWSDGGCYVGTWTRGLKDGKGVFYPAGSRVPAVQEFYLNALRKRGVLPDLRRQNQVLSSHNSEQLSRGVSSDKLSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 288 GSLINLEQSRNGRVSLERRWSLEVSIEKVIGHGYSDLSTAVLDSGSSVQYKANIPILEREYMQGVLISELVVNNGFSRTS 367
Cdd:PLN03185 241 GSLLPLEQSRNRNVSLERRWSLEVSIEKVIGHDYSGSSSAVLDEGSEVEYKANRPILEREYMQGVLISELVLNNSFSSTS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 368 RRAKRKHKRLVKEAKKPGEVVIKGHRSYDLMLSLQLGIRYTVGKITPIQRRQVRTADFGPRASFWMTFPRAGSTMTPPHH 447
Cdd:PLN03185 321 RRAKRRQKKLVKEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMNFPKAGSQLTPSHQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 448 SEDFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYH 527
Cdd:PLN03185 401 SEDFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 528 HHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSADKVEIDENTILKDLDLNYSFFL 607
Cdd:PLN03185 481 HHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENTTLKDLDLNYSFYL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 608 ETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVHHRAPQHLRSQLVRSQSITTDALESVAEDDTIEDDMLSYHEGLVLVP 687
Cdd:PLN03185 561 EPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITADGLEVVAEEDTIEDEELSYPEGLVLVP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 688 RGSE--NTVTGPHIRGSRLRASAVGDEEVDLLLPGTARLQIQQGVNMPARAELIPGREDKEKQILHDCCDVVLYLGIIDI 765
Cdd:PLN03185 641 RGADdgSTVPGPHIRGSRLRASAAGDEEVDLLLPGTARLQIQLGVNMPARAERIPGREDKEKQSFHEVYDVVLYLGIIDI 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1063710527 766 LQEYNMTKKIEHAYKSLHFDSLSISAVDPTFYSQRFLEFIKKVFP 810
Cdd:PLN03185 721 LQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFIQKVFP 765
|
|
| PIPKc_AtPIP5K_like |
cd17302 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ... |
394-808 |
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: 570.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 394 SYDLMLSLQLGIRYTVGKITPIQRRQVRTADFGPRASFWMTFPRAGSTMtPPHHSEDFKWKDYCPMVFRNLREMFKIDAA 473
Cdd:cd17302 1 SYDLMLNLQLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTP-PPHQSSDFKWKDYCPMVFRNLRELFGIDAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 474 DYMMSICGNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQ 553
Cdd:cd17302 80 DYMLSLCGDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVKPVGGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 554 KFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSADK--VEIDENTILKDLDLNYSFFLETSWREGLLRQLEIDSKFLEAQNI 631
Cdd:cd17302 160 KVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKpeSEIDPNTTLKDLDLDFKFRLEKGWRDALMRQIDADCAFLEALRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 632 MDYSLLLGVHHRAPqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvprgsentvtgphirgsrlrasavgd 711
Cdd:cd17302 240 MDYSLLLGVHFRAG------------------------------------------------------------------ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 712 eevdlllpgtarlqiqqgvnmparaelipgredkekQILHDCCDVVLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSISA 791
Cdd:cd17302 254 ------------------------------------DSTGEPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPASISA 297
|
410
....*....|....*..
