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Conserved domains on  [gi|1773394682|ref|NP_001362968|]
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phosphatidylinositol 4-phosphate 5-kinase type-1 beta isoform 2 [Homo sapiens]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase type-1 beta( domain architecture ID 13022714)

phosphatidylinositol 4-phosphate 5-kinase type-1 beta 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-400 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: 706.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  27 SAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17307     1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 107 YSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 186
Cdd:cd17307    81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 187 VMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMD 266
Cdd:cd17307   161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 267 YSLLLGIHFLdhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmGGIPAKSHRGEKLLLFM 346
Cdd:cd17307   241 YSLLLGIHVL-----------------------------------------------------GGIPAKNHKGEKLLLFM 267
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1773394682 347 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQ 400
Cdd:cd17307   268 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ 321
 
Name Accession Description Interval E-value
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-400 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: 706.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  27 SAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17307     1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 107 YSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 186
Cdd:cd17307    81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 187 VMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMD 266
Cdd:cd17307   161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 267 YSLLLGIHFLdhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmGGIPAKSHRGEKLLLFM 346
Cdd:cd17307   241 YSLLLGIHVL-----------------------------------------------------GGIPAKNHKGEKLLLFM 267
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1773394682 347 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQ 400
Cdd:cd17307   268 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ 321
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
53-393 3.21e-148

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 429.11  E-value: 3.21e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682   53 LMQDFYVVESVFLPSEGS-NLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTS 131
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  132 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGG---INIRIVVMNNVLPRSMRMHFTYDLKGST 208
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  209 YKRRASrKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETP 288
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  289 QNVPDAKRTGMQKVLYSTamESIQGPGKSGDGiiTENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKAL 368
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNS--PDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSI 315
                          330       340
                   ....*....|....*....|....*
gi 1773394682  369 VYDGDTVSVHRPSFYADRFLKFMNS 393
Cdd:smart00330 316 GHDGKTISVVHPEQYAKRFRDFMDK 340
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
108-393 1.22e-120

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: 354.08  E-value: 1.22e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 108 SICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVV 187
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 188 MNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPT-FKDLDFLQDMHEgLYFDTETYNALMKTLQRDCRVLESFKIMD 266
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 267 YSLLLGIHFLDhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmggipakshRGEKLLLFM 346
Cdd:pfam01504 160 YSLLLGIHDLD------------------------------------------------------------EDGKEIYYL 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1773394682 347 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNS 393
Cdd:pfam01504 180 GIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEK 226
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
19-396 1.21e-77

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 259.77  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  19 KTYKKTASSAIKG--------AIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFL--PSEGSNLTPAHHYPDFRFKTYAP 88
Cdd:PLN03185  332 KEIKRPGETIIKGhrsydlmlSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMnfPKAGSQLTPSHQSEDFKWKDYCP 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  89 LAFRYFRELFGIKPDDYLYSIC-SEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLL 167
Cdd:PLN03185  412 MVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLI 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 168 PKFYGLYCMQ-SGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKsNPTFKDLdflqDMHEGLYFDTETYN 246
Cdd:PLN03185  492 TKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDE-NTTLKDL----DLNYSFYLEPSWRD 566
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 247 ALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDakrTGMQKVLYSTAME-----SIQG----PGKS 317
Cdd:PLN03185  567 ALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITA---DGLEVVAEEDTIEdeelsYPEGlvlvPRGA 643
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 318 GDGIITENPDTMGG-----------------------------IPAKSHR------GEK--------LLLFMGIIDILQS 354
Cdd:PLN03185  644 DDGSTVPGPHIRGSrlrasaagdeevdlllpgtarlqiqlgvnMPARAERipgredKEKqsfhevydVVLYLGIIDILQE 723
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1773394682 355 YRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNsRVF 396
Cdd:PLN03185  724 YNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFIQ-KVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
69-395 5.37e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 142.01  E-value: 5.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  69 GSNLTPAHHYpDFRFKTYAPLAFRYFRELFGIkpDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFL 148
Cdd:COG5253   325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 149 QKLLPGYYMNLNQNPRTLLPKFYGLY--CMQSGGINIR-----IVVMNNVLPRSmRMHFTYDLKGSTYKRraSRKEREKS 221
Cdd:COG5253   402 RPMIFEYYVHVLFNPLTLLCKIFGFYrvKSRSSISSSKsrkiyFIVMENLFYPH-GIHRIFDLKGSMRNR--HVERTGKS 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 222 NPTFKDLDFLQDMHEGLYFDTETYNALMKT-LQRDCRVLESFKIMDYSLLLGIHFldhslkEKEEETPQNVPDAKRTGMq 300
Cdd:COG5253   479 MSVLLDMNDVEWIRESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDD------EREEASVGLIIDFIRTRM- 551
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 301 kvlystamesiqgpgkSGDGIitenpdtmggipakshrgekllLFMGIIDILQSYRLMKKLEhswkalvydgdtVSVHRP 380
Cdd:COG5253   552 ----------------TGDKK----------------------LESGIKDKLTVGSFTKRKE------------PTAVTP 581
                         330
                  ....*....|....*
gi 1773394682 381 SFYADRFLKFMNSRV 395
Cdd:COG5253   582 RQYKNRFRKAMEAYI 596
 
