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Conserved domains on  [gi|1063710527|ref|NP_001327647|]
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phosphatidyl inositol monophosphate 5 kinase [Arabidopsis thaliana]

Protein Classification

MORN repeat-containing protein; serine/threonine-protein kinase( domain architecture ID 11477553)

MORN repeat-containing protein similar to plant -phosphatidylinositol-4-phosphate 5-kinases| serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

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
 
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
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
 
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
                          10        20
                  ....*....|....*....|..
gi 1063710527 196 YEGSWLNGMMHGVGVYTWSDGG 217
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGD 22
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
                           10        20
                   ....*....|....*....|..
gi 1063710527  194 DSYEGSWLNGMMHGVGVYTWSD 215
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
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
                           10        20
                   ....*....|....*....|.
gi 1063710527   79 CVYDGEWRRGMRHGIGNMRWA 99
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYA 21
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
                          10        20
                  ....*....|....*....|.
gi 1063710527  81 YDGEWRRGMRHGIGNMRWASG 101
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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