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Conserved domains on  [gi|154345468|ref|XP_001568671|]
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phosphatidylinositol-4-phosphate 5-kinase-like protein [Leishmania braziliensis MHOM/BR/75/M2904]

Protein Classification

1-phosphatidylinositol-4-phosphate 5-kinase family protein( domain architecture ID 10065413)

1-phosphatidylinositol-4-phosphate 5-kinase family protein may phosphorylate phosphatidylinositol-4-phosphate to produce phosphatidylinositol-4,5-bisphosphate as a precursor of two second messengers, inositol-1,4,5-triphosphate and diacylglycerol

CATH:  3.30.800.10
EC:  2.7.1.-
Gene Ontology:  GO:0016307|GO:0016310|GO:0005524
PubMed:  9838059
SCOP:  4002087

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
81-443 4.75e-75

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: 235.54  E-value: 4.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  81 VKVHVTEYAPNVFSFLRQLEGVADSHFADEWSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYM 160
Cdd:cd00139    1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 161 QHIAAHPGSLLMRFYMLLKVSV-RKEKGYILCFNDIFAAASVLHEKWDIKGRipkpgkslrnpdflrrgselnlhlieaq 239
Cdd:cd00139   81 EHIKKNPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGS---------------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 240 kkrngivkpvtdaseqLYNREdgvVVKEAKGAQSPPTLHDKDLTRLFL---LPQNTRKRLLEQLLRDYDFLNSAGMMDYS 316
Cdd:cd00139  133 ----------------TVGRR---VSKEKEKKKGLKVLKDLDFLEKGEkiiLGPEDRAELLEQLEKDVEFLRSLNIMDYS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 317 LLIGVTYHenkapqsgrhcisdrmsnsaqhdaasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYY 396
Cdd:cd00139  194 LLVGIHRL---------------------------------------------------------------------VYY 204
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 154345468 397 VGIIDVLTAYTIKKKGANFFKSFLWEQNM-LSTIPPDYYARRLTSFTE 443
Cdd:cd00139  205 LGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFME 252
 
Name Accession Description Interval E-value
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
81-443 4.75e-75

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: 235.54  E-value: 4.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  81 VKVHVTEYAPNVFSFLRQLEGVADSHFADEWSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYM 160
Cdd:cd00139    1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 161 QHIAAHPGSLLMRFYMLLKVSV-RKEKGYILCFNDIFAAASVLHEKWDIKGRipkpgkslrnpdflrrgselnlhlieaq 239
Cdd:cd00139   81 EHIKKNPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGS---------------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 240 kkrngivkpvtdaseqLYNREdgvVVKEAKGAQSPPTLHDKDLTRLFL---LPQNTRKRLLEQLLRDYDFLNSAGMMDYS 316
Cdd:cd00139  133 ----------------TVGRR---VSKEKEKKKGLKVLKDLDFLEKGEkiiLGPEDRAELLEQLEKDVEFLRSLNIMDYS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 317 LLIGVTYHenkapqsgrhcisdrmsnsaqhdaasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYY 396
Cdd:cd00139  194 LLVGIHRL---------------------------------------------------------------------VYY 204
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 154345468 397 VGIIDVLTAYTIKKKGANFFKSFLWEQNM-LSTIPPDYYARRLTSFTE 443
Cdd:cd00139  205 LGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFME 252
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
112-445 2.03e-57

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: 188.83  E-value: 2.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  112 SLPEDCLRmELG-EGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHPGSLLMRFYMLLKVSVRKEKGYIL 190
Cdd:pfam01504   1 LTGKSILS-ELSsPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  191 CFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgselnlhlieaqkkrngivkpvtdaseQLYNREdgvVVKEAKG 270
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKG--------------------------------------------STVGRT---AKKKERE 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  271 AQSPPTLHDKDLTR---LFLLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIGVtyhenkapqsgrhcisdrmsnsaqHD 347
Cdd:pfam01504 113 KDEPTTLKDLDFLErklKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGI------------------------HD 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  348 aasasswaevrpaplakdshlsdkktshsvtppefangvRSVCEQEIYYVGIIDVLTAYTIKKKGANFFKSFLWEQNMLS 427
Cdd:pfam01504 169 ---------------------------------------LDEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSIS 209
                         330
                  ....*....|....*...
gi 154345468  428 TIPPDYYARRLTSFTELI 445
Cdd:pfam01504 210 AVPPKEYAERFLKFIEKI 227
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
85-446 3.69e-42

