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Conserved domains on  [gi|17298686|ref|NP_473438|]
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phosphatidylinositol 5-phosphate 4-kinase type-2 gamma [Mus musculus]

Protein Classification

phosphatidylinositol 5-phosphate 4-kinase type-2 gamma( domain architecture ID 13022741)

phosphatidylinositol 5-phosphate 4-kinase type-2 gamma displays low enzymatic activity, and may be a GTP sensor; it has higher GTP-dependent kinase activity than ATP-dependent kinase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
46-418 0e+00

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: 532.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHFFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVS 125
Cdd:cd17311   1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 126 LTRSPP-SETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMR 204
Cdd:cd17311  81 LTRSPPySESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 205 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLL 284
Cdd:cd17311 161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 285 LGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidvyairsaegapq 364
Cdd:cd17311 241 LGIHDV-------------------------------------------------------------------------- 246
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17298686 365 keVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17311 247 --VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
 
Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
46-418 0e+00

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: 532.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHFFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVS 125
Cdd:cd17311   1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 126 LTRSPP-SETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMR 204
Cdd:cd17311  81 LTRSPPySESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 205 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLL 284
Cdd:cd17311 161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 285 LGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidvyairsaegapq 364
Cdd:cd17311 241 LGIHDV-------------------------------------------------------------------------- 246
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17298686 365 keVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17311 247 --VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
72-420 1.74e-137

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 397.14  E-value: 1.74e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686     72 LPDDFKASSKIKVNNHFfHRENLPSH----FKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSE---TEGSDGRFLIS 144
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLElssGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686    145 YDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHgNTLLPQFLGMYRVSVENE---DSYMLVMRNMFSHRLPVHRKYDLKG 221
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686    222 SLVSREAsDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEG 300
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686    301 PVREEESEWDGDCNLAGPPAlvgsygtsPEGIGGYIHSHRPLGPGEFESfIDVYAIRSAEgapqkEVYFMGLIDILTQYD 380
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKA--------PDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYT 303
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 17298686    381 AKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIANIF 420
Cdd:smart00330 304 WDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
125-419 5.43e-65

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: 207.70  E-value: 5.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   125 SLTRSPPSE--TEG-SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVENEDSYML 201
Cdd:pfam01504   1 LTGKSILSElsSPGkSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   202 VMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMD 280
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   281 YSLLLGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidvyairsae 360
Cdd:pfam01504 160 YSLLLGIHDL---------------------------------------------------------------------- 169
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17298686   361 GAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIANI 419
Cdd:pfam01504 170 DEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
73-420 6.69e-41

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 154.61  E-value: 6.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   73 PDDFKASSKIKVNnhfFHREN---LPSH----FKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGR----F 141
Cdd:PLN03185 375 PSDFGPRASFWMN---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKsgsvF 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  142 LISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSVENEDSY-MLVMRNMFSHRLPVHRKYDLK 220
Cdd:PLN03185 452 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLK 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  221 GSLVSREAsDKEKVKELPTLKDMDFlnkNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHdiIRGSEPEEEG 300
Cdd:PLN03185 531 GSSLGRSA-DKVEIDENTTLKDLDL---NYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRAPQHLRSL 604
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  301 PVREEESEWDGDCNLAGPPALVGSYGTSPEGI--------------GGYIHSHR------------PLGPGEFESFID-- 352
Cdd:PLN03185 605 LPYSRSITADGLEVVAEEDTIEDEELSYPEGLvlvprgaddgstvpGPHIRGSRlrasaagdeevdLLLPGTARLQIQlg 684
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  353 VYAIRSAEGAPQKE-------------VYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHPEQYAKRFLDFIANI 419
Cdd:PLN03185 685 VNMPARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763

                 .
gi 17298686  420 F 420
Cdd:PLN03185 764 F 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
91-290 1.07e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 130.07  E-value: 1.07e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  91 RENLPS---HFKFKEYCPQVFRNLRDRFAIDDHdyLVSLT-RSPPSETEG--SDGRFLISYDRTLVIKEVSSEDIADMHS 164
Cdd:COG5253 326 NEQFEEglyEFSCKDYFPEVFRELRALCGCDEA--LVSLLsRYILWESNGgkSGSFFLFTRDYKFIIKTISHSEHICFRP 403
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 165 NLSNYHQYiVKCHGNTLLPQFLGMYRVSVENEDS-------YMLVMRNMFSHRLPvHRKYDLKGSLVSREASDKEKVKE- 236
Cdd:COG5253 404 MIFEYYVH-VLFNPLTLLCKIFGFYRVKSRSSISssksrkiYFIVMENLFYPHGI-HRIFDLKGSMRNRHVERTGKSMSv 481
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17298686 237 LPTLKDMDFLNKNQKVYIGEEeKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDI 290
Cdd:COG5253 482 LLDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
 
Name Accession Description Interval E-value
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
46-418 0e+00

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: 532.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHFFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVS 125
Cdd:cd17311   1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 126 LTRSPP-SETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMR 204
Cdd:cd17311  81 LTRSPPySESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLVMR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 205 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLL 284
Cdd:cd17311 161 NMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 285 LGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidvyairsaegapq 364
Cdd:cd17311 241 LGIHDV-------------------------------------------------------------------------- 246
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17298686 365 keVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17311 247 --VYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITN 298
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
46-418 0e+00

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: 508.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  46 PLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHFFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVS 125
Cdd:cd17305   1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 126 LTRSPPSETEG---SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLV 202
Cdd:cd17305  81 LTRSQPLASDSpgrSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 203 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYS 282
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 283 LLLGIHDIIrgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidvyairsaega 362
Cdd:cd17305 241 LLVGIHDCI----------------------------------------------------------------------- 249
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17298686 363 pqkevYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17305 250 -----YFMAIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
36-418 6.90e-166

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: 467.99  E-value: 6.90e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  36 QKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHFFHRENLPSHFKFKEYCPQVFRNLRDRF 115
Cdd:cd17310   2 QKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 116 AIDDHDYLVSLTRSPP--SETEGSDG-RFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVS 192
Cdd:cd17310  82 GIDDQDYQNSVTRSAPinSDSQGRCGtRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 193 VENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEF 272
Cdd:cd17310 162 VDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEF 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 273 LVQLKIMDYSLLLGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfid 352
Cdd:cd17310 242 LAQLKIMDYSLLVGIHDV-------------------------------------------------------------- 259
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17298686 353 vyairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17310 260 --------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
37-418 6.47e-154

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: 437.49  E-value: 6.47e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  37 KVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHFFHRENLPSHFKFKEYCPQVFRNLRDRFA 116
Cdd:cd17309   1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 117 IDDHDYLVSLTRSPP--SETEGSDG-RFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSV 193
Cdd:cd17309  81 IDDQDFQNSLTRSAPlaNDSQARSGaRFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 194 ENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFL 273
Cdd:cd17309 161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 274 VQLKIMDYSLLLGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidv 353
Cdd:cd17309 241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17298686 354 yairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17309 258 -------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
72-420 1.74e-137

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 397.14  E-value: 1.74e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686     72 LPDDFKASSKIKVNNHFfHRENLPSH----FKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSE---TEGSDGRFLIS 144
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLElssGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686    145 YDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHgNTLLPQFLGMYRVSVENE---DSYMLVMRNMFSHRLPVHRKYDLKG 221
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686    222 SLVSREAsDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEG 300
Cdd:smart00330 159 STRGREA-DKKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686    301 PVREEESEWDGDCNLAGPPAlvgsygtsPEGIGGYIHSHRPLGPGEFESfIDVYAIRSAEgapqkEVYFMGLIDILTQYD 380
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKA--------PDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYT 303
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 17298686    381 AKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIANIF 420
Cdd:smart00330 304 WDKKLEHWVKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
97-418 4.19e-75

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family includes phosphatidylinositol 5-phosphate 4-kinases (PIP5Ks) and similar proteins. PIP5Ks catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate. The family includes type I and II PIP5Ks (-alpha, -beta, and -gamma) kinases. Signalling by phosphorylated species of phosphatidylinositol regulates secretion, vesicular trafficking, membrane translocation, cell adhesion, chemotaxis, DNA synthesis, and cell cycling.


Pssm-ID: 340436  Cd Length: 253  Bit Score: 234.39  E-value: 4.19e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  97 HFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPP----SETEG-SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQ 171
Cdd:cd00139   2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENlrelKESEGkSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 172 YIVKcHGNTLLPQFLGMYRVSVENEDS-YMLVMRNMFSHRLPVHRKYDLKGSLVSREAS-DKEKVKELPTLKDMDFLNKN 249
Cdd:cd00139  82 HIKK-NPNSLLTRFYGLYSIKLQKGKKvYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 250 QKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtsp 329
Cdd:cd00139 161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 330 egiggyihshrplgpgefesfidvyairsaegapqkeVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYA 409
Cdd:cd00139 202 -------------------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYA 244

                ....*....
gi 17298686 410 KRFLDFIAN 418
Cdd:cd00139 245 ERFLKFMES 253
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
71-418 3.69e-66

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: 213.70  E-value: 3.69e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  71 LLPDDFKASSKIKVNNHffHRENLPSH---FKFKEYCPQVFRNLRDRFAIDDHDYLVSLT-RSPPSETeGSDGR----FL 142
Cdd:cd17303  26 LTDADFKAVHKFSFDIT--GNELTPSSkydFKFKDYAPWVFRFLRELFGIDPADYLMSLTgKYILSEL-GSPGKsgsfFY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 143 ISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSV-ENEDSYMLVMRNMFSHRLPVHRKYDLKG 221
Cdd:cd17303 103 FSRDYRFIIKTIHHSEHKFLRKILPDYYNH-VKENPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 222 SLVSREAS-DKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDiirgsepeeeg 300
Cdd:cd17303 182 STVGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHD----------- 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 301 pvreeesewdgdcnlagppalvgsygtspegIGGYIHShrplgpgefesfidvyaiRSAEGAPQKEVYFMGLIDILTQYD 380
Cdd:cd17303 251 -------------------------------LDGGFQA------------------TDENNEPGDEIYYLGIIDILTPYN 281
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 17298686 381 AKKKAAHAAKTVKHgAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17303 282 AKKKLEHFFKSLRH-DRHTISAVPPKEYARRFLKFIED 318
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
125-419 5.43e-65

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: 207.70  E-value: 5.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   125 SLTRSPPSE--TEG-SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVENEDSYML 201
Cdd:pfam01504   1 LTGKSILSElsSPGkSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   202 VMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPT-LKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMD 280
Cdd:pfam01504  80 VMNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   281 YSLLLGIHDIirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihshrplgpgefesfidvyairsae 360
Cdd:pfam01504 160 YSLLLGIHDL---------------------------------------------------------------------- 169
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17298686   361 GAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIANI 419
Cdd:pfam01504 170 DEDGKEIYYLGIIDILTEYNLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
54-418 1.89e-52

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: 178.21  E-value: 1.89e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  54 GVAHSINELSQVPPpVMLLPDDFKASSKIkvnnhFFHRE---NLPSH----FKFKEYCPQVFRNLRDRFAIDDHDYLVSL 126
Cdd:cd17301  10 GIGHSVGSLSSKPE-RDVLMQDFEVVESV-----FFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGIKPDDYLLSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 127 TRSPPSE--TEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVENEDSYMLVM 203
Cdd:cd17301  84 CNEPLRElsNPGASGSlFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQSGGKNIRFVVM 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 204 RNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEK-LKRDVEFLVQLKIMDYS 282
Cdd:cd17301 163 NNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKtIQRDCRVLESFKIMDYS 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 283 LLLGIHdiirgsepeeegpvreeesewdgdcNLAGPPAlvgsygtspegiggyihshrplgpgefesfidvyaiRSAEGa 362
Cdd:cd17301 243 LLLGVH-------------------------NLGGIPA------------------------------------RNSKG- 260
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17298686 363 pQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17301 261 -ERLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMAN 314
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
54-419 1.70e-48

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: 167.47  E-value: 1.70e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  54 GVAHSINELSQVPPpVMLLPDDFkaSSKIKVnnHFF---HRENLPSH----FKFKEYCPQVFRNLRDRFAIDDHDYLVSL 126
Cdd:cd17302  11 GIRYSVGKIAPVAR-RDLKPSDF--DPKAKQ--WFPfpgSGSTPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 127 T-----RSPPSetEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRV-SVENEDSY 199
Cdd:cd17302  86 CgddalRELSS--PGKSGSvFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH-VKAYENTLLTKFFGVHRVkPVGGRKVR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 200 MLVMRNMFSHRLPVHRKYDLKGSLVSREAS-DKEKVKELPTLKDMDFlnkNQKVYIGEEEKKVFLEKLKRDVEFLVQLKI 278
Cdd:cd17302 163 FVVMGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNTTLKDLDL---DFKFRLEKGWRDALMRQIDADCAFLEALRI 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 279 MDYSLLLGIHdiirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyihsHRPLGPGefesfidvyairs 358
Cdd:cd17302 240 MDYSLLLGVH--------------------------------------------------FRAGDST------------- 256
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17298686 359 aeGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAeISTVHPEQYAKRFLDFIANI 419
Cdd:cd17302 257 --GEPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSRRFRDFIRKV 314
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
73-420 6.69e-41

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 154.61  E-value: 6.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686   73 PDDFKASSKIKVNnhfFHREN---LPSH----FKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGR----F 141
Cdd:PLN03185 375 PSDFGPRASFWMN---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRELSSPGKsgsvF 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  142 LISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSVENEDSY-MLVMRNMFSHRLPVHRKYDLK 220
Cdd:PLN03185 452 FLSQDDRFMIKTLRKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKPSSGQKFrFVVMGNMFCTELRIHRRFDLK 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  221 GSLVSREAsDKEKVKELPTLKDMDFlnkNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHdiIRGSEPEEEG 300
Cdd:PLN03185 531 GSSLGRSA-DKVEIDENTTLKDLDL---NYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVH--FRAPQHLRSL 604
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  301 PVREEESEWDGDCNLAGPPALVGSYGTSPEGI--------------GGYIHSHR------------PLGPGEFESFID-- 352
Cdd:PLN03185 605 LPYSRSITADGLEVVAEEDTIEDEELSYPEGLvlvprgaddgstvpGPHIRGSRlrasaagdeevdLLLPGTARLQIQlg 684
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  353 VYAIRSAEGAPQKE-------------VYFMGLIDILTQYDAKKKAAHAAKTVKHGAgAEISTVHPEQYAKRFLDFIANI 419
Cdd:PLN03185 685 VNMPARAERIPGREdkekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFIQKV 763

                 .
gi 17298686  420 F 420
Cdd:PLN03185 764 F 764
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
47-416 2.44e-39

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: 143.59  E-value: 2.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  47 LVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKikvnnhFFHRE--NL-PSH----FKFKEYCPQVFRNLRDRFAIDD 119
Cdd:cd17307   3 IKGAIQLGIGYTVGNLTSKPDRDVLMQDFYVVESV------FLPSEgsNLtPAHhypdFRFKTYAPLAFRYFRELFGIKP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 120 HDYLVSLTRSPPSE--TEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVENE 196
Cdd:cd17307  77 DDYLYSICSEPLIElsNPGASGSlFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCMQSGGI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 197 DSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQK-VYIGEEEKKVFLEKLKRDVEFLVQ 275
Cdd:cd17307 156 NIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQDMHDgLYFDPETYNALMKTLQRDCRVLES 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 276 LKIMDYSLLLGIHdiirgsepeeegpvreeesewdgdