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Conserved domains on  [gi|226442759|ref|NP_001140159|]
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phosphatidylinositol 4-phosphate 5-kinase type-1 gamma isoform 2 [Mus musculus]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase type-1 gamma( domain architecture ID 13022717)

phosphatidylinositol 4-phosphate 5-kinase type-1 gamma catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
76-449 0e+00

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: 693.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  76 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDY 155
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 156 LYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 235
Cdd:cd17308   81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 236 VVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIM 315
Cdd:cd17308  161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 316 DYSLLLGVHNidqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtMGGIPAVNGRGERLLLHIG 395
Cdd:cd17308  241 DYSLLLGVHN---------------------------------------------------IGGIPAVNGKGERLLLYIG 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226442759 396 IIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFRKSSS 449
Cdd:cd17308  270 IIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKSSS 323
 
Name Accession Description Interval E-value
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
76-449 0e+00

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: 693.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  76 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDY 155
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 156 LYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 235
Cdd:cd17308   81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 236 VVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIM 315
Cdd:cd17308  161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 316 DYSLLLGVHNidqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtMGGIPAVNGRGERLLLHIG 395
Cdd:cd17308  241 DYSLLLGVHN---------------------------------------------------IGGIPAVNGKGERLLLYIG 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226442759 396 IIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFRKSSS 449
Cdd:cd17308  270 IIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKSSS 323
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
103-443 3.54e-155

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 450.29  E-value: 3.54e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   103 LMQDFYVVESIFFPSEGS-NLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTS 181
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   182 DDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGK---NIRVVVMNNVLPRVVKMHLKFDLKGST 258
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   259 YKRRASKKeKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGA 338
Cdd:smart00330 161 RGREADKK-KVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   339 QSKADEKRPVAQKALYSTamESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVH 418
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGH 317
                          330       340
                   ....*....|....*....|....*
gi 226442759   419 DGDTVSVHRPSFYAERFFKFMSSTV 443
Cdd:smart00330 318 DGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
158-442 2.56e-124

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: 366.79  E-value: 2.56e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  158 SLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVV 237
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  238 MNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPT-YKDLDFMQDMPEgLLLDSDTFGALVKTLQRDCLVLESFKIMD 316
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  317 YSLLLGVHNIDQqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmggipavngrGERLLLHIGI 396
Cdd:pfam01504 160 YSLLLGIHDLDE----------------------------------------------------------DGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 226442759  397 IDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSST 442
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
52-444 5.34e-77

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 260.54  E-value: 5.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  52 PGHGKKLGHRGVDasgettykkttsstLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHFQ 129
Cdd:PLN03185 337 PGETIIKGHRSYD--------------LMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWmnFPKAGSQLTPSHQSE 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 130 DFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-NEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMN 208
Cdd:PLN03185 403 DFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 209 LNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSlPTYKDLdfmqDMPEG 287
Cdd:PLN03185 483 VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN-TTLKDL----DLNYS 557
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 288 LLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKAL--------YSTAME 359
Cdd:PLN03185 558 FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITADGLEVVAEEDtiedeelsYPEGLV 637
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 360 SIQGGAA----------RGEAI--------ETDDTMGGIP------AVN--GRGER-----------------LLLHIGI 396
Cdd:PLN03185 638 LVPRGADdgstvpgphiRGSRLrasaagdeEVDLLLPGTArlqiqlGVNmpARAERipgredkekqsfhevydVVLYLGI 717
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 226442759 397 IDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMsSTVF 444
Cdd:PLN03185 718 IDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
130-445 2.12e-38

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 150.48  E-value: 2.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 130 DFRFKTYAPVAFRYFRELFGIrpDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNL 209
Cdd:COG5253  335 EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHV 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 210 NQNPRTLLPKFYGLYCVQ-------SGGKNIRVVVMNNVLPRvVKMHLKFDLKGSTYKRRASKKEKEKS-LPTYKDLDFM 281
Cdd:COG5253  413 LFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYP-HGIHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWI 491
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 282 QdmpEGLLLDSDTFGALVKT-LQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkaLYSTAMES 360
Cdd:COG5253  492 R---ESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDDE--------------------------REEASVGL 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 361 IQggaargEAIETDDTMGGIpavngrgerllLHIGIIDILQSYRFIKKLEhtwkalvhdgdtVSVHRPSFYAERFFKFMS 440
Cdd:COG5253  543 II------DFIRTRMTGDKK-----------LESGIKDKLTVGSFTKRKE------------PTAVTPRQYKNRFRKAME 593

                 ....*
gi 226442759 441 STVFR 445
Cdd:COG5253  594 AYIDP 598
 
Name Accession Description Interval E-value
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
76-449 0e+00