Name Accession Description Interval E-value
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
27-400 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: 706.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  27 SAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17307     1 SAIKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 107 YSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 186
Cdd:cd17307    81 YSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 187 VMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMD 266
Cdd:cd17307   161 VMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 267 YSLLLGIHFLdhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmGGIPAKSHRGEKLLLFM 346
Cdd:cd17307   241 YSLLLGIHVL-----------------------------------------------------GGIPAKNHKGEKLLLFM 267
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1773394682 347 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQ 400
Cdd:cd17307   268 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKVQ 321
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
27-399 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: 657.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  27 SAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYL 106
Cdd:cd17301     1 SELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 107 YSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIV 186
Cdd:cd17301    81 LSLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 187 VMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMD 266
Cdd:cd17301   161 VMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 267 YSLLLGIHFLdhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmGGIPAKSHRGEKLLLFM 346
Cdd:cd17301   241 YSLLLGVHNL-----------------------------------------------------GGIPARNSKGERLLLFI 267
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1773394682 347 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKI 399
Cdd:cd17301   268 GIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHRPSFYAERFQNFMANTVFKKI 320
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
26-398 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: 612.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  26 SSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDY 105
Cdd:cd17308     1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 106 LYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRI 185
Cdd:cd17308    81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 186 VVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIM 265
Cdd:cd17308   161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 266 DYSLLLGIHfldhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdTMGGIPAKSHRGEKLLLF 345
Cdd:cd17308   241 DYSLLLGVH-----------------------------------------------------NIGGIPAVNGKGERLLLY 267
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1773394682 346 MGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKK 398
Cdd:cd17308   268 IGIIDILQSYRLIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRK 320
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
24-399 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: 577.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  24 TASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPD 103
Cdd:cd17306     1 TTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 104 DYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINI 183
Cdd:cd17306    81 DYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 184 RIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFK 263
Cdd:cd17306   161 RIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 264 IMDYSLLLGIHFLdhslkekeeetpqnvpDAKRTGMqkvlystamesiqgpgksgdgiiTENPDTMGGIPAKSHRGEKLL 343
Cdd:cd17306   241 IMDYSLLVGIHNI----------------DARRGGT-----------------------IETDDQMGGIPARNSKGERLL 281
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1773394682 344 LFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKI 399
Cdd:cd17306   282 LYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKI 337
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
53-393 3.21e-148

