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Conserved domains on  [gi|665402358|ref|NP_001286647|]
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skittles, isoform C [Drosophila melanogaster]

Protein Classification

phosphatidylinositol 4-phosphate 5-kinase type-1( domain architecture ID 13022639)

phosphatidylinositol 4-phosphate 5-kinase type-1 phosphorylates the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes

CATH:  3.30.800.10
EC:  2.7.1.68
PubMed:  9535851
SCOP:  4002087

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
158-577 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: 628.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 158 QIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLM 237
Cdd:cd17301    2 ELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 238 SMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRLVA 317
Cdd:cd17301   82 SLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 318 MNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDY 397
Cdd:cd17301  162 MNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 398 SLLVGIHNLdlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmn 477
Cdd:cd17301  242 SLLLGVHNL----------------------------------------------------------------------- 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 478 rqrlvahstalesitadmdvpleededvpaGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCR 557
Cdd:cd17301  251 ------------------------------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHR 300
                        410       420
                 ....*....|....*....|
gi 665402358 558 PSFYAKRFQDAMGKQVFKKT 577
Cdd:cd17301  301 PSFYAERFQNFMANTVFKKI 320
 
Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
158-577 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: 628.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 158 QIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLM 237
Cdd:cd17301    2 ELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 238 SMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRLVA 317
Cdd:cd17301   82 SLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 318 MNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDY 397
Cdd:cd17301  162 MNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 398 SLLVGIHNLdlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmn 477
Cdd:cd17301  242 SLLLGVHNL----------------------------------------------------------------------- 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 478 rqrlvahstalesitadmdvpleededvpaGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCR 557
Cdd:cd17301  251 ------------------------------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHR 300
                        410       420
                 ....*....|....*....|
gi 665402358 558 PSFYAKRFQDAMGKQVFKKT 577
Cdd:cd17301  301 PSFYAERFQNFMANTVFKKI 320
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
183-573 3.31e-163

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 476.10  E-value: 3.31e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   183 LMNDFWEMETISFPPDGSS-ITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLMSMCASPLRELSNPGASGSIFYLTT 261
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHLeLTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   262 DDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSK---NVRLVAMNNLLPSDIKMHCKYDLKGSS 338
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   339 FRRKASKaERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIHNLDLAAKEKREERI 418
Cdd:smart00330 161 RGREADK-KKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   419 LNARAKLQRKESAAQGPPslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmnrqrlvahstalESITADMDVP 498
Cdd:smart00330 240 VYGSDESPSSESSNGGKA----------------------------------------------------PDITGNLLVS 267
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402358   499 LEEDEDVPAGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRPSFYAKRFQDAMGKQV 573
Cdd:smart00330 268 NSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
238-571 7.21e-107

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: 326.35  E-value: 7.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  238 SMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRLVA 317
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  318 MNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPT-FKDLDFAEHHPNgIFLETDKYNALMSTIKRDCMVLESFQIMD 396
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  397 YSLLVGIHNLDlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsm 476
Cdd:pfam01504 160 YSLLLGIHDLD--------------------------------------------------------------------- 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  477 nrqrlvahstalesitadmdvpleededvpaggiparseNDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVC 556
Cdd:pfam01504 171 ---------------------------------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAV 211
                         330
                  ....*....|....*
gi 665402358  557 RPSFYAKRFQDAMGK 571
Cdd:pfam01504 212 PPKEYAERFLKFIEK 226
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
119-574 2.08e-84