gi 1063710527 792 VDPTFYSQRFLEFIKKV 808
Cdd:cd17302 298 VDPKLYSRRFRDFIRKV 314
|
|
| PIPKc |
smart00330 |
Phosphatidylinositol phosphate kinases; |
423-809 |
9.34e-132 |
|
Phosphatidylinositol phosphate kinases;
Pssm-ID: 214623 [Multi-domain] Cd Length: 342 Bit Score: 395.98 E-value: 9.34e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 423 ADFGPRASFWMTFPRAgSTMTPPHHSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDtLRELSSPGKSGSVFFLSQ 502
Cdd:smart00330 3 SDFKATEKIKFPTPGH-LELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSP-PLELSSGGKSGSFFYLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 503 DDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQ--KFRFVVMGNMFFTDLRIHRRFDLKGSS 580
Cdd:smart00330 81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGTekKIYFLVMENLFYSDLKVHRKYDLKGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 581 LGRSADKVEIDENTILKDLDL----NYSFFLETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVHHRapqhlrsqlvrsq 656
Cdd:smart00330 161 RGREADKKKVKELPVLKDLDLvemwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDI------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 657 sittdalESVAEDDTIEDDMLSYHEGlvlvprgsentvtgphiRGSRLRASAVGDEEVDLLLPGTARLQIQQGVNMPARA 736
Cdd:smart00330 228 -------ERGQREEIELPPVYGSDES-----------------PSSESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARA 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710527 737 ElipgredkekqilhDCCDVVLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSISAVDPTFYSQRFLEFIKKVF 809
Cdd:smart00330 284 I--------------RARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
|
|
| PIP5K |
pfam01504 |
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ... |
479-808 |
6.16e-111 |
|
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: 337.52 E-value: 6.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 479 ICGNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKPsSGQKFRFV 558
Cdd:pfam01504 1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKP-GGKKIYFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 559 VMGNMFFTDLRIHRRFDLKGSSLGRSADKVE--IDENTILKDLDLNYS---FFLETSWREGLLRQLEIDSKFLEAQNIMD 633
Cdd:pfam01504 80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEreKDEPTTLKDLDFLERklkLRLGPEKREALLKQLERDCEFLESLNIMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 634 YSLLLGVHhrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvprgsentvtgphirgsrlrasavgdee 713
Cdd:pfam01504 160 YSLLLGIH------------------------------------------------------------------------ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 714 vdlllpgtarlqiqqgvnmparaelipgredkekqILHDCCDVVLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSISAVD 793
Cdd:pfam01504 168 -----------------------------------DLDEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAVP 212
|
330
....*....|....*
gi 1063710527 794 PTFYSQRFLEFIKKV 808
Cdd:pfam01504 213 PKEYAERFLKFIEKI 227
|
|
| PIPKc_PIP5K_yeast_like |
cd17303 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ... |
395-805 |
3.44e-100 |
|
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: 313.08 E-value: 3.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 395 YDLMLSLQLGIRYTVGKITPIQRRQVRTADFGPRASFwmTFPRAGSTMTPPHHSeDFKWKDYCPMVFRNLREMFKIDAAD 474
Cdd:cd17303 1 YVLMYNMLTGIRVAVSRCAAKVDRELTDADFKAVHKF--SFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 475 YMMSICGNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQK 554
Cdd:cd17303 78 YLMSLTGKYILSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKMPRGRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 555 FRFVVMGNMFFTDLRIHRRFDLKGSSLGR--SADKVEIDENTILKDLD---LNYSFFLETSWREGLLRQLEIDSKFLEAQ 629
Cdd:cd17303 158 IHFVVMNNLFPPHRDIHQTFDLKGSTVGRetPEDKLAKGPRATLKDLNwlrRKRKLALGPEKRKQFLTQLKRDVEFLASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 630 NIMDYSLLLGVHHrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvprgsentvtgphiRGSRLRASAV 709
Cdd:cd17303 238 NIMDYSLLVGIHD---------------------------------------------------------LDGGFQATDE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 710 GDEEvdlllpgtarlqiqqgvnmparaelipgredkekqilhdcCDVVLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSI 789
Cdd:cd17303 261 NNEP----------------------------------------GDEIYYLGIIDILTPYNAKKKLEHFFKSLRHDRHTI 300
|
410
....*....|....*.
gi 1063710527 790 SAVDPTFYSQRFLEFI 805
Cdd:cd17303 301 SAVPPKEYARRFLKFI 316
|
|
| PIPKc_PIP5KI |
cd17301 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ... |
395-809 |
1.60e-97 |
|
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: 306.48 E-value: 1.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 395 YDLMLSLQLGIRYTVGKITPIQRRQVRTADFGPRASfwMTFPRAGSTMTPPHHSEDFKWKDYCPMVFRNLREMFKIDAAD 474
Cdd:cd17301 1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVES--VFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 475 YMMSICgNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQK 554
Cdd:cd17301 79 YLLSLC-NEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQ-SGGKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 555 FRFVVMGNMFFTDLRIHRRFDLKGSSLGRSADKVEIDENT-ILKDLDLNY----SFFLETSWREGLLRQLEIDSKFLEAQ 629
Cdd:cd17301 157 IRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSpTLKDLDFMEdhpeGILLEPDTYDALLKTIQRDCRVLESF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 630 NIMDYSLLLGVHHrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvprgsentvtgphirgsrlrasav 709
Cdd:cd17301 237 KIMDYSLLLGVHN------------------------------------------------------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 710 gdeevdlllPGTarlqiqqgvnmparaelIPGREDKEKQILhdccdvvLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSI 789
Cdd:cd17301 250 ---------LGG-----------------IPARNSKGERLL-------LFIGIIDILQSYRLKKKLEHTWKSVVHDGDTV 296
|
410 420
....*....|....*....|.