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 152.54  E-value: 3.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468    85 VTEYAPNVFSFLRQLEGVADSHFADewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA 164
Cdd:smart00330  32 FKDYCPEVFRNLRELFGIDPADYLR--SLCRSPPLELSSGGKSGSFFYLSLDDRFIIKTVSKSEIKSLLPMLPNYYEHIV 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468   165 AHPGSLLMRFYMLLKVSVRKE---KGYILCFNDIFAAASVLHEKWDIKGripkpgkSLRNpdflrRgselnlhliEAQKK 241
Cdd:smart00330 110 QNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG-------STRG-----R---------EADKK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468   242 RngivkpvtdaseqlynredgvvvkeakgAQSPPTLHDKDLTR-----LFLLPqNTRKRLLEQLLRDYDFLNSAGMMDYS 316
Cdd:smart00330 169 K----------------------------VKELPVLKDLDLVEmwnqpIYVDP-LAKKALLKQIKRDCEFLESLKIMDYS 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468   317 LLIGVTYhENKAPQSGRHCISDRMSNSAQHDAASASSWAEVRPAPLAKDShlsdkkTSHSVTPPEFANGVRSVCEQEIYY 396
Cdd:smart00330 220 LLVGIHD-IERGQREEIELPPVYGSDESPSSESSNGGKAPDITGNLLVSN------SPDGDGPFGGIPARAIRARRVVLY 292
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 154345468   397 VGIIDVLTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSFTELIF 446
Cdd:smart00330 293 LGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
72-447 4.25e-21

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 96.44  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  72 PSTDSKGKrvkvhvtEYAPNVFSFLRQLEGVaDShfADEW-SL-PEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEV 149
Cdd:PLN03185 400 QSEDFKWK-------DYCPMVFRNLREMFKI-DA--ADYMmSIcGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEV 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 150 RVLLDILHAYMQHIAAHPGSLLMRFYMLLKVSVRK-EKGYILCFNDIFAAASVLHEKWDIKGRipKPGKSlrnpdflrrg 228
Cdd:PLN03185 470 KVLLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSgQKFRFVVMGNMFCTELRIHRRFDLKGS--SLGRS---------- 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 229 selnlhlieaqkkrngivkpvtdaseqlynrEDGVVVKEAKgaqsppTLHDKDLTRLFLLPQNTRKRLLEQLLRDYDFLN 308
Cdd:PLN03185 538 -------------------------------ADKVEIDENT------TLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLE 580
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 309 SAGMMDYSLLIGVTYhenKAPQ-------SGRHCISDRMSNSAQHDAASASSWA---------------------EVRPA 360
Cdd:PLN03185 581 AQRIMDYSLLLGVHF---RAPQhlrsllpYSRSITADGLEVVAEEDTIEDEELSypeglvlvprgaddgstvpgpHIRGS 657
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 361 PLaKDSHLSDK------------KTSHSVTPPEFANGV--RSVCEQEIY--------YVGIIDVLTAYTIKKKGANFFKS 418
Cdd:PLN03185 658 RL-RASAAGDEevdlllpgtarlQIQLGVNMPARAERIpgREDKEKQSFhevydvvlYLGIIDILQEYNMSKKIEHAYKS 736
                        410       420
                 ....*....|....*....|....*....
gi 154345468 419 FLWEQNMLSTIPPDYYARRLTSFTELIFP 447
Cdd:PLN03185 737 LQFDSLSISAVDPTFYSKRFLEFIQKVFP 765
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
88-453 2.97e-17