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 284.80  E-value: 2.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 119 LDASISRNPSTTGGKHEKKLghRRVAEGGEVTYKKIQSKQIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETI--SFP 196
Cdd:PLN03185 312 LNNSFSSTSRRAKRRQKKLV--KEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFwmNFP 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 197 PDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLMSMCA-SPLRELSNPGASGSIFYLTTDDEFIIKTVQKKEC 275
Cdd:PLN03185 390 KAGSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICGnDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEV 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 276 EFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFH-YNSKNVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASpT 354
Cdd:PLN03185 470 KVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENT-T 548
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 355 FKDLDFAEHhpngIFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIHnldLAAKEKReeRILNARAKLQRKESAAQG 434
Cdd:PLN03185 549 LKDLDLNYS----FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH---FRAPQHL--RSLLPYSRSITADGLEVV 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 435 PPSLNPDDDAPEADQNqLQAVASYASIPGTSAGAALNRTrsmnrqRLVAHSTALESI------TADMDVPLEEDEDVPAG 508
Cdd:PLN03185 620 AEEDTIEDEELSYPEG-LVLVPRGADDGSTVPGPHIRGS------RLRASAAGDEEVdlllpgTARLQIQLGVNMPARAE 692
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665402358 509 GIPARSENDERL-------ILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRPSFYAKRFQDAMgKQVF 574
Cdd:PLN03185 693 RIPGREDKEKQSfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
210-406 4.84e-30

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 126.21  E-value: 4.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 210 DFRFKVYAPIAFRYFRDLFGIapDDFLMSMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNL 289
Cdd:COG5253  335 EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHV 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 290 SQNPRTLLPKFFGLY-------CFHYNSKNVRLVAMNNLLPsDIKMHCKYDLKGSSFRR-KASKAERQKASPTFKDLDFA 361
Cdd:COG5253  413 LFNPLTLLCKIFGFYrvksrssISSSKSRKIYFIVMENLFY-PHGIHRIFDLKGSMRNRhVERTGKSMSVLLDMNDVEWI 491
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 665402358 362 EHHPNgIFLETDKyNALMSTIKRDCMVLESFQIMDYSLLVGIHNL 406
Cdd:COG5253  492 RESPK-IVFGLKK-KLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
 
Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
158-577 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: 628.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 158 QIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLM 237
Cdd:cd17301    2 ELMGAIQLGIGHSVGSLSSKPERDVLMQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 238 SMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRLVA 317
Cdd:cd17301   82 SLCNEPLRELSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 318 MNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDY 397
Cdd:cd17301  162 MNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 398 SLLVGIHNLdlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmn 477
Cdd:cd17301  242 SLLLGVHNL----------------------------------------------------------------------- 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 478 rqrlvahstalesitadmdvpleededvpaGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCR 557
Cdd:cd17301  251 ------------------------------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTVSVHR 300
                        410       420
                 ....*....|....*....|
gi 665402358 558 PSFYAKRFQDAMGKQVFKKT 577
Cdd:cd17301  301 PSFYAERFQNFMANTVFKKI 320
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
159-577 3.45e-168

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: 487.96  E-value: 3.45e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 159 IMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLMS 238
Cdd:cd17307    3 IKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 239 MCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRLVAM 318
Cdd:cd17307   83 ICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 319 NNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDYS 398
Cdd:cd17307  163 NNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDYS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 399 LLVGIHNLdlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmnr 478
Cdd:cd17307  243 LLLGIHVL------------------------------------------------------------------------ 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 479 qrlvahstalesitadmdvpleededvpaGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRP 558
Cdd:cd17307  251 -----------------------------GGIPAKNHKGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRP 301
                        410
                 ....*....|....*....
gi 665402358 559 SFYAKRFQDAMGKQVFKKT 577
Cdd:cd17307  302 SFYADRFLKFMNSRVFKKV 320
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
156-577 1.82e-163

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: 476.02  E-value: 1.82e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 156 SKQIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDF 235
Cdd:cd17308    1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 236 LMSMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRL 315
Cdd:cd17308   81 LYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 316 VAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIM 395
Cdd:cd17308  161 VVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 396 DYSLLVGIHNLdlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrs 475
Cdd:cd17308  241 DYSLLLGVHNI--------------------------------------------------------------------- 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 476 mnrqrlvahstalesitadmdvpleededvpaGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSV 555
Cdd:cd17308  252 --------------------------------GGIPAVNGKGERLLLYIGIIDILQSYRLIKKLEHTWKALVHDGDTVSV 299
                        410       420
                 ....*....|....*....|..
gi 665402358 556 CRPSFYAKRFQDAMGKQVFKKT 577
Cdd:cd17308  300 HRPSFYAERFFKFMSNTVFRKS 321
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
183-573 3.31e-163

