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Conserved domains on  [gi|24658744|ref|NP_611729.2|]
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PIP5K59B, isoform A [Drosophila melanogaster]

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List of domain hits

Name Accession Description Interval E-value
PIPKc cd00139
Phosphatidylinositol phosphate kinases (PIPK) catalyze the phosphorylation of ...
77-470 1.48e-141

Phosphatidylinositol phosphate kinases (PIPK) catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. CD alignment includes type II phosphatidylinositol phosphate kinases (PIPKII-beta), type I andII PIPK (-alpha, -beta, and -gamma) kinases and related yeast Fab1p and Mss4p kinases. Signaling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling. The catalytic core domains of PIPKs are structurally similar to PI3K, PI4K, and cAMP-dependent protein kinases (PKA), the dimerization region is a unique feature of the PIPKs.


:

Pssm-ID: 238081  Cd Length: 313  Bit Score: 420.55  E-value: 1.48e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  77 TSQIMGSIQLGIQHTVGSLASKPK-RDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDD 155
Cdd:cd00139   1 SYPLMSNLQLGIRHSVGELSSVPSpRDLLPDDFKAKSKIKFPNHGSHLTPPHLSADFKFKDYCPEVFRALRELFGIDEAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 156 FMMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNP-RTLLPKFFGLYCLQTSNA-- 232
Cdd:cd00139  81 YLRSLCRSPLWELSSGGKSGSFFYKTLDDRFIIKTVSHSEIESLLKFLPNYYEYITQNPqNTLLPKFFGLYRVKVKSGtg 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 233 KNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLE 312
Cdd:cd00139 161 KKVDFLVMENLFYSRLKIHRKYDLKGSTRNREASKKEKQKENPVLKDLNLLEMIEQPLFVGEHSKKALLTQIKRDCEFLE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 313 SFKIMDYSLLLGVHNldvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaes 392
Cdd:cd00139 241 SLNIMDYSLLVGIHD----------------------------------------------------------------- 255
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658744 393 epiddeedvppggiparsekgERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGE-TVSVCRPSFYAQRFQNFMAKTVF 470
Cdd:cd00139 256 ---------------------IRLVLYLGIIDILRTYTWDKKLEHWVKSLGHDGGkTPSVVSPEQYAKRFREFMDKYFL 313
 
Name Accession Description Interval E-value
PIPKc cd00139
Phosphatidylinositol phosphate kinases (PIPK) catalyze the phosphorylation of ...
77-470 1.48e-141

Phosphatidylinositol phosphate kinases (PIPK) catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. CD alignment includes type II phosphatidylinositol phosphate kinases (PIPKII-beta), type I andII PIPK (-alpha, -beta, and -gamma) kinases and related yeast Fab1p and Mss4p kinases. Signaling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling. The catalytic core domains of PIPKs are structurally similar to PI3K, PI4K, and cAMP-dependent protein kinases (PKA), the dimerization region is a unique feature of the PIPKs.


Pssm-ID: 238081  Cd Length: 313  Bit Score: 420.55  E-value: 1.48e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  77 TSQIMGSIQLGIQHTVGSLASKPK-RDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDD 155
Cdd:cd00139   1 SYPLMSNLQLGIRHSVGELSSVPSpRDLLPDDFKAKSKIKFPNHGSHLTPPHLSADFKFKDYCPEVFRALRELFGIDEAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 156 FMMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNP-RTLLPKFFGLYCLQTSNA-- 232
Cdd:cd00139  81 YLRSLCRSPLWELSSGGKSGSFFYKTLDDRFIIKTVSHSEIESLLKFLPNYYEYITQNPqNTLLPKFFGLYRVKVKSGtg 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 233 KNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLE 312
Cdd:cd00139 161 KKVDFLVMENLFYSRLKIHRKYDLKGSTRNREASKKEKQKENPVLKDLNLLEMIEQPLFVGEHSKKALLTQIKRDCEFLE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 313 SFKIMDYSLLLGVHNldvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaes 392
Cdd:cd00139 241 SLNIMDYSLLVGIHD----------------------------------------------------------------- 255
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658744 393 epiddeedvppggiparsekgERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGE-TVSVCRPSFYAQRFQNFMAKTVF 470
Cdd:cd00139 256 ---------------------IRLVLYLGIIDILRTYTWDKKLEHWVKSLGHDGGkTPSVVSPEQYAKRFREFMDKYFL 313
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
104-469 4.15e-146