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 84.23  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVaDSHFAdewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHP 167
Cdd:COG5253  341 YFPEVFRELRALCGC-DEALV---SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNP 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 168 GSLLMRFYMLLKVSVRKE-------KGYILCFNDIFAAASVlHEKWDIKgripkpgkslrnpdflrrGSELNLHLIEAQK 240
Cdd:COG5253  417 LTLLCKIFGFYRVKSRSSisssksrKIYFIVMENLFYPHGI-HRIFDLK------------------GSMRNRHVERTGK 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 241 KRNgivkPVTDASEQLYNREDGVVVKEAKgaqspptlhdkdltrlfllpqntRKRLLEQLLRDYDFLNSAGMMDYSLLIG 320
Cdd:COG5253  478 SMS----VLLDMNDVEWIRESPKIVFGLK-----------------------KKLLLSQVWNDVLFLSKLNIMDYSLLVG 530
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 321 VtyhenkapqsgrhcisdrmsnsaqHDAASASSwaevrpAPLAKDSHlsdkktsHSVTPPEFangvrsvceqeIYYVGII 400
Cdd:COG5253  531 I------------------------DDEREEAS------VGLIIDFI-------RTRMTGDK-----------KLESGIK 562
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 154345468 401 DVLTAYTIKKKganffksflweqNMLSTIPPDYYARRLTSFTE---LIFPDASEES 453
Cdd:COG5253  563 DKLTVGSFTKR------------KEPTAVTPRQYKNRFRKAMEayiDPFPDKKTQE 606
 
Name Accession Description Interval E-value
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
81-443 4.75e-75

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: 235.54  E-value: 4.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  81 VKVHVTEYAPNVFSFLRQLEGVADSHFADEWSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYM 160
Cdd:cd00139    1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 161 QHIAAHPGSLLMRFYMLLKVSV-RKEKGYILCFNDIFAAASVLHEKWDIKGRipkpgkslrnpdflrrgselnlhlieaq 239
Cdd:cd00139   81 EHIKKNPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGS---------------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 240 kkrngivkpvtdaseqLYNREdgvVVKEAKGAQSPPTLHDKDLTRLFL---LPQNTRKRLLEQLLRDYDFLNSAGMMDYS 316
Cdd:cd00139  133 ----------------TVGRR---VSKEKEKKKGLKVLKDLDFLEKGEkiiLGPEDRAELLEQLEKDVEFLRSLNIMDYS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 317 LLIGVTYHenkapqsgrhcisdrmsnsaqhdaasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYY 396
Cdd:cd00139  194 LLVGIHRL---------------------------------------------------------------------VYY 204
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 154345468 397 VGIIDVLTAYTIKKKGANFFKSFLWEQNM-LSTIPPDYYARRLTSFTE 443
Cdd:cd00139  205 LGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFME 252
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
112-445 2.03e-57

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: 188.83  E-value: 2.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  112 SLPEDCLRmELG-EGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHPGSLLMRFYMLLKVSVRKEKGYIL 190
Cdd:pfam01504   1 LTGKSILS-ELSsPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  191 CFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgselnlhlieaqkkrngivkpvtdaseQLYNREdgvVVKEAKG 270
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKG--------------------------------------------STVGRT---AKKKERE 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  271 AQSPPTLHDKDLTR---LFLLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIGVtyhenkapqsgrhcisdrmsnsaqHD 347
Cdd:pfam01504 113 KDEPTTLKDLDFLErklKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGI------------------------HD 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  348 aasasswaevrpaplakdshlsdkktshsvtppefangvRSVCEQEIYYVGIIDVLTAYTIKKKGANFFKSFLWEQNMLS 427
Cdd:pfam01504 169 ---------------------------------------LDEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSIS 209
                         330
                  ....*....|....*...
gi 154345468  428 TIPPDYYARRLTSFTELI 445
Cdd:pfam01504 210 AVPPKEYAERFLKFIEKI 227
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
85-446 3.69e-42