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 429.11  E-value: 3.21e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682   53 LMQDFYVVESVFLPSEGS-NLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTS 131
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  132 DDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGG---INIRIVVMNNVLPRSMRMHFTYDLKGST 208
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  209 YKRRASrKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETP 288
Cdd:smart00330 161 RGREAD-KKKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  289 QNVPDAKRTGMQKVLYSTamESIQGPGKSGDGiiTENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKAL 368
Cdd:smart00330 240 VYGSDESPSSESSNGGKA--PDITGNLLVSNS--PDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSI 315
                          330       340
                   ....*....|....*....|....*
gi 1773394682  369 VYDGDTVSVHRPSFYADRFLKFMNS 393
Cdd:smart00330 316 GHDGKTISVVHPEQYAKRFRDFMDK 340
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
108-393 1.22e-120

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: 354.08  E-value: 1.22e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 108 SICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVV 187
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 188 MNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPT-FKDLDFLQDMHEgLYFDTETYNALMKTLQRDCRVLESFKIMD 266
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 267 YSLLLGIHFLDhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmggipakshRGEKLLLFM 346
Cdd:pfam01504 160 YSLLLGIHDLD------------------------------------------------------------EDGKEIYYL 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1773394682 347 GIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNS 393
Cdd:pfam01504 180 GIIDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEK 226
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
79-393 7.05e-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: 291.78  E-value: 7.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  79 PDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSN--PGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYY 156
Cdd:cd00139     1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKesEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 157 MNLNQNPRTLLPKFYGLYCMQ-SGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASR-KEREKSNPTFKDLDFLqDM 234
Cdd:cd00139    81 EHIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKeKEKKKGLKVLKDLDFL-EK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 235 HEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHfldhslkekeeetpqnvpdakrtgmqKVLYstamesiqgp 314
Cdd:cd00139   160 GEKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH--------------------------RLVY---------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 315 gksgdgiitenpdtmggipakshrgeklllFMGIIDILQSYRLMKKLEHSWKALVYDGDT-VSVHRPSFYADRFLKFMNS 393
Cdd:cd00139   204 ------------------------------YLGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
34-392 8.51e-96

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: 293.81  E-value: 8.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  34 QLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHY-PDFRFKTYAPLAFRYFRELFGIKPDDYLYSIC-S 111
Cdd:cd17302     9 QLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQsSDFKWKDYCPMVFRNLRELFGIDAADYMLSLCgD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 112 EPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCM-QSGGINIRIVVMNN 190
Cdd:cd17302    89 DALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 191 VLPRSMRMHFTYDLKGSTYKRRASRKERE-KSNPTFKDLDFlqdmheGLYF--DTETYNALMKTLQRDCRVLESFKIMDY 267
Cdd:cd17302   169 LFCTELRIHRRFDLKGSTHGRTTGKPESEiDPNTTLKDLDL------DFKFrlEKGWRDALMRQIDADCAFLEALRIMDY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 268 SLLLGIHFLDhslkEKEEETPQNVpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmggipakshrgeklLLFMG 347
Cdd:cd17302   243 SLLLGVHFRA----GDSTGEPYDV---------------------------------------------------VLYFG 267
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1773394682 348 IIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMN 392
Cdd:cd17302   268 IIDILQEYNISKKLEHAYKSLQYDPASISAVDPKLYSRRFRDFIR 312
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
35-393 4.41e-85

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: 266.47  E-value: 4.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  35 LGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYpDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSE-P 113
Cdd:cd17303     9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKyI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 114 LIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLY--CMQSGGiNIRIVVMNNV 191
Cdd:cd17303    88 LSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHrvKMPRGR-KIHFVVMNNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 192 LPRSMRMHFTYDLKGSTYKRRAS-RKEREKSNPTFKDLDFLQdMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLL 270
Cdd:cd17303   167 FPPHRDIHQTFDLKGSTVGRETPeDKLAKGPRATLKDLNWLR-RKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 271 LGIHFLDhslkekeeetpqnvpdakrtgmqkvlystamesiqgpgksgdgiitenpdtmGGIPAKSHRGEK--LLLFMGI 348
Cdd:cd17303   246 VGIHDLD----------------------------------------------------GGFQATDENNEPgdEIYYLGI 273
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1773394682 349 IDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNS 393
Cdd:cd17303   274 IDILTPYNAKKKLEHFFKSLRHDRHTISAVPPKEYARRFLKFIED 318
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
19-396 1.21e-77