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 476.10  E-value: 3.31e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   183 LMNDFWEMETISFPPDGSS-ITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLMSMCASPLRELSNPGASGSIFYLTT 261
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHLeLTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   262 DDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSK---NVRLVAMNNLLPSDIKMHCKYDLKGSS 338
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   339 FRRKASKaERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIHNLDLAAKEKREERI 418
Cdd:smart00330 161 RGREADK-KKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358   419 LNARAKLQRKESAAQGPPslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmnrqrlvahstalESITADMDVP 498
Cdd:smart00330 240 VYGSDESPSSESSNGGKA----------------------------------------------------PDITGNLLVS 267
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402358   499 LEEDEDVPAGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRPSFYAKRFQDAMGKQV 573
Cdd:smart00330 268 NSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
156-578 1.45e-159

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: 466.78  E-value: 1.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 156 SKQIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDF 235
Cdd:cd17306    3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 236 LMSMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRL 315
Cdd:cd17306   83 LYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 316 VAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNALMSTIKRDCMVLESFQIM 395
Cdd:cd17306  163 VVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFKIM 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 396 DYSLLVGIHNLDlaakekreerilnaraklqrkesAAQGppslnpdddapeadqnqlqavasyasipGTsagaalnrtrs 475
Cdd:cd17306  243 DYSLLVGIHNID-----------------------ARRG----------------------------GT----------- 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 476 mnrqrlvahstalesitadmdvpLEEDEDVpaGGIPARSENDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSV 555
Cdd:cd17306  261 -----------------------IETDDQM--GGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSV 315
                        410       420
                 ....*....|....*....|...
gi 665402358 556 CRPSFYAKRFQDAMGKQVFKKTP 578
Cdd:cd17306  316 HRPGFYAERFQRFMCNTVFKKIP 338
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
238-571 7.21e-107

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: 326.35  E-value: 7.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  238 SMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFHYNSKNVRLVA 317
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  318 MNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPT-FKDLDFAEHHPNgIFLETDKYNALMSTIKRDCMVLESFQIMD 396
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  397 YSLLVGIHNLDlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsm 476
Cdd:pfam01504 160 YSLLLGIHDLD--------------------------------------------------------------------- 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358  477 nrqrlvahstalesitadmdvpleededvpaggiparseNDERLILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVC 556
Cdd:pfam01504 171 ---------------------------------------EDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHDGDSISAV 211
                         330
                  ....*....|....*
gi 665402358  557 RPSFYAKRFQDAMGK 571
Cdd:pfam01504 212 PPKEYAERFLKFIEK 226
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
156-571 2.24e-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: 299.98  E-value: 2.24e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 156 SKQIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYN-DFRFKVYAPIAFRYFRDLFGIAPDD 234
Cdd:cd17302    1 SYDLMLNLQLGIRYSVGKIAPVARRDLKPSDFDPKAKQWFPFPGSGSTPPPHQSsDFKWKDYCPMVFRNLRELFGIDAAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 235 FLMSMCAS-PLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFH-YNSKN 312
Cdd:cd17302   81 YMLSLCGDdALRELSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVKpVGGRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 313 VRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPT-FKDLDFaehhpNGIF-LETDKYNALMSTIKRDCMVLE 390
Cdd:cd17302  161 VRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESEIDPNTtLKDLDL-----DFKFrLEKGWRDALMRQIDADCAFLE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 391 SFQIMDYSLLVGIHNLDLAakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaal 470
Cdd:cd17302  236 ALRIMDYSLLLGVHFRAGD------------------------------------------------------------- 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 471 nrtrsmnrqrlvAHSTAlesitadmdvpleedEDVpaggiparsenderlILYIGIIDILQSYRLEKKLEHTFKSILYNG 550
Cdd:cd17302  255 ------------STGEP---------------YDV---------------VLYFGIIDILQEYNISKKLEHAYKSLQYDP 292
                        410       420
                 ....*....|....*....|.
gi 665402358 551 DTVSVCRPSFYAKRFQDAMGK 571
Cdd:cd17302  293 ASISAVDPKLYSRRFRDFIRK 313
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
119-574 2.08e-84

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 284.80  E-value: 2.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 119 LDASISRNPSTTGGKHEKKLghRRVAEGGEVTYKKIQSKQIMGSIQLGIQHTVGSLASKPKRDLLMNDFWEMETI--SFP 196
Cdd:PLN03185 312 LNNSFSSTSRRAKRRQKKLV--KEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFwmNFP 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 197 PDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDDFLMSMCA-SPLRELSNPGASGSIFYLTTDDEFIIKTVQKKEC 275
Cdd:PLN03185 390 KAGSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICGnDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEV 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 276 EFLQKLLPGYYMNLSQNPRTLLPKFFGLYCFH-YNSKNVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASpT 354
Cdd:PLN03185 470 KVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENT-T 548
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 355 FKDLDFAEHhpngIFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIHnldLAAKEKReeRILNARAKLQRKESAAQG 434
Cdd:PLN03185 549 LKDLDLNYS----FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH---FRAPQHL--RSLLPYSRSITADGLEVV 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 435 PPSLNPDDDAPEADQNqLQAVASYASIPGTSAGAALNRTrsmnrqRLVAHSTALESI------TADMDVPLEEDEDVPAG 508
Cdd:PLN03185 620 AEEDTIEDEELSYPEG-LVLVPRGADDGSTVPGPHIRGS------RLRASAAGDEEVdlllpgTARLQIQLGVNMPARAE 692
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665402358 509 GIPARSENDERL-------ILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRPSFYAKRFQDAMgKQVF 574
Cdd:PLN03185 693 RIPGREDKEKQSfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
210-571 1.19e-80

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: 259.04  E-value: 1.19e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 210 DFRFKVYAPIAFRYFRDLFGIAPDDFLMSMCASP-LRELSN-PGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYM 287
Cdd:cd00139    2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEEnLRELKEsEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 288 NLSQNPRTLLPKFFGLYCFH-YNSKNVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKA-ERQKASPTFKDLDFAEHHP 365
Cdd:cd00139   82 HIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKEkEKKKGLKVLKDLDFLEKGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 366 nGIFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIHnldlaakekreerilnaraklqrkesaaqgppslnpdddap 445
Cdd:cd00139  162 -KIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH----------------------------------------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 446 eadqnqlqavasyasipgtsagaalnrtrsmnrqrlvahstalesitadmdvpleededvpaggiparsendeRLILYIG 525
Cdd:cd00139  200 -------------------------------------------------------------------------RLVYYLG 206
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 665402358 526 IIDILQSYRLEKKLEHTFKSILYNGDT-VSVCRPSFYAKRFQDAMGK 571
Cdd:cd00139  207 IIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
165-571 2.80e-76

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: 249.52  E-value: 2.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 165 LGIQHTVGSLASKPKRDLLMNDFWEMETISFPPDGSSITPAHHYnDFRFKVYAPIAFRYFRDLFGIAPDDFLMSMCAS-P 243
Cdd:cd17303    9 TGIRVAVSRCAAKVDRELTDADFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKyI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 244 LRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQNPRTLLPKFFGLY--CFHYNSKnVRLVAMNNL 321
Cdd:cd17303   88 LSELGSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHrvKMPRGRK-IHFVVMNNL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 322 LPSDIKMHCKYDLKGSSFRRKASKAE-RQKASPTFKDLDFAEHHPNgIFLETDKYNALMSTIKRDCMVLESFQIMDYSLL 400
Cdd:cd17303  167 FPPHRDIHQTFDLKGSTVGRETPEDKlAKGPRATLKDLNWLRRKRK-LALGPEKRKQFLTQLKRDVEFLASLNIMDYSLL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 401 VGIHNLDlaakekreerilnaraklqrkesaaqgppslnpdddapeadqnqlqavasyasipgtsagaalnrtrsmnrqr 480
Cdd:cd17303  246 VGIHDLD------------------------------------------------------------------------- 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 481 lvahstalesitadmdvpleededvpaGGIPARSENDER--LILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRP 558
Cdd:cd17303  253 ---------------------------GGFQATDENNEPgdEIYYLGIIDILTPYNAKKKLEHFFKSLRHDRHTISAVPP 305
                        410
                 ....*....|...
gi 665402358 559 SFYAKRFQDAMGK 571
Cdd:cd17303  306 KEYARRFLKFIED 318
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
159-404 6.85e-54

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: 188.63  E-value: 6.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 159 IMGSIQLGIQHTVGSLASKPKRDLLM-NDFWEMETISFppDGssitpaHHYND------FRFKVYAPIAFRYFRDLFGIA 231
Cdd:cd17305    2 LLSVFMWGINHSINELSHVPIPVMLMpDDFKAYSKIKV--DN------HLFNKenlpshFKVKEYCPLVFRNLRERFGID 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 232 PDDFLMSMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNL-SQNPRTLLPKFFGLYCFHYNS 310
Cdd:cd17305   74 DDDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIvERHGKTLLPQYLGMYRITVNG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 311 KNVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAEHHPNGIFLETDKYNaLMSTIKRDCMVLE 390
Cdd:cd17305  154 VETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAK-LLETLKRDVEFLA 232
                        250
                 ....*....|....
gi 665402358 391 SFQIMDYSLLVGIH 404
Cdd:cd17305  233 KLNLMDYSLLVGIH 246
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
156-406 5.63e-38

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: 144.04  E-value: 5.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 156 SKQIMGSIQLGIQHTVGSLASKPKRDLLM-NDFWEMETISFppDGSSITPAHHYNDFRFKVYAPIAFRYFRDLFGIAPDD 234
Cdd:cd17310   10 SEPILSVLMWGVNHTINELSNVPVPVMLMpDDFKAYSKIKV--DNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 235 FLMSMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQ-NPRTLLPKFFGLYCFHYNSKNV 313
Cdd:cd17310   88 YQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVEcHGNTLLPQFLGMYRLTVDGVET 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 314 RLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAeHHPNGIFLETDKYNALMSTIKRDCMVLESFQ 393
Cdd:cd17310  168 YMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFL-NEGQKLHVGEESKKNFLEKLKRDVEFLAQLK 246
                        250
                 ....*....|...
gi 665402358 394 IMDYSLLVGIHNL 406
Cdd:cd17310  247 IMDYSLLVGIHDV 259
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
159-406 6.80e-34

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: 131.91  E-value: 6.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 159 IMGSIQLGIQHTVGSLASKPKRDLLMNDfwemetiSFPPDGSSITPAHHYN------DFRFKVYAPIAFRYFRDLFGIAP 232
Cdd:cd17311    2 LVSVFMWGVNHSINELSQVPVPVMLLPD-------DFKANSKIKVNNHLFNrenlpsHFKFKEYCPQVFRNLRERFGIDD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 233 DDFLMSMCASPlrELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNLSQ-NPRTLLPKFFGLYCFHYNSK 311
Cdd:cd17311   75 QDYQVSLTRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKcHGNTLLPQFLGMYRLSVDNE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 312 NVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFAeHHPNGIFLETDKYNALMSTIKRDCMVLES 391
Cdd:cd17311  153 DSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFL-NKNQKVYVGEEQKRIFLEKLKRDVEFLVQ 231
                        250
                 ....*....|....*
gi 665402358 392 FQIMDYSLLVGIHNL 406
Cdd:cd17311  232 LKIMDYSLLLGIHDV 246
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
211-571 7.59e-34

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: 130.71  E-value: 7.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 211 FRFKVYAPIAFRYFRDLFGIAPDDFLMSMCASpLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGY--YM- 287
Cdd:cd17300    3 FTCTIYFAEQFHALRSLYCGGEDDFIRSLSRC-VKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfeYMa 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 288 -NLSQNPRTLLPKFFGLY-CFHYNSKN-----VRLVAMNNLLPSDiKMHCKYDLKGSSFRRKASKAERQKAspTFKDLDF 360
Cdd:cd17300   82 kALFHKRPSLLAKILGVYrISVKNSTTnktskQDLLVMENLFYGR-NISQVYDLKGSLRNRYVNVAEDEDS--VLLDENF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 361 AEHHPNG-IFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIhnldlaakekreerilnaraklqrkesaaqgppsln 439
Cdd:cd17300  159 LEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI------------------------------------ 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 440 pdddapeadqnqlqavasyasipgtsagaalnrtrsmnrqrlvahstalesitadmdvpleededvpaggiparseNDER 519
Cdd:cd17300  203 ----------------------------------------------------------------------------DEEK 206
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665402358 520 LILYIGIIDILQSYRLEKKLEHTFKSILYNGDTVS--VCRPSFYAKRFQDAMGK 571
Cdd:cd17300  207 KELVVGIIDYIRTYTWDKKLESWVKSLGILGGGGEptVISPELYKKRFREAMDK 260
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
204-406 1.08e-32