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 152.54  E-value: 3.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468    85 VTEYAPNVFSFLRQLEGVADSHFADewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA 164
Cdd:smart00330  32 FKDYCPEVFRNLRELFGIDPADYLR--SLCRSPPLELSSGGKSGSFFYLSLDDRFIIKTVSKSEIKSLLPMLPNYYEHIV 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468   165 AHPGSLLMRFYMLLKVSVRKE---KGYILCFNDIFAAASVLHEKWDIKGripkpgkSLRNpdflrRgselnlhliEAQKK 241
Cdd:smart00330 110 QNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG-------STRG-----R---------EADKK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468   242 RngivkpvtdaseqlynredgvvvkeakgAQSPPTLHDKDLTR-----LFLLPqNTRKRLLEQLLRDYDFLNSAGMMDYS 316
Cdd:smart00330 169 K----------------------------VKELPVLKDLDLVEmwnqpIYVDP-LAKKALLKQIKRDCEFLESLKIMDYS 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468   317 LLIGVTYhENKAPQSGRHCISDRMSNSAQHDAASASSWAEVRPAPLAKDShlsdkkTSHSVTPPEFANGVRSVCEQEIYY 396
Cdd:smart00330 220 LLVGIHD-IERGQREEIELPPVYGSDESPSSESSNGGKAPDITGNLLVSN------SPDGDGPFGGIPARAIRARRVVLY 292
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 154345468   397 VGIIDVLTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSFTELIF 446
Cdd:smart00330 293 LGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
87-443 8.85e-38

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: 140.12  E-value: 8.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  87 EYAPNVFSFLRQLEGV-ADSHFAdewSLPEDCLRMELG-EGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA 164
Cdd:cd17303   58 DYAPWVFRFLRELFGIdPADYLM---SLTGKYILSELGsPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 165 AHPGSLLMRFYMLLKVSVRK-EKGYILCFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgselnlhlieaqkkrn 243
Cdd:cd17303  135 ENPNTLLSQFYGLHRVKMPRgRKIHFVVMNNLFPPHRDIHQTFDLKG--------------------------------- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 244 givkpvtdaseQLYNREdgvvVKEAKGAQSP-PTLHDKDLTR----LFLLPQNtRKRLLEQLLRDYDFLNSAGMMDYSLL 318
Cdd:cd17303  182 -----------STVGRE----TPEDKLAKGPrATLKDLNWLRrkrkLALGPEK-RKQFLTQLKRDVEFLASLNIMDYSLL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 319 IGVtyhenkapqsgrhcisdrmsnsaqHDAASasswaevrpaplakdshlsdkktshsvtppefanGVRSVCEQ-----E 393
Cdd:cd17303  246 VGI------------------------HDLDG----------------------------------GFQATDENnepgdE 267
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 154345468 394 IYYVGIIDVLTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSFTE 443
Cdd:cd17303  268 IYYLGIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIE 317
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
72-441 4.73e-27

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: 110.46  E-value: 4.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  72 PSTDSKGKrvkvhvtEYAPNVFSFLRQLEGVADSHFAdeWSL-PEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVR 150
Cdd:cd17302   53 QSSDFKWK-------DYCPMVFRNLRELFGIDAADYM--LSLcGDDALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 151 VLLDILHAYMQHIAAHPGSLLMRFYMLLKV-SVRKEKGYILCFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgs 229
Cdd:cd17302  124 VLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGNLFCTELRIHRRFDLKG------------------- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 230 elnlhlieaqkkrngivkpvtdaSEQlyNREDGvvvKEAKGAQSPPTLHDKDLTRLFLLPQNTRKRLLEQLLRDYDFLNS 309
Cdd:cd17302  185 -----------------------STH--GRTTG---KPESEIDPNTTLKDLDLDFKFRLEKGWRDALMRQIDADCAFLEA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 310 AGMMDYSLLIGVtyhenkapqsgrhcisdrmsnsaqHDAASASSwAEVRPAplakdshlsdkktshsvtppefangvrsv 389
Cdd:cd17302  237 LRIMDYSLLLGV------------------------HFRAGDST-GEPYDV----------------------------- 262
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154345468 390 ceqeIYYVGIIDVLTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSF 441
Cdd:cd17302  263 ----VLYFGIIDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDF 310
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
85-441 9.16e-27

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: 109.28  E-value: 9.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  85 VTEYAPNVFSFLRQLEGVADSHFADewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA 164
Cdd:cd17305   55 VKEYCPLVFRNLRERFGIDDDDYLN--SLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 165 AHPG-SLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGRIpkpgkslrnpdFLRRGSElnlhlieaqkkrn 243
Cdd:cd17305  133 ERHGkTLLPQYLGMYRITVNGVETYLVVMRNVFSPRLPIHKKYDLKGST-----------VDRQASD------------- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 244 givkpvtdaseqlynredgvvvKEAkgAQSPPTLHD----KDLTRLFLLpQNTRKRLLEQLLRDYDFLNSAGMMDYSLLI 319
Cdd:cd17305  189 ----------------------KEK--AKDLPTLKDndflNDGTKIYIG-DEAKAKLLETLKRDVEFLAKLNLMDYSLLV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 320 GVtyhenkapqsgrhcisdrmsnsaqHDAasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYYVGI 399
Cdd:cd17305  244 GI------------------------HDC---------------------------------------------IYFMAI 254
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 154345468 400 IDVLTAYTIKKKGANFFKSFLW-EQNMLSTIPPDYYARRLTSF 441
Cdd:cd17305  255 IDILTHYGAKKRAAHAAKTVKHgAGAEISTVKPEQYAKRFLEF 297
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
88-443 1.38e-26

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: 109.37  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVADSHFADEWSlPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHP 167
Cdd:cd17304   54 YAGPVFATLRQSLGISEKEYQNSLS-PDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 168 GSLLMRFYMLLKVSV-RKEKGYILCFNDIFAAASVLHEKWDIKG----RIPKPgkslrNPDflrrGSELnlhlieaqkkr 242
Cdd:cd17304  133 HSLLVKFLGVHSIKLpGKKKKYFIVMQSVFYPDERINERYDIKGcqvsRYTDP-----EPE----GSQI----------- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 243 ngivkpvtdaseqlynredgVVVkeakgaqspptLHDKDLTRLFLLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIGVT 322
Cdd:cd17304  193 --------------------IVV-----------LKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLLVGFQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 323 yhenkapqsgrhcisdrmsnsaqhdaasasswaevrpaPLAKDSH---LSDKKTS-HSVTPPEFAngvrsvceqeiYYVG 398
Cdd:cd17304  242 --------------------------------------PLHSDENrrlLPNYKNAlHVVDGPEYR-----------YFVG 272
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 154345468 399 IIDVLTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSFTE 443
Cdd:cd17304  273 IIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVE 317
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
72-447 4.25e-21

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 96.44  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  72 PSTDSKGKrvkvhvtEYAPNVFSFLRQLEGVaDShfADEW-SL-PEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEV 149
Cdd:PLN03185 400 QSEDFKWK-------DYCPMVFRNLREMFKI-DA--ADYMmSIcGNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEV 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 150 RVLLDILHAYMQHIAAHPGSLLMRFYMLLKVSVRK-EKGYILCFNDIFAAASVLHEKWDIKGRipKPGKSlrnpdflrrg 228
Cdd:PLN03185 470 KVLLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSgQKFRFVVMGNMFCTELRIHRRFDLKGS--SLGRS---------- 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 229 selnlhlieaqkkrngivkpvtdaseqlynrEDGVVVKEAKgaqsppTLHDKDLTRLFLLPQNTRKRLLEQLLRDYDFLN 308
Cdd:PLN03185 538 -------------------------------ADKVEIDENT------TLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLE 580
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 309 SAGMMDYSLLIGVTYhenKAPQ-------SGRHCISDRMSNSAQHDAASASSWA---------------------EVRPA 360
Cdd:PLN03185 581 AQRIMDYSLLLGVHF---RAPQhlrsllpYSRSITADGLEVVAEEDTIEDEELSypeglvlvprgaddgstvpgpHIRGS 657
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 361 PLaKDSHLSDK------------KTSHSVTPPEFANGV--RSVCEQEIY--------YVGIIDVLTAYTIKKKGANFFKS 418
Cdd:PLN03185 658 RL-RASAAGDEevdlllpgtarlQIQLGVNMPARAERIpgREDKEKQSFhevydvvlYLGIIDILQEYNMSKKIEHAYKS 736
                        410       420
                 ....*....|....*....|....*....
gi 154345468 419 FLWEQNMLSTIPPDYYARRLTSFTELIFP 447
Cdd:PLN03185 737 LQFDSLSISAVDPTFYSKRFLEFIQKVFP 765
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
88-441 1.26e-18