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 259.77  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  19 KTYKKTASSAIKG--------AIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFL--PSEGSNLTPAHHYPDFRFKTYAP 88
Cdd:PLN03185  332 KEIKRPGETIIKGhrsydlmlSLQLGIRYTVGKITPIQRREVRPSDFGPRASFWMnfPKAGSQLTPSHQSEDFKWKDYCP 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  89 LAFRYFRELFGIKPDDYLYSIC-SEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLL 167
Cdd:PLN03185  412 MVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHVKTYENTLI 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 168 PKFYGLYCMQ-SGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKsNPTFKDLdflqDMHEGLYFDTETYN 246
Cdd:PLN03185  492 TKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDE-NTTLKDL----DLNYSFYLEPSWRD 566
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 247 ALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDakrTGMQKVLYSTAME-----SIQG----PGKS 317
Cdd:PLN03185  567 ALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITA---DGLEVVAEEDTIEdeelsYPEGlvlvPRGA 643
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 318 GDGIITENPDTMGG-----------------------------IPAKSHR------GEK--------LLLFMGIIDILQS 354
Cdd:PLN03185  644 DDGSTVPGPHIRGSrlrasaagdeevdlllpgtarlqiqlgvnMPARAERipgredKEKqsfhevydVVLYLGIIDILQE 723
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1773394682 355 YRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNsRVF 396
Cdd:PLN03185  724 YNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFIQ-KVF 764
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
29-391 1.03e-63

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: 210.21  E-value: 1.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  29 IKGAIQLGIGYTVGNLTSKPERDVLM-QDFYV-----VESVFLPSEgsNLtPAHhypdFRFKTYAPLAFRYFRELFGIKP 102
Cdd:cd17305     2 LLSVFMWGINHSINELSHVPIPVMLMpDDFKAyskikVDNHLFNKE--NL-PSH----FKVKEYCPLVFRNLRERFGIDD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 103 DDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNL-NQNPRTLLPKFYGLYCMQSGGI 181
Cdd:cd17305    75 DDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRITVNGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 182 NIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEgLYFDTETYNALMKTLQRDCRVLES 261
Cdd:cd17305   155 ETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTK-IYIGDEAKAKLLETLKRDVEFLAK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 262 FKIMDYSLLLGIHfldhslkekeeetpqnvpdakrtgmqKVLYstamesiqgpgksgdgiitenpdtmggipakshrgek 341
Cdd:cd17305   234 LNLMDYSLLVGIH--------------------------DCIY------------------------------------- 250
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1773394682 342 lllFMGIIDILQSYRLMKKLEHSWKALVYDGDT-VSVHRPSFYADRFLKFM 391
Cdd:cd17305   251 ---FMAIIDILTHYGAKKRAAHAAKTVKHGAGAeISTVKPEQYAKRFLEFI 298
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
25-393 5.38e-48

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: 169.07  E-value: 5.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  25 ASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFlpSEGSNLTPAHHYPD-FRFKTYAPLAFRYFRELFGIKPD 103
Cdd:cd17310     9 ASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKI--KVDNHLFNKENLPSrFKFKEYCPMVFRNLRERFGIDDQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 104 DYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCMQSGGIN 182
Cdd:cd17310    87 DYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 183 IRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEgLYFDTETYNALMKTLQRDCRVLESF 262
Cdd:cd17310   167 TYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQK-LHVGEESKKNFLEKLKRDVEFLAQL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 263 KIMDYSLLLGIHfldhslkekeeetpqnvpdakrtgmqKVLYstamesiqgpgksgdgiitenpdtmggipakshrgekl 342
Cdd:cd17310   246 KIMDYSLLVGIH--------------------------DVVY-------------------------------------- 261
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1773394682 343 llFMGIIDILQSYRLMKKLEHSWKALVYD-GDTVSVHRPSFYADRFLKFMNS 393
Cdd:cd17310   262 --FMAIIDILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
74-393 2.67e-41

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (PIP5K2A) and similar proteins; PIP5K2A (EC 2.7.1.149), also known as PIP4K2A, or 1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha, or diphosphoinositide kinase 2-alpha, or PIP5KIII, or phosphatidylinositol 5-phosphate 4-kinase type II alpha, or PI(5)P 4-kinase type II alpha, or PIP4KII-alpha, or PtdIns(4)P-5-kinase C isoform, or PtdIns(5)P-4-kinase isoform 2-alpha, catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), one of the key metabolic crossroads in phosphoinositide signaling. It is possibly involved in a mechanism protecting against tardive dyskinesia-inducing neurotoxicity. PIP5K2A is associated with schizophrenia. It controls the function of KCNQ channels via phosphatidylinositol-4,5-bisphosphate (PIP2) synthesis, and plays a potential role in the regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors.


Pssm-ID: 340446  Cd Length: 309  Bit Score: 150.90  E-value: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  74 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSIC-SEPLIELSNpGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLL 152
Cdd:cd17309    59 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTrSAPLANDSQ-ARSGARFHTSYDKRYIIKTITSEDVAEMHNIL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 153 PGYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFL 231
Cdd:cd17309   134 KKYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFI 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 232 QDMHEgLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHfldhslkekeeetpqnvpdakrtgmqKVLYstamesi 311
Cdd:cd17309   214 NDGQK-IYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIH--------------------------DVVY------- 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 312 qgpgksgdgiitenpdtmggipakshrgeklllFMGIIDILQSYRLMKKLEHSWKALVYD-GDTVSVHRPSFYADRFLKF 390
Cdd:cd17309   260 ---------------------------------FMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDF 306

                  ...
gi 1773394682 391 MNS 393
Cdd:cd17309   307 ITS 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
74-393 1.24e-39

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: 146.16  E-value: 1.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  74 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPliELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLP 153
Cdd:cd17311    50 PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 154 GYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQ 232
Cdd:cd17311   124 HYHQYIVKcHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLN 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 233 DMhEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHfldhslkekeeetpqnvpdakrtgmqKVLYstamesiq 312
Cdd:cd17311   204 KN-QKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIH--------------------------DVVY-------- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 313 gpgksgdgiitenpdtmggipakshrgeklllFMGIIDILQSYRLMKKLEHSWKALVYD-GDTVSVHRPSFYADRFLKFM 391
Cdd:cd17311   249 --------------------------------FMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFI 296

                  ..
gi 1773394682 392 NS 393
Cdd:cd17311   297 TN 298
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
79-393 2.21e-37

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in 1-phosphatidylinositol-3-phosphate 5-kinase and similar proteins; 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is also called FYVE finger-containing phosphoinositide kinase, PIKfyve, phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase). It forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] by catalyzing the phosphorylation of phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) on the fifth hydroxyl of the myo-inositol ring. Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. PIKfyve is vital in early embryonic development. It forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, playing a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human Ether-a-go-go-Related Gene (hERG) channels. This family also includes the yeast ortholog of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal catalytic lipid kinase domain related to PtdInsP kinases (or the PIPKc domain).