gi 1063710527 790 SAVDPTFYSQRFLEFI-KKVF 809
Cdd:cd17301 297 SVHRPSFYAERFQNFMaNTVF 317
|
|
| PIPKc |
cd00139 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ... |
449-807 |
2.70e-97 |
|
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: 302.95 E-value: 2.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 449 EDFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLREL-SSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYH 527
Cdd:cd00139 1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 528 HHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSADKVE--IDENTILKDLDL---N 602
Cdd:cd00139 81 EHIKKNPNSLLTRFYGLYSIKLQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEKekKKGLKVLKDLDFlekG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 603 YSFFLETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVHHRapqhlrsqlvrsqsittdalesvaeddtieddmlsyheg 682
Cdd:cd00139 161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 683 lvlvprgsentvtgphirgsrlrasavgdeevdlllpgtarlqiqqgvnmparaelipgredkekqilhdccdvVLYLGI 762
Cdd:cd00139 202 --------------------------------------------------------------------------VYYLGI 207
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1063710527 763 IDILQEYNMTKKIEHAYKSLHFDSLS-ISAVDPTFYSQRFLEFIKK 807
Cdd:cd00139 208 IDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
|
|
| PIPKc_PIP5K1B |
cd17307 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
400-812 |
1.05e-69 |
|
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: 232.57 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 400 SLQLGIRYTVGKITPIQRRQVRTADFGPRASFWMtfPRAGSTMTPPHHSEDFKWKDYCPMVFRNLREMFKIDAADYMMSI 479
Cdd:cd17307 6 AIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFL--PSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 480 CgNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQKFRFVV 559
Cdd:cd17307 84 C-SEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQ-SGGINIRIVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 560 MGNMFFTDLRIHRRFDLKGSSLGRSADKVEIDENT-ILKDLD----LNYSFFLETSWREGLLRQLEIDSKFLEAQNIMDY 634
Cdd:cd17307 162 MNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCpTYKDLDflqdMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 635 SLLLGVHhrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvprgsentvtgphirgsrlrasavgdeev 714
Cdd:cd17307 242 SLLLGIH------------------------------------------------------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 715 dlLLPGtarlqiqqgvnmparaelIPGREDKEKQILhdccdvvLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSISAVDP 794
Cdd:cd17307 249 --VLGG------------------IPAKNHKGEKLL-------LFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRP 301
|
410
....*....|....*....
gi 1063710527 795 TFYSQRFLEFIK-KVFPQN 812
Cdd:cd17307 302 SFYADRFLKFMNsRVFKKV 320
|
|
| PIPKc_PIP5K1C |
cd17308 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
394-815 |
2.11e-65 |
|
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: 221.02 E-value: 2.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 394 SYDLMLSLQLGIRYTVGKITPIQRRQVRTADFGPRASFWmtFPRAGSTMTPPHHSEDFKWKDYCPMVFRNLREMFKIDAA 473
Cdd:cd17308 1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 474 DYMMSICgNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQ 553
Cdd:cd17308 79 DYLYSLC-NEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 554 KFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSADKVEIDEN-TILKDLDLNYSF----FLETSWREGLLRQLEIDSKFLEA 628
Cdd:cd17308 157 NIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSkPTFKDLDFMQDMpeglMLDADTFSALVKTLQRDCLVLES 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 629 QNIMDYSLLLGVHHrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvpRGSENTVTGphiRGSRLrasa 708
Cdd:cd17308 237 FKIMDYSLLLGVHN---------------------------------------------IGGIPAVNG---KGERL---- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 709 vgdeevdlllpgtarlqiqqgvnmparaelipgredkekqilhdccdvVLYLGIIDILQEYNMTKKIEHAYKSLHFDSLS 788
Cdd:cd17308 265 ------------------------------------------------LLYIGIIDILQSYRLIKKLEHTWKALVHDGDT 296
|
410 420
....*....|....*....|....*..