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: 86.53  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVADSHFAdeWSLPEDCLRmELGE-GRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAH 166
Cdd:cd17301   60 YAPVAFRYFRELFGIKPDDYL--LSLCNEPLR-ELSNpGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 167 PGSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGRIPKpgkslrnpdflRRGSELnlhliEAQKKRngiv 246
Cdd:cd17301  137 PRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYK-----------RKASKK-----ERQKKS---- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 247 kpvtdaseqlynredgvvvkeakgaqspPTLHDKDLTRLF----LLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIGVt 322
Cdd:cd17301  197 ----------------------------PTLKDLDFMEDHpegiLLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGV- 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 323 YHENKAPqsgrhcisdrmsnsaqhdaasasswaevrpaplAKDShlsdkktshsvtppefaNGvrsvcEQEIYYVGIIDV 402
Cdd:cd17301  248 HNLGGIP---------------------------------ARNS-----------------KG-----ERLLLFIGIIDI 272
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 154345468 403 LTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSF 441
Cdd:cd17301  273 LQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNF 311
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
87-441 1.24e-17

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: 83.18  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  87 EYAPNVFSFLRQLEGVADSHFADewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA-A 165
Cdd:cd17310   68 EYCPMVFRNLRERFGIDDQDYQN--SVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVeC 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 166 HPGSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgselnlhlieaqkkrngi 245
Cdd:cd17310  146 HGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKG----------------------------------- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 246 vkpvtdaseqlynredGVVVKEAKG---AQSPPTLHDKDL----TRLFLLPQNtRKRLLEQLLRDYDFLNSAGMMDYSLL 318
Cdd:cd17310  191 ----------------STVSREASDkekAKDLPTFKDNDFlnegQKLHVGEES-KKNFLEKLKRDVEFLAQLKIMDYSLL 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 319 IGVtyhenkapqsgrhcisdrmsnsaqHDAasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYYVG 398
Cdd:cd17310  254 VGI------------------------HDV---------------------------------------------VYFMA 264
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 154345468 399 IIDVLTAYTIKKKGANFFKSFLWEQNM-LSTIPPDYYARRLTSF 441
Cdd:cd17310  265 IIDILTPYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFNEF 308
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
88-453 2.97e-17

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 84.23  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVaDSHFAdewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHP 167
Cdd:COG5253  341 YFPEVFRELRALCGC-DEALV---SLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHVLFNP 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 168 GSLLMRFYMLLKVSVRKE-------KGYILCFNDIFAAASVlHEKWDIKgripkpgkslrnpdflrrGSELNLHLIEAQK 240
Cdd:COG5253  417 LTLLCKIFGFYRVKSRSSisssksrKIYFIVMENLFYPHGI-HRIFDLK------------------GSMRNRHVERTGK 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 241 KRNgivkPVTDASEQLYNREDGVVVKEAKgaqspptlhdkdltrlfllpqntRKRLLEQLLRDYDFLNSAGMMDYSLLIG 320
Cdd:COG5253  478 SMS----VLLDMNDVEWIRESPKIVFGLK-----------------------KKLLLSQVWNDVLFLSKLNIMDYSLLVG 530
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 321 VtyhenkapqsgrhcisdrmsnsaqHDAASASSwaevrpAPLAKDSHlsdkktsHSVTPPEFangvrsvceqeIYYVGII 400
Cdd:COG5253  531 I------------------------DDEREEAS------VGLIIDFI-------RTRMTGDK-----------KLESGIK 562
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 154345468 401 DVLTAYTIKKKganffksflweqNMLSTIPPDYYARRLTSFTE---LIFPDASEES 453
Cdd:COG5253  563 DKLTVGSFTKR------------KEPTAVTPRQYKNRFRKAMEayiDPFPDKKTQE 606
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
87-441 6.41e-17