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623  Cd Length: 342  Bit Score: 433.35  E-value: 4.15e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    104 LMMDFWEIESITFPPEGSS-LTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPLRELSNPGASGSIFYLTT 182
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHLeLTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    183 DDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSN--AKNIRLVVMNNLLPSSVKMHLKYDLKGST 260
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgtEKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    261 FKRKANKaERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNLDVALKEKqseqr 340
Cdd:smart00330 161 RGREADK-KKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREE----- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    341 kplraplAEDSDVDADDPLDGDaatgisrnksvnrqRLVAHSTAMESIQAESEPIDDEEDVPPGGIPARSEKGERLLLYI 420
Cdd:smart00330 235 -------IELPPVYGSDESPSS--------------ESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYL 293
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 24658744    421 GIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTV 469
Cdd:smart00330 294 GIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
159-469 1.02e-101

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 catalyses the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signaling pathway.


Pssm-ID: 250669  Cd Length: 254  Bit Score: 314.98  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   159 SMCT-SPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSN-AKNIR 236
Cdd:pfam01504   1 SLCSlWTLSELSSGGKSGSFFYKSRDDRFIIKTIKKSEVKFLLKFLPAYFEHVKENPNTLLPKFYGLYRVKPSGgEKKIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   237 LVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKkspTYKDLDFMEQHpNGIFLEAETYAALIKTIQRDCTVLESFKI 316
Cdd:pfam01504  81 FVVMENLFYSPRKIHRKYDLKGSTVGREVSKKEKEK---VLKDLDFLEDG-QPIFLGPEKKKLLLEQLKRDTEFLESLNI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   317 MDYSLLLGVHNLDvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstaMESIQAESEPID 396
Cdd:pfam01504 157 MDYSLLVGIHEVE-------------------------------------------------------TEDLEEGSAEAD 181
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24658744   397 DEEDVPPGGIPARSEKgERLLLYIGIIDILQSYRLKKKLEHTFKSII-HDGETVSVCRPSFYAQRFQNFMAKTV 469
Cdd:pfam01504 182 GEFDLSEGGIRAGDDP-ENEIYYIGIIDILTPYTWDKKLEHFVKSLLyLDGKTISIVPPKEYAKRFLKFIEKYF 254
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
42-470 5.96e-85

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 286.34  E-value: 5.96e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   42 LGNRPNRASSKADKERKIGHRRVGEGGEITYKKIQTSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESI--TFPPE 119
Cdd:PLN03185 312 LNNSFSSTSRRAKRRQKKLVKEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFwmNFPKA 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  120 GSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMC-TSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEF 198
Cdd:PLN03185 392 GSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKV 471
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  199 LQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAErAKKSPTYK 278
Cdd:PLN03185 472 LLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVE-IDENTTLK 550
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  279 DLDFMEQhpngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVH-----NLDVALKEKQSEQRKPLRAPLAEDS-D 352
Cdd:PLN03185 551 DLDLNYS----FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqHLRSLLPYSRSITADGLEVVAEEDTiE 626
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  353 VDADDPLDGDAatgisrnksvnrqrLVAHSTAMES----IQAESEPI------DDEED-VPPG----------GIPARSE 411
Cdd:PLN03185 627 DEELSYPEGLV--------------LVPRGADDGStvpgPHIRGSRLrasaagDEEVDlLLPGtarlqiqlgvNMPARAE 692
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24658744  412 K------GER--------LLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMaKTVF 470
Cdd:PLN03185 693 RipgredKEKqsfhevydVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
47-328 1.03e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 132.76  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  47 NRASSKADKERKIGHRRVgEGGEITYkkiQTSQIMGSiqlGIQHTVGslaskpkrdllmmdfwEIESITFPPEGSSL--- 123
Cdd:COG5253 272 RLRDSETMDERLLNGMPL-EGGHRNP---QESYNMLT---GIRVTLS----------------RIEEIMIKKTDTHLneq 328
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 124 TPAHHYsEFRYKIYAPIAFRYFRDLFGIQPDdFMMSMCTSPLRElSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLL 203
Cdd:COG5253 329 FEEGLY-EFSCKDYFPEVFRELRALCGCDEA-LVSLLSRYILWE-SNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMI 405
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 204 PGYYMNLNQNPRTLLPKFFGLYCLQ------TSNAKNIRLVVMNNLLPSSvKMHLKYDLKGSTFKRKANKAERAKKS-PT 276
Cdd:COG5253 406 FEYYVHVLFNPLTLLCKIFGFYRVKsrssisSSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKSMSVlLD 484
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 24658744 277 YKDLDFMEQHPngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNL 328
Cdd:COG5253 485 MNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
 