gi 1063710527 789 ISAVDPTFYSQRFLEFIKKVFPQNNKS 815
Cdd:cd17308 297 VSVHRPSFYAERFFKFMSNTVFRKSSS 323
|
|
| PIPKc_PIP5K1A_like |
cd17306 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
400-805 |
5.30e-62 |
|
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: 212.55 E-value: 5.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 400 SLQLGIRYTVGKITPIQRRQVRTADFGPRASFWmtFPRAGSTMTPPHHSEDFKWKDYCPMVFRNLREMFKIDAADYMMSI 479
Cdd:cd17306 9 AIQLGITHTVGSLSTKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 480 CgNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQKFRFVV 559
Cdd:cd17306 87 C-SEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-AGGKNIRIVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 560 MGNMFFTDLRIHRRFDLKGSSLGRSADKVEIDENT-ILKDL----DLNYSFFLETSWREGLLRQLEIDSKFLEAQNIMDY 634
Cdd:cd17306 165 MNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLpTYKDLdflqDIPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 635 SLLLGVHHrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvlvprgsentvtgphirgsrlrasavgdeeV 714
Cdd:cd17306 245 SLLVGIHN-----------------------------------------------------------------------I 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 715 DLLLPGTARLQIQQGVnmparaelIPGREDKEKQILhdccdvvLYLGIIDILQEYNMTKKIEHAYKSLHFDSLSISAVDP 794
Cdd:cd17306 254 DARRGGTIETDDQMGG--------IPARNSKGERLL-------LYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRP 318
|
410
....*....|.
gi 1063710527 795 TFYSQRFLEFI 805
Cdd:cd17306 319 GFYAERFQRFM 329
|
|
| PIPKc_PIP5KII |
cd17305 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ... |
445-807 |
3.26e-58 |
|
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: 200.58 E-value: 3.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 445 PHHsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLrELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLP 524
Cdd:cd17305 50 PSH---FKVKEYCPLVFRNLRERFGIDDDDYLNSLTRSQPL-ASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 525 DYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFFTDLRIHRRFDLKGSSLGRSA-DKVEIDENTILKDLDln 602
Cdd:cd17305 126 QYHQYiVERHGKTLLPQYLGMYRITVNGVETY-LVVMRNVFSPRLPIHKKYDLKGSTVDRQAsDKEKAKDLPTLKDND-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 603 ysfFLETSW--------REGLLRQLEIDSKFLEAQNIMDYSLLLGVHhrapqhlrsqlvrsqsittdalesvaeddtied 674
Cdd:cd17305 203 ---FLNDGTkiyigdeaKAKLLETLKRDVEFLAKLNLMDYSLLVGIH--------------------------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 675 dmlsyheglvlvprgsentvtgphirgsrlrasavgdeevdlllpgtarlqiqqgvnmparaelipgredkekqilhdcc 754
Cdd:cd17305 --------------------------------------------------------------------------------
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1063710527 755 DVVLYLGIIDILQEYNMTKKIEHAYKSL-HFDSLSISAVDPTFYSQRFLEFIKK 807
Cdd:cd17305 247 DCIYFMAIIDILTHYGAKKRAAHAAKTVkHGAGAEISTVKPEQYAKRFLEFISK 300
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
41-223 |
1.48e-46 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 167.44 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 41 EDARFRVRELVLPDGESYSGSLLGNVPEGPGKYIWSDGCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYV 120
Cdd:COG4642 87 DGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 121 DANKLTYKGRWRLNLKHGLGYQVYPNGDVFEGSWIQGLGEGPGKYTWANKNVYLGDMKGGKMSGKGTLTWVTGDSYEGSW 200
Cdd:COG4642 167 YADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
170 180
....*....|....*....|...
gi 1063710527 201 LNGMMHGVGVYTWSDGGCYVGTW 223
Cdd:COG4642 247 KNGKRHGQGTMTYADGSVYEGEW 269
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
55-241 |
5.74e-46 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 165.90 E-value: 5.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 55 GESYSGSLLGNVPEGPGKYIWSD-GCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYVDANKLTYKGRWRL 133
Cdd:COG4642 77 GGGGGGGGKGDGGDGGGGEGGFGgGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 134 NLKHGLGYQVYPNGDVFEGSWIQGLGEGPGKYTWANKNVYLGDMKGGKMSGKGTLTWVTGDSYEGSWLNGMMHGVGVYTW 213
Cdd:COG4642 157 GKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTY 236
|
170 180
....*....|....*....|....*...
gi 1063710527 214 SDGGCYVGTWTRGLKDGKGSFYSAGTRV 241
Cdd:COG4642 237 ADGDRYEGEFKNGKRHGQGTMTYADGSV 264
|
|
| PIPKc_PIP5KL1 |
cd17304 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ... |
449-805 |
6.70e-46 |
|
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PIP5KL1) and similar proteins; PIP5KL1 (EC 2.7.1.68), also known as PI(4)P 5-kinase-like protein 1, or PtdIns(4)P-5-kinase-like protein 1, may act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment, and conversion to PI(3,4,5)P3.