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (PIP5K2C) and similar proteins; PIP5K2C (EC 2.7.1.149), also known as 1-phosphatidylinositol 5-phosphate 4-kinase 2-gamma, or PI5P4Kgamma, or diphosphoinositide kinase 2-gamma, or phosphatidylinositol 5-phosphate 4-kinase type II gamma, or PI(5)P 4-kinase type II gamma, or PIP4KII-gamma, or PIP4K2C, may play an important role in the production of phosphatidylinositol bisphosphate (PIP2) in the endoplasmic reticulum. It contributes to the development and maintenance of epithelial cell functional polarity. It also plays a role in the regulation of the immune system via mTORC1 signaling. Moreover, PIP5K2C is involved in arsenic trioxide (ATO) cytotoxicity. It mediates PIP2 generation required for positioning and assembly of bipolar spindles and alteration of PIP5K2C function by ATO may thus lead to spindle abnormalities.


Pssm-ID: 340448  Cd Length: 298  Bit Score: 81.07  E-value: 6.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  87 EYAPNVFSFLRQLEGVADSHFADEWSLPEDCLRMELGEGRsqafFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA-A 165
Cdd:cd17311   57 EYCPQVFRNLRERFGIDDQDYQVSLTRSPPYSESEGSDGR----FLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVkC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 166 HPGSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgselnlhlieaqkkrngi 245
Cdd:cd17311  133 HGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKG----------------------------------- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 246 vkpvtdaseQLYNRE--DGVVVKEAkgaqspPTLHDKDL---TRLFLLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIG 320
Cdd:cd17311  178 ---------SLVSREasDKEKVKEL------PTLKDMDFlnkNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 321 VtyhenkapqsgrhcisdrmsnsaqHDAasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYYVGII 400
Cdd:cd17311  243 I------------------------HDV---------------------------------------------VYFMGLI 253
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 154345468 401 DVLTAYTIKKKGANFFKSFLWEQNM-LSTIPPDYYARRLTSF 441
Cdd:cd17311  254 DILTQYDAKKKAAHAAKTVKHGAGAeISTVHPEQYAKRFLDF 295
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
87-441 2.48e-16

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: 79.64  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  87 EYAPNVFSFLRQLEGVADSHFADewSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIA-A 165
Cdd:cd17309   66 EYCPMVFRNLRERFGIDDQDFQN--SLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVeC 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 166 HPGSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGripkpgkslrnpdflrrgselnlhlieaqkkrngi 245
Cdd:cd17309  144 HGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKG----------------------------------- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 246 vkpvtdaseqlynredGVVVKEA---KGAQSPPTLHDKDLT---RLFLLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLI 319
Cdd:cd17309  189 ----------------STVAREAsdkEKAKELPTLKDNDFIndgQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLV 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 320 GVtyhenkapqsgrhcisdrmsnsaqHDAasasswaevrpaplakdshlsdkktshsvtppefangvrsvceqeIYYVGI 399
Cdd:cd17309  253 GI------------------------HDV---------------------------------------------VYFMAI 263
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 154345468 400 IDVLTAYTIKKKGANFFKSFLWEQNM-LSTIPPDYYARRLTSF 441
Cdd:cd17309  264 IDILTHYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSKRFLDF 306
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
88-441 1.10e-13

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: 71.95  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVADSHFAdeWSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHP 167
Cdd:cd17306   63 YAPVAFRYFRELFGIRPDDYL--YSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 168 GSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGRIPKpgkslrnpdflRRGSelnlhlieaQKKRNgivK 247
Cdd:cd17306  141 RTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYK-----------RRAS---------QKERE---K 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 248 PVtdaseqlynredgvvvkeakgaqspPTLHD----KDLTRLFLLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIGVty 323
Cdd:cd17306  198 PL-------------------------PTYKDldflQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGI-- 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 324 HENKAPQSGRHCISDRMSNsaqhdaasasswaevrpaplakdshlsdkktshsvTPPEFANGvrsvcEQEIYYVGIIDVL 403
Cdd:cd17306  251 HNIDARRGGTIETDDQMGG-----------------------------------IPARNSKG-----ERLLLYIGIIDIL 290
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 154345468 404 TAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSF 441
Cdd:cd17306  291 QSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRF 328
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
88-450 2.51e-13