Name Accession Description Interval E-value
PIPKc cd00139
Phosphatidylinositol phosphate kinases (PIPK) catalyze the phosphorylation of ...
77-470 1.48e-141

Phosphatidylinositol phosphate kinases (PIPK) catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. CD alignment includes type II phosphatidylinositol phosphate kinases (PIPKII-beta), type I andII PIPK (-alpha, -beta, and -gamma) kinases and related yeast Fab1p and Mss4p kinases. Signaling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling. The catalytic core domains of PIPKs are structurally similar to PI3K, PI4K, and cAMP-dependent protein kinases (PKA), the dimerization region is a unique feature of the PIPKs.


Pssm-ID: 238081  Cd Length: 313  Bit Score: 420.55  E-value: 1.48e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  77 TSQIMGSIQLGIQHTVGSLASKPK-RDLLMMDFWEIESITFPPEGSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDD 155
Cdd:cd00139   1 SYPLMSNLQLGIRHSVGELSSVPSpRDLLPDDFKAKSKIKFPNHGSHLTPPHLSADFKFKDYCPEVFRALRELFGIDEAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 156 FMMSMCTSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNP-RTLLPKFFGLYCLQTSNA-- 232
Cdd:cd00139  81 YLRSLCRSPLWELSSGGKSGSFFYKTLDDRFIIKTVSHSEIESLLKFLPNYYEYITQNPqNTLLPKFFGLYRVKVKSGtg 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 233 KNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLE 312
Cdd:cd00139 161 KKVDFLVMENLFYSRLKIHRKYDLKGSTRNREASKKEKQKENPVLKDLNLLEMIEQPLFVGEHSKKALLTQIKRDCEFLE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 313 SFKIMDYSLLLGVHNldvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstamesiqaes 392
Cdd:cd00139 241 SLNIMDYSLLVGIHD----------------------------------------------------------------- 255
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658744 393 epiddeedvppggiparsekgERLLLYIGIIDILQSYRLKKKLEHTFKSIIHDGE-TVSVCRPSFYAQRFQNFMAKTVF 470
Cdd:cd00139 256 ---------------------IRLVLYLGIIDILRTYTWDKKLEHWVKSLGHDGGkTPSVVSPEQYAKRFREFMDKYFL 313
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
104-469 4.15e-146

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623  Cd Length: 342  Bit Score: 433.35  E-value: 4.15e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    104 LMMDFWEIESITFPPEGSS-LTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMCTSPLRELSNPGASGSIFYLTT 182
Cdd:smart00330   1 LPSDFKATEKIKFPTPGHLeLTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    183 DDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSN--AKNIRLVVMNNLLPSSVKMHLKYDLKGST 260
Cdd:smart00330  81 DDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGgtEKKIYFLVMENLFYSDLKVHRKYDLKGST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    261 FKRKANKaERAKKSPTYKDLDFMEQHPNGIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNLDVALKEKqseqr 340
Cdd:smart00330 161 RGREADK-KKVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREE----- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744    341 kplraplAEDSDVDADDPLDGDaatgisrnksvnrqRLVAHSTAMESIQAESEPIDDEEDVPPGGIPARSEKGERLLLYI 420
Cdd:smart00330 235 -------IELPPVYGSDESPSS--------------ESSNGGKAPDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYL 293
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 24658744    421 GIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMAKTV 469
Cdd:smart00330 294 GIIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
159-469 1.02e-101

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 catalyses the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signaling pathway.