Pssm-ID: 340441 Cd Length: 319 Bit Score: 167.15 E-value: 6.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 449 EDFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHH 528
Cdd:cd17304 47 KGFEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 529 HVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSADKVEIDEN--TILKDLDLNYSFF 606
Cdd:cd17304 127 HLENYPHSLLVKFLGVHSIKLPGKKKKYFIVMQSVFYPDERINERYDIKGCQVSRYTDPEPEGSQiiVVLKDLNFEGNSI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 607 LETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVhhrapqhlrsqlvrsQSITTDalesvaeddtieddmlsyheglvlv 686
Cdd:cd17304 207 NLGQQRSWFLRQVEIDTEFLKGLNVLDYSLLVGF---------------QPLHSD------------------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 687 prgsENtvtgphirgSRlrasavgdeevdlLLPgtarlqiqqgvNMPARAELIPGREDKekqilhdccdvvLYLGIIDIL 766
Cdd:cd17304 247 ----EN---------RR-------------LLP-----------NYKNALHVVDGPEYR------------YFVGIIDIF 277
|
330 340 350
....*....|....*....|....*....|....*....
gi 1063710527 767 QEYNMTKKIEHAYKSLHFDSLSISAVDPTFYSQRFLEFI 805
Cdd:cd17304 278 TVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWV 316
|
|
| MSS4 |
COG5253 |
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms]; |
262-641 |
5.80e-45 |
|
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
Pssm-ID: 227578 [Multi-domain] Cd Length: 612 Bit Score: 171.67 E-value: 5.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 262 RRQNQVASSVNMENLRVGvnrNKLSKGSLINLEQSRNGRVSLERRWSLEVSIEKvIGHGYS--DLSTAVLDSGSSVqyka 339
Cdd:COG5253 177 SQPSRKPTSENPKSESDN---SKLPTSVNSPLPDKSLLKRTLSNFWAERNSYNW-KPLVYPscPSEHIFSDSDVII---- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 340 nipileREYMQGVLISELV-VNNGFSRTSRRAKRKhkrLVKEAKKPGEVVIKGHRSYDLMLSLQLGIRYTVGKITPIQRR 418
Cdd:COG5253 249 ------REDEPSSLIAFCLsTSDYRNKMMRLRDSE---TMDERLLNGMPLEGGHRNPQESYNMLTGIRVTLSRIEEIMIK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 419 QVRTADfgpRASFwmtfpragstmtpPHHSEDFKWKDYCPMVFRNLREMFKIDAAdyMMSICGNDTLRElSSPGKSGSVF 498
Cdd:COG5253 320 KTDTHL---NEQF-------------EEGLYEFSCKDYFPEVFRELRALCGCDEA--LVSLLSRYILWE-SNGGKSGSFF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 499 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIK-PSSGQ-----KFRFVVMGNMFFtDLRIHR 572
Cdd:COG5253 381 LFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNPLTLLCKIFGFYRVKsRSSISssksrKIYFIVMENLFY-PHGIHR 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063710527 573 RFDLKGSSLGRSADKVEIDENTILKDLDLNY-----SFFLETSwREGLLRQLEIDSKFLEAQNIMDYSLLLGVH 641
Cdd:COG5253 460 IFDLKGSMRNRHVERTGKSMSVLLDMNDVEWirespKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGID 532
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
49-202 |
1.48e-42 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 155.88 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 49 ELVLPDGESYSGSLLGNVPEGPGKYIWSDGCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYVDANKLTYK 128
Cdd:COG4642 118 VLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYE 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063710527 129 GRWRLNLKHGLGYQVYPNGDVFEGSWIQGLGEGPGKYTWANKNVYLGDMKGGKMSGKGTLTWVTGDSYEGSWLN 202
Cdd:COG4642 198 GEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEWKN 271
|
|
| PIPKc_PIKfyve |
cd17300 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ... |
461-809 |
1.51e-37 |
|
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: 141.49 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 461 FRNLREMFKIDAADYMMSICgnDTLRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYEN----T 536
Cdd:cd17300 13 FHALRSLYCGGEDDFIRSLS--RCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFhkrpS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 537 LITKFFGLHRIK---PSSGQKFR--FVVMGNMFFtDLRIHRRFDLKGSSLGRSADkVEIDENTILkdLDLNysfFLETSW 611
Cdd:cd17300 91 LLAKILGVYRISvknSTTNKTSKqdLLVMENLFY-GRNISQVYDLKGSLRNRYVN-VAEDEDSVL--LDEN---FLEYTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 612 REG----------LLRQLEIDSKFLEAQNIMDYSLLLGVhhrapqhlrsqlvrsqsittdalesvaeddtieddmlsyhe 681
Cdd:cd17300 164 GSPlylrehskavLMAAIWNDTLFLSSQNVMDYSLLVGI----------------------------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 682 glvlvprgsentvtgphirgsrlrasavgdeevdlllpgtarlqiqqgvnmparaelipgreDKEKQilhdccdvVLYLG 761
Cdd:cd17300 203 --------------------------------------------------------------DEEKK--------ELVVG 212
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1063710527 762 IIDILQEYNMTKKIEHAYKSL--HFDSLSISAVDPTFYSQRFLEFIKKVF 809
Cdd:cd17300 213 IIDYIRTYTWDKKLESWVKSLgiLGGGGEPTVISPELYKKRFREAMDKYF 262
|
|
| PIPKc_PIP5K2B |
cd17310 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ... |
451-805 |
1.84e-37 |
|
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: 142.88 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 451 FKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLRElSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH- 529
Cdd:cd17310 64 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINS-DSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFi 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 530 VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSA-DKVEIDENTILKDLD-LN--YSF 605
Cdd:cd17310 143 VECHGNTLLPQFLGMYRLT-VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREAsDKEKAKDLPTFKDNDfLNegQKL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 606 FLETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVHhrapqhlrsqlvrsqsittdalesvaeddtieddmlsyheglvl 685
Cdd:cd17310 222 HVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIH-------------------------------------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 686 vprgsentvtgphirgsrlrasavgdeevdlllpgtarlqiqqgvnmparaelipgredkekqilhdccDVVLYLGIIDI 765
Cdd:cd17310 258 ---------------------------------------------------------------------DVVYFMAIIDI 268
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063710527 766 LQEYNMTKKIEHAYKSL-HFDSLSISAVDPTFYSQRFLEFI 805
Cdd:cd17310 269 LTPYDAKKKAAHAAKTVkHGAGAEISTVNPEQYSKRFNEFM 309
|
|
| PIPKc_PIP5K2C |
cd17311 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ... |
445-805 |
2.75e-37 |
|
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: 141.93 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 445 PHHsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLRElssPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLP 524
Cdd:cd17311 50 PSH---FKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSPPYSE---SEGSDGRFLLSYDRTLVIKEISSEDVADMHSILS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 525 DYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFFTDLRIHRRFDLKGSSLGRSA-DKVEIDENTILKDLDL- 601
Cdd:cd17311 124 HYHQYiVKCHGNTLLPQFLGMYRLSVDNEDSY-MLVMRNMFSHRLPVHRKYDLKGSLVSREAsDKEKVKELPTLKDMDFl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 602 --NYSFFLETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVHhrapqhlrsqlvrsqsittdalesvaeddtieddmlsy 679
Cdd:cd17311 203 nkNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIH-------------------------------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 680 heglvlvprgsentvtgphirgsrlrasavgdeevdlllpgtarlqiqqgvnmparaelipgredkekqilhdccDVVLY 759
Cdd:cd17311 245 ---------------------------------------------------------------------------DVVYF 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1063710527 760 LGIIDILQEYNMTKKIEHAYKSL-HFDSLSISAVDPTFYSQRFLEFI 805
Cdd:cd17311 250 MGLIDILTQYDAKKKAAHAAKTVkHGAGAEISTVHPEQYAKRFLDFI 296
|
|
| PIPKc_PIP5K2A |
cd17309 |
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ... |
445-805 |
1.54e-36 |
|
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: 140.11 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 445 PHHsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDTLRElSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLP 524
Cdd:cd17309 59 PSH---FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLAN-DSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 525 DYHHH-VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFFTDLRIHRRFDLKGSSLGRSA-DKVEIDENTILKDLDL- 601