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: 128.94  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 204 PAHhyndFRFKVYAPIAFRYFRDLFGIAPDDFLMSMC-ASPLRELSNpGASGSIFYLTTDDEFIIKTVQKKECEFLQKLL 282
Cdd:cd17309   59 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTrSAPLANDSQ-ARSGARFHTSYDKRYIIKTITSEDVAEMHNIL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 283 PGYYMNLSQ-NPRTLLPKFFGLYCFHYNSKNVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKAERQKASPTFKDLDFA 361
Cdd:cd17309  134 KKYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFI 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 665402358 362 eHHPNGIFLETDKYNALMSTIKRDCMVLESFQIMDYSLLVGIHNL 406
Cdd:cd17309  214 -NDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV 257
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
210-406 4.84e-30

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 126.21  E-value: 4.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 210 DFRFKVYAPIAFRYFRDLFGIapDDFLMSMCASPLRELSNPGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMNL 289
Cdd:COG5253  335 EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHV 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 290 SQNPRTLLPKFFGLY-------CFHYNSKNVRLVAMNNLLPsDIKMHCKYDLKGSSFRR-KASKAERQKASPTFKDLDFA 361
Cdd:COG5253  413 LFNPLTLLCKIFGFYrvksrssISSSKSRKIYFIVMENLFY-PHGIHRIFDLKGSMRNRhVERTGKSMSVLLDMNDVEWI 491
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 665402358 362 EHHPNgIFLETDKyNALMSTIKRDCMVLESFQIMDYSLLVGIHNL 406
Cdd:COG5253  492 RESPK-IVFGLKK-KLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
211-565 1.92e-26

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PIP5KL1) and similar proteins; PIP5KL1 (EC 2.7.1.68), also known as PI(4)P 5-kinase-like protein 1, or PtdIns(4)P-5-kinase-like protein 1, may act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment, and conversion to PI(3,4,5)P3.


Pssm-ID: 340441  Cd Length: 319  Bit Score: 110.91  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 211 FRFKVYAPIAFRYFRDLFGIAPDDFLMSM-CASP-LRELSNpGASGSIFYLTTDDEFIIKTVQKKECEFLQKLLPGYYMN 288
Cdd:cd17304   49 FEFRTYAGPVFATLRQSLGISEKEYQNSLsPDEPyLQFISN-SKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQH 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 289 LSQNPRTLLPKFFGLYCFHY-NSKNVRLVAMNNLLPSDIKMHCKYDLKGSSFRRKASKA-ERQKASPTFKDLDFaehhpN 366
Cdd:cd17304  128 LENYPHSLLVKFLGVHSIKLpGKKKKYFIVMQSVFYPDERINERYDIKGCQVSRYTDPEpEGSQIIVVLKDLNF-----E 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 367 GIFLETDKYNA-LMSTIKRDCMVLESFQIMDYSLLVGIHNLDlaAKEKReeRILnaraklqrkesaaqgPPSLNPDD--D 443
Cdd:cd17304  203 GNSINLGQQRSwFLRQVEIDTEFLKGLNVLDYSLLVGFQPLH--SDENR--RLL---------------PNYKNALHvvD 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402358 444 APEadqnqlqavasyasipgtsagaalnrtrsmnrQRlvahstalesitadmdvpleededvpaggiparsenderliLY 523
Cdd:cd17304  264 GPE--------------------------------YR-----------------------------------------YF 270
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 665402358 524 IGIIDILQSYRLEKKLEHTFKSILYNGDTVSVCRPSFYAKRF 565
Cdd:cd17304  271 VGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRF 312
 
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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