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: 693.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  76 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDY 155
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 156 LYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 235
Cdd:cd17308   81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 236 VVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIM 315
Cdd:cd17308  161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 316 DYSLLLGVHNidqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtMGGIPAVNGRGERLLLHIG 395
Cdd:cd17308  241 DYSLLLGVHN---------------------------------------------------IGGIPAVNGKGERLLLYIG 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226442759 396 IIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFRKSSS 449
Cdd:cd17308  270 IIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKSSS 323
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
79-445 0e+00

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: 682.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  79 LKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYS 158
Cdd:cd17301    3 LMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 159 LCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVM 238
Cdd:cd17301   83 LCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVVM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 239 NNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYS 318
Cdd:cd17301  163 NNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDYS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 319 LLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGERLLLHIGIID 398
Cdd:cd17301  243 LLLGVHNL---------------------------------------------------GGIPARNSKGERLLLFIGIID 271
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 226442759 399 ILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFR 445
Cdd:cd17301  272 ILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFK 318
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
79-445 0e+00

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: 633.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  79 LKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYS 158
Cdd:cd17307    3 IKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 159 LCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVM 238
Cdd:cd17307   83 ICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 239 NNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYS 318
Cdd:cd17307  163 NNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDYS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 319 LLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGERLLLHIGIID 398
Cdd:cd17307  243 LLLGIHVL---------------------------------------------------GGIPAKNHKGEKLLLFMGIID 271
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 226442759 399 ILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFR 445
Cdd:cd17307  272 ILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFK 318
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
79-445 0e+00

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: 620.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  79 LKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYS 158
Cdd:cd17306    6 LKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 159 LCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVM 238
Cdd:cd17306   86 LCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 239 NNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYS 318
Cdd:cd17306  166 NNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYS 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 319 LLLGVHNIDqqererqaegaqskadekrpvaqkalystamesiqggAARGEAIETDDTMGGIPAVNGRGERLLLHIGIID 398
Cdd:cd17306  246 LLVGIHNID-------------------------------------ARRGGTIETDDQMGGIPARNSKGERLLLYIGIID 288
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 226442759 399 ILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFR 445
Cdd:cd17306  289 ILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFK 335
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
103-443 3.54e-155

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 450.29  E-value: 3.54e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   103 LMQDFYVVESIFFPSEGS-NLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTS 181
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   182 DDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGK---NIRVVVMNNVLPRVVKMHLKFDLKGST 258
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   259 YKRRASKKeKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGA 338
Cdd:smart00330 161 RGREADKK-KVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759   339 QSKADEKRPVAQKALYSTamESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVH 418
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGH 317
                          330       340
                   ....*....|....*....|....*
gi 226442759   419 DGDTVSVHRPSFYAERFFKFMSSTV 443
Cdd:smart00330 318 DGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
158-442 2.56e-124

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: 366.79  E-value: 2.56e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  158 SLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVV 237
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  238 MNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPT-YKDLDFMQDMPEgLLLDSDTFGALVKTLQRDCLVLESFKIMD 316
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  317 YSLLLGVHNIDQqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmggipavngrGERLLLHIGI 396
Cdd:pfam01504 160 YSLLLGIHDLDE----------------------------------------------------------DGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 226442759  397 IDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSST 442
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
129-441 8.95e-96

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: 294.48  E-value: 8.95e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 129 QDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSN--PGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYY 206
Cdd:cd00139    1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKesEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 207 MNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASK-KEKEKSLPTYKDLDFMQDM 284
Cdd:cd00139   81 EHIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKeKEKKKGLKVLKDLDFLEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 285 pEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHnidqqererqaegaqskadekrpvaqkalystamesiqgg 364
Cdd:cd00139  161 -EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH---------------------------------------- 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226442759 365 aargeaietddtmggipavngrgeRLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDT-VSVHRPSFYAERFFKFMSS 441
Cdd:cd00139  200 ------------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
84-440 2.06e-95

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: 295.74  E-value: 2.06e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  84 QLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQ-DFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-N 161
Cdd:cd17302    9 QLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSsDFKWKDYCPMVFRNLRELFGIDAADYMLSLCgD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 162 EPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCV-QSGGKNIRVVVMNN 240
Cdd:cd17302   89 DALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 241 VLPRVVKMHLKFDLKGSTYKRRASKKEKE-KSLPTYKDLDFmqDMPegLLLDSDTFGALVKTLQRDCLVLESFKIMDYSL 319
Cdd:cd17302  169 LFCTELRIHRRFDLKGSTHGRTTGKPESEiDPNTTLKDLDL--DFK--FRLEKGWRDALMRQIDADCAFLEALRIMDYSL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 320 LLGVHnidqqererqaegaqskadekrpvaqkalystamesIQGGAARGEAIEtddtmggipavngrgerLLLHIGIIDI 399
Cdd:cd17302  245 LLGVH------------------------------------FRAGDSTGEPYD-----------------VVLYFGIIDI 271
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 226442759 400 LQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMS 440
Cdd:cd17302  272 LQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIR 312
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
85-441 9.20e-89

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: 278.80  E-value: 9.20e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  85 LGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFqDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNE-P 163
Cdd:cd17303    9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKyI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 164 LIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVL 242
Cdd:cd17303   88 LSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKmPRGRKIHFVVMNNLF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 243 PRVVKMHLKFDLKGSTYKRRAS-KKEKEKSLPTYKDLDFMQdMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLL 321
Cdd:cd17303  168 PPHRDIHQTFDLKGSTVGRETPeDKLAKGPRATLKDLNWLR-RKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 322 GVHNIDqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGER--LLLHIGIIDI 399
Cdd:cd17303  247 GIHDLD--------------------------------------------------GGFQATDENNEPgdEIYYLGIIDI 276
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 226442759 400 LQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSS 441
Cdd:cd17303  277 LTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
52-444 5.34e-77

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 260.54  E-value: 5.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  52 PGHGKKLGHRGVDasgettykkttsstLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIF--FPSEGSNLTPAHHFQ 129
Cdd:PLN03185 337 PGETIIKGHRSYD--------------LMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWmnFPKAGSQLTPSHQSE 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 130 DFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-NEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMN 208
Cdd:PLN03185 403 DFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 209 LNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSlPTYKDLdfmqDMPEG 287
Cdd:PLN03185 483 VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN-TTLKDL----DLNYS 557
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 288 LLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKAL--------YSTAME 359
Cdd:PLN03185 558 FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITADGLEVVAEEDtiedeelsYPEGLV 637
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 360 SIQGGAA----------RGEAI--------ETDDTMGGIP------AVN--GRGER-----------------LLLHIGI 396
Cdd:PLN03185 638 LVPRGADdgstvpgphiRGSRLrasaagdeEVDLLLPGTArlqiqlGVNmpARAERipgredkekqsfhevydVVLYLGI 717
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 226442759 397 IDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMsSTVF 444
Cdd:PLN03185 718 IDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
79-441 9.43e-68

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: 222.92  E-value: 9.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  79 LKGAIQLGIGYTVGNLSSKPERDVLM-QDFYV-----VESIFFPSEgsNLtPAHhfqdFRFKTYAPVAFRYFRELFGIRP 152
Cdd:cd17305    2 LLSVFMWGINHSINELSHVPIPVMLMpDDFKAyskikVDNHLFNKE--NL-PSH----FKVKEYCPLVFRNLRERFGIDD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 153 DDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNL-NQNPRTLLPKFYGLYCVQSGGK 231
Cdd:cd17305   75 DDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRITVNGV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 232 NIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMpEGLLLDSDTFGALVKTLQRDCLVLES 311
Cdd:cd17305  155 ETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDG-TKIYIGDEAKAKLLETLKRDVEFLAK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 312 FKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkaLYstamesiqggaargeaietddtmggipavngrgerll 391
Cdd:cd17305  234 LNLMDYSLLVGIHDC--------------------------IY------------------------------------- 250
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226442759 392 lHIGIIDILQSYRFIKKLEHTWKALVHDGDT-VSVHRPSFYAERFFKFMSS 441
Cdd:cd17305  251 -FMAIIDILTHYGAKKRAAHAAKTVKHGAGAeISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
86-441 1.24e-44

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: 161.37  E-value: 1.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  86 GIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhfqdFRFKTYAPVAFRYFRELFGIRPDDYLYSL 159
Cdd:cd17310   20 GVNHTINELSNVPVPVMLMPDDFKayskikVDNHLFNKE--NL-PSR----FKFKEYCPMVFRNLRERFGIDDQDYQNSV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 160 CNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVM 238
Cdd:cd17310   93 TRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVETYMVVT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 239 NNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDmPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYS 318
Cdd:cd17310  173 RNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNE-GQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 319 LLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmggipavngrgerlLLHIGIID 398
Cdd:cd17310  252 LLVGIHDV----------------------------------------------------------------VYFMAIID 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 226442759 399 ILQSYRFIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSS 441
Cdd:cd17310  268 ILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
124-441 7.37e-40