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: 70.79  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVADSHFAdeWSLPEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAHP 167
Cdd:cd17308   61 YAPVAFRYFRELFGIRPDDYL--YSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 168 GSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGRIPKpgkslrnpdflRRGSELnlhliEAQKKRngivk 247
Cdd:cd17308  139 RTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYK-----------RRASKK-----EREKSK----- 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 248 pvtdaseqlynredgvvvkeakgaqspPTLHDKDLTRLF----LLPQNTRKRLLEQLLRDYDFLNSAGMMDYSLLIGVty 323
Cdd:cd17308  198 ---------------------------PTFKDLDFMQDMpeglMLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGV-- 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 324 henkapqsgrhcisdrmsnsaqHDAASAsswaevrPAplakdshlsdkktshsvtppefangVRSVCEQEIYYVGIIDVL 403
Cdd:cd17308  249 ----------------------HNIGGI-------PA-------------------------VNGKGERLLLYIGIIDIL 274
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 154345468 404 TAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSF-TELIFPDAS 450
Cdd:cd17308  275 QSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFmSNTVFRKSS 322
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
88-441 6.13e-13

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: 69.63  E-value: 6.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  88 YAPNVFSFLRQLEGVADSHFAdeWSLPEDCLrMELGE-GRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYMQHIAAH 166
Cdd:cd17307   60 YAPLAFRYFRELFGIKPDDYL--YSICSEPL-IELSNpGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 167 PGSLLMRFYMLLKVSVRKEKGYILCFNDIFAAASVLHEKWDIKGRIPKpgkslrnpdflRRGSelnlhlieaQKKRNgiv 246
Cdd:cd17307  137 PRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYK-----------RRAS---------RKERE--- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 247 kpvtdaseqlynredgvvvkeakgaQSPPTLHDKDLTR-----LFLLPQnTRKRLLEQLLRDYDFLNSAGMMDYSLLIGV 321
Cdd:cd17307  194 -------------------------KSCPTYKDLDFLQdmhdgLYFDPE-TYNALMKTLQRDCRVLESFKIMDYSLLLGI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 322 tyhenkapqsgrHCISDrmsnsaqhdaasasswaevRPAPLAKDshlsdkktshsvtppefangvrsvcEQEIYYVGIID 401
Cdd:cd17307  248 ------------HVLGG-------------------IPAKNHKG-------------------------EKLLLFMGIID 271
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 154345468 402 VLTAYTIKKKGANFFKSFLWEQNMLSTIPPDYYARRLTSF 441
Cdd:cd17307  272 ILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKF 311
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
81-327 4.11e-12

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: 66.00  E-value: 4.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468  81 VKVHVTEYAPNVFSFLRQLEGVADSHFADewSLpEDCLRMELGEGRSQAFFLKSKTMAFMCKTISVEEVRVLLDILHAYM 160
Cdd:cd17300    1 TKFTCTIYFAEQFHALRSLYCGGEDDFIR--SL-SRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 161 QHIAAHP----GSLLMRFYMLLKVSVR------KEKGYILCFNDIFAAASVLHeKWDIKGripkpgkSLRNpdflrrgse 230
Cdd:cd17300   78 EYMAKALfhkrPSLLAKILGVYRISVKnsttnkTSKQDLLVMENLFYGRNISQ-VYDLKG-------SLRN--------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154345468 231 lnlhlieaqkkRNGIVKPVTDAseqlynredgvvvkeakgaqsppTLHDKDL------TRLFLLPqNTRKRLLEQLLRDY 304
Cdd:cd17300  141 -----------RYVNVAEDEDS-----------------------VLLDENFleytkgSPLYLRE-HSKAVLMAAIWNDT 185
                        250       260
                 ....*....|....*....|...
gi 154345468 305 DFLNSAGMMDYSLLIGVtYHENK 327
Cdd:cd17300  186 LFLSSQNVMDYSLLVGI-DEEKK 207
 
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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