Pssm-ID: 250669  Cd Length: 254  Bit Score: 314.98  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   159 SMCT-SPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSN-AKNIR 236
Cdd:pfam01504   1 SLCSlWTLSELSSGGKSGSFFYKSRDDRFIIKTIKKSEVKFLLKFLPAYFEHVKENPNTLLPKFYGLYRVKPSGgEKKIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   237 LVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAERAKkspTYKDLDFMEQHpNGIFLEAETYAALIKTIQRDCTVLESFKI 316
Cdd:pfam01504  81 FVVMENLFYSPRKIHRKYDLKGSTVGREVSKKEKEK---VLKDLDFLEDG-QPIFLGPEKKKLLLEQLKRDTEFLESLNI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   317 MDYSLLLGVHNLDvalkekqseqrkplraplaedsdvdaddpldgdaatgisrnksvnrqrlvahstaMESIQAESEPID 396
Cdd:pfam01504 157 MDYSLLVGIHEVE-------------------------------------------------------TEDLEEGSAEAD 181
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24658744   397 DEEDVPPGGIPARSEKgERLLLYIGIIDILQSYRLKKKLEHTFKSII-HDGETVSVCRPSFYAQRFQNFMAKTV 469
Cdd:pfam01504 182 GEFDLSEGGIRAGDDP-ENEIYYIGIIDILTPYTWDKKLEHFVKSLLyLDGKTISIVPPKEYAKRFLKFIEKYF 254
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
42-470 5.96e-85

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 286.34  E-value: 5.96e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744   42 LGNRPNRASSKADKERKIGHRRVGEGGEITYKKIQTSQIMGSIQLGIQHTVGSLASKPKRDLLMMDFWEIESI--TFPPE 119
Cdd:PLN03185 312 LNNSFSSTSRRAKRRQKKLVKEIKRPGETIIKGHRSYDLMLSLQLGIRYTVGKITPIQRREVRPSDFGPRASFwmNFPKA 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  120 GSSLTPAHHYSEFRYKIYAPIAFRYFRDLFGIQPDDFMMSMC-TSPLRELSNPGASGSIFYLTTDDEFIIKTVQHKEGEF 198
Cdd:PLN03185 392 GSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKSEVKV 471
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  199 LQKLLPGYYMNLNQNPRTLLPKFFGLYCLQTSNAKNIRLVVMNNLLPSSVKMHLKYDLKGSTFKRKANKAErAKKSPTYK 278
Cdd:PLN03185 472 LLRMLPDYHHHVKTYENTLITKFFGLHRIKPSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVE-IDENTTLK 550
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  279 DLDFMEQhpngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVH-----NLDVALKEKQSEQRKPLRAPLAEDS-D 352
Cdd:PLN03185 551 DLDLNYS----FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqHLRSLLPYSRSITADGLEVVAEEDTiE 626
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  353 VDADDPLDGDAatgisrnksvnrqrLVAHSTAMES----IQAESEPI------DDEED-VPPG----------GIPARSE 411
Cdd:PLN03185 627 DEELSYPEGLV--------------LVPRGADDGStvpgPHIRGSRLrasaagDEEVDlLLPGtarlqiqlgvNMPARAE 692
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24658744  412 K------GER--------LLLYIGIIDILQSYRLKKKLEHTFKSIIHDGETVSVCRPSFYAQRFQNFMaKTVF 470
Cdd:PLN03185 693 RipgredKEKqsfhevydVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
47-328 1.03e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 132.76  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744  47 NRASSKADKERKIGHRRVgEGGEITYkkiQTSQIMGSiqlGIQHTVGslaskpkrdllmmdfwEIESITFPPEGSSL--- 123
Cdd:COG5253 272 RLRDSETMDERLLNGMPL-EGGHRNP---QESYNMLT---GIRVTLS----------------RIEEIMIKKTDTHLneq 328
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 124 TPAHHYsEFRYKIYAPIAFRYFRDLFGIQPDdFMMSMCTSPLRElSNPGASGSIFYLTTDDEFIIKTVQHKEGEFLQKLL 203
Cdd:COG5253 329 FEEGLY-EFSCKDYFPEVFRELRALCGCDEA-LVSLLSRYILWE-SNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMI 405
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658744 204 PGYYMNLNQNPRTLLPKFFGLYCLQ------TSNAKNIRLVVMNNLLPSSvKMHLKYDLKGSTFKRKANKAERAKKS-PT 276
Cdd:COG5253 406 FEYYVHVLFNPLTLLCKIFGFYRVKsrssisSSKSRKIYFIVMENLFYPH-GIHRIFDLKGSMRNRHVERTGKSMSVlLD 484
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 24658744 277 YKDLDFMEQHPngIFLEAETYAALIKTIQRDCTVLESFKIMDYSLLLGVHNL 328
Cdd:COG5253 485 MNDVEWIRESP--KIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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