Cdd:cd17309 135 KYHQYiVECHGNTLLPQFLGMYRLT-VDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREAsDKEKAKELPTLKDNDFi 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 602 --NYSFFLETSWREGLLRQLEIDSKFLEAQNIMDYSLLLGVHhrapqhlrsqlvrsqsittdalesvaeddtieddmlsy 679
Cdd:cd17309 214 ndGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIH-------------------------------------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 680 heglvlvprgsentvtgphirgsrlrasavgdeevdlllpgtarlqiqqgvnmparaelipgredkekqilhdccDVVLY 759
Cdd:cd17309 256 ---------------------------------------------------------------------------DVVYF 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1063710527 760 LGIIDILQEYNMTKKIEHAYKSL-HFDSLSISAVDPTFYSQRFLEFI 805
Cdd:cd17309 261 MAIIDILTHYDAKKKAAHAAKTVkHGAGAEISTVNPEQYSKRFLDFI 307
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
58-240 |
4.47e-36 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 137.39 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 58 YSGSLLGNVPEGPGKYIWSDGCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYVDANKLTYKGRWRLNLKH 137
Cdd:COG4642 58 GGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 138 GLGYQVYPNGDVFEGSWIQGLGEGPGKYTWANKNVYLGDMKGGKMSGKGTLTWVTGDSYEGSWLNGMMHGVGVYTWSDGG 217
Cdd:COG4642 138 GGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGD 217
|
170 180
....*....|....*....|....
gi 1063710527 218 CYVGTWTRGLKDGKGSFYSA-GTR 240
Cdd:COG4642 218 RYEGEFKNGKRHGQGTLTYAdGDR 241
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
69-237 |
2.99e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 67.67 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 69 GPGKYIWSDGCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYVDANKLTYKGRWRLNLKHGLGYQVYPNGD 148
Cdd:COG4642 11 GGGDATALGGGGEGGLAAAGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 149 VFEGSWIQGLGEGpgkytwanknvYLGDMKGGKMSGKGTLTWVTGDSYEGSWLNGMMHGVGVYTWSDGGCYVGTWTRGLK 228
Cdd:COG4642 91 GGGGEGGFGGGGG-----------GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKP 159
|
....*....
gi 1063710527 229 DGKGSFYSA 237
Cdd:COG4642 160 HGQGTLTYA 168
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
196-217 |
2.93e-06 |
|
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: 44.32 E-value: 2.93e-06
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
194-215 |
4.88e-06 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 43.48 E-value: 4.88e-06
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
79-99 |
3.39e-05 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 41.17 E-value: 3.39e-05
|
| YwqK |
COG2849 |
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms]; |
101-185 |
7.37e-04 |
|
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
Pssm-ID: 442097 [Multi-domain] Cd Length: 163 Bit Score: 41.21 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 101 GASYDGEFSGGYMHGSGTYVDAN-KLTYKGRWRLNLKHGLGYQVYPNGDV-FEGSWIQGLGEGPGKYTWANKNV-YLGDM 177
Cdd:COG2849 54 KLGKGLGKYKKGKLGEWKTYYPNgQLKSEGTYKNGKLEGEWKEYYENGKLkSEGNYKNGKLHGEWKEYYENGKLkEEGNY 133
|
....*...
gi 1063710527 178 KGGKMSGK 185
Cdd:COG2849 134 KNGKKDGV 141
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
81-101 |
7.73e-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: 7.73e-04
|
| YwqK |
COG2849 |
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms]; |
54-151 |
2.86e-03 |
|
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
Pssm-ID: 442097 [Multi-domain] Cd Length: 163 Bit Score: 39.28 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710527 54 DGESYSGSLLGNVPEGPGKYIWSDGCVYD-GEWRRGMRHGIGNMRWASGA-SYDGEFSGGYMHGSGTYVDAN-KLTYKGR 130
Cdd:COG2849 53 KKLGKGLGKYKKGKLGEWKTYYPNGQLKSeGTYKNGKLEGEWKEYYENGKlKSEGNYKNGKLHGEWKEYYENgKLKEEGN 132
|
90 100
....*....|....*....|.
gi 1063710527 131 WRLNLKHGLGYQVYPNGDVFE 151
Cdd:COG2849 133 YKNGKKDGVWKYYDENGKLVK 153
|
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|