Pssm-ID: 340437  Cd Length: 262  Bit Score: 138.80  E-value: 2.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  79 PDFRFKTYAPLAFRYFRELFGIKPDDYLYSIC-SEPLIelSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGY-- 155
Cdd:cd17300     1 TKFTCTIYFAEQFHALRSLYCGGEDDFIRSLSrCVKWD--ASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfe 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 156 YM--NLNQNPRTLLPKFYGLY--CMQSGGIN----IRIVVMNNVLPRSmRMHFTYDLKGSTYKRRASRKEREKSnpTFKD 227
Cdd:cd17300    79 YMakALFHKRPSLLAKILGVYriSVKNSTTNktskQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDEDS--VLLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 228 LDFLQDMHEG-LYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIhflDHSLKEkeeetpqnvpdakrtgmqkvlyst 306
Cdd:cd17300   156 ENFLEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI---DEEKKE------------------------ 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 307 amesiqgpgksgdgiitenpdtmggipakshrgekllLFMGIIDILQSYRLMKKLEHSWKALVYDGD----TVsVHrPSF 382
Cdd:cd17300   209 -------------------------------------LVVGIIDYIRTYTWDKKLESWVKSLGILGGggepTV-IS-PEL 249
                         330
                  ....*....|.
gi 1773394682 383 YADRFLKFMNS 393
Cdd:cd17300   250 YKKRFREAMDK 260
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
32-393 2.90e-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: 140.19  E-value: 2.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  32 AIQLGIGYTVGNLTSKPERDVLMQDFY--VVESVFLPSEGsnltpahhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSI 109
Cdd:cd17304     9 MMKEGLRAAIQNSIDVPPKESLSDDDYteVLTQVIPKHKG-----------FEFRTYAGPVFATLRQSLGISEKEYQNSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 110 -CSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQ-SGGINIRIVV 187
Cdd:cd17304    78 sPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLENYPHSLLVKFLGVHSIKlPGKKKKYFIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 188 MNNVLPRSMRMHFTYDLKGSTYKrRASRKEREKSN--PTFKDLDFLQDMhegLYFDtETYNALMKTLQRDCRVLESFKIM 265
Cdd:cd17304   158 MQSVFYPDERINERYDIKGCQVS-RYTDPEPEGSQiiVVLKDLNFEGNS---INLG-QQRSWFLRQVEIDTEFLKGLNVL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 266 DYSLLLGIHFLdHSlkekeEETPQNVPDAKrtgmqkvlysTAMESIQGPgksgdgiitenpdtmggipakshrgeKLLLF 345
Cdd:cd17304   233 DYSLLVGFQPL-HS-----DENRRLLPNYK----------NALHVVDGP--------------------------EYRYF 270
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1773394682 346 MGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNS 393
Cdd:cd17304   271 VGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVED 318
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
69-395 5.37e-36

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 142.01  E-value: 5.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682  69 GSNLTPAHHYpDFRFKTYAPLAFRYFRELFGIkpDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFL 148
Cdd:COG5253   325 LNEQFEEGLY-EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICF 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 149 QKLLPGYYMNLNQNPRTLLPKFYGLY--CMQSGGINIR-----IVVMNNVLPRSmRMHFTYDLKGSTYKRraSRKEREKS 221
Cdd:COG5253   402 RPMIFEYYVHVLFNPLTLLCKIFGFYrvKSRSSISSSKsrkiyFIVMENLFYPH-GIHRIFDLKGSMRNR--HVERTGKS 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 222 NPTFKDLDFLQDMHEGLYFDTETYNALMKT-LQRDCRVLESFKIMDYSLLLGIHFldhslkEKEEETPQNVPDAKRTGMq 300
Cdd:COG5253   479 MSVLLDMNDVEWIRESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDD------EREEASVGLIIDFIRTRM- 551
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773394682 301 kvlystamesiqgpgkSGDGIitenpdtmggipakshrgekllLFMGIIDILQSYRLMKKLEhswkalvydgdtVSVHRP 380
Cdd:COG5253   552 ----------------TGDKK----------------------LESGIKDKLTVGSFTKRKE------------PTAVTP 581
                         330
                  ....*....|....*
gi 1773394682 381 SFYADRFLKFMNSRV 395
Cdd:COG5253   582 RQYKNRFRKAMEAYI 596
 
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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