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: 148.20  E-value: 7.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 124 PAHhfqdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLP 203
Cdd:cd17309   59 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 204 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQ 282
Cdd:cd17309  135 KYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 283 DmPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiq 362
Cdd:cd17309  215 D-GQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV------------------------------------ 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 363 ggaargeaietddtmggipavngrgerlLLHIGIIDILQSYRFIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSS 441
Cdd:cd17309  258 ----------------------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
131-441 1.57e-38

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: 143.04  E-value: 1.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 131 FRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNpGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGY--YM- 207
Cdd:cd17300    3 FTCTIYFAEQFHALRSLYCGGEDDFIRSLSRCVKWDASG-GKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfeYMa 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 208 -NLNQNPRTLLPKFYGLYCVQ----SGGKNIR--VVVMNNVLPRvVKMHLKFDLKGSTYKRRASKKEKEKS-LPtykDLD 279
Cdd:cd17300   82 kALFHKRPSLLAKILGVYRISvknsTTNKTSKqdLLVMENLFYG-RNISQVYDLKGSLRNRYVNVAEDEDSvLL---DEN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 280 FMQDMPEG-LLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGvhnIDQQERErqaegaqskadekrpvaqkalystam 358
Cdd:cd17300  158 FLEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVG---IDEEKKE-------------------------- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 359 esiqggaargeaietddtmggipavngrgerllLHIGIIDILQSYRFIKKLEHTWKALVHDGD----TVsVHrPSFYAER 434
Cdd:cd17300  209 ---------------------------------LVVGIIDYIRTYTWDKKLESWVKSLGILGGggepTV-IS-PELYKKR 253

                 ....*..
gi 226442759 435 FFKFMSS 441
Cdd:cd17300  254 FREAMDK 260
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
130-445 2.12e-38

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 150.48  E-value: 2.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 130 DFRFKTYAPVAFRYFRELFGIrpDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNL 209
Cdd:COG5253  335 EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHV 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 210 NQNPRTLLPKFYGLYCVQ-------SGGKNIRVVVMNNVLPRvVKMHLKFDLKGSTYKRRASKKEKEKS-LPTYKDLDFM 281
Cdd:COG5253  413 LFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYP-HGIHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWI 491
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 282 QdmpEGLLLDSDTFGALVKT-LQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkaLYSTAMES 360
Cdd:COG5253  492 R---ESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDDE--------------------------REEASVGL 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 361 IQggaargEAIETDDTMGGIpavngrgerllLHIGIIDILQSYRFIKKLEhtwkalvhdgdtVSVHRPSFYAERFFKFMS 440
Cdd:COG5253  543 II------DFIRTRMTGDKK-----------LESGIKDKLTVGSFTKRKE------------PTAVTPRQYKNRFRKAME 593

                 ....*
gi 226442759 441 STVFR 445
Cdd:COG5253  594 AYIDP 598
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
86-441 2.54e-38

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: 143.47  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759  86 GIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhfqdFRFKTYAPVAFRYFRELFGIRPDDYLYSL 159
Cdd:cd17311    9 GVNHSINELSQVPVPVMLLPDDFKanskikVNNHLFNRE--NL-PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVSL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 160 CNEPliELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVM 238
Cdd:cd17311   82 TRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKcHGNTLLPQFLGMYRLSVDNEDSYMLVM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 239 NNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMpEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYS 318
Cdd:cd17311  160 RNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKN-QKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 319 LLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmggipavngrgerlLLHIGIID 398
Cdd:cd17311  239 LLLGIHDV----------------------------------------------------------------VYFMGLID 254
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 226442759 399 ILQSYRFIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSS 441
Cdd:cd17311  255 ILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
129-441 5.26e-37

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: 140.57  E-value: 5.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 129 QDFRFKTYAPVAFRYFRELFGIRPDDYLYSL-CNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYM 207
Cdd:cd17304   47 KGFEFRTYAGPVFATLRQSLGISEKEYQNSLsPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQ 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 208 NLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKrRASKKEKEKS--LPTYKDLDFmqdm 284
Cdd:cd17304  127 HLENYPHSLLVKFLGVHSIKlPGKKKKYFIVMQSVFYPDERINERYDIKGCQVS-RYTDPEPEGSqiIVVLKDLNF---- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 285 pEGLLLDSDTFGA-LVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqsKADEKR---PVAQKALYstames 360
Cdd:cd17304  202 -EGNSINLGQQRSwFLRQVEIDTEFLKGLNVLDYSLLVGFQPL--------------HSDENRrllPNYKNALH------ 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442759 361 iqggaargeaietddtmggipAVNGRGERLLlhIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMS 440
Cdd:cd17304  261 ---------------------VVDGPEYRYF--VGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVE 317

                 .
gi 226442759 441 S 441
Cdd:cd17304  318 D 318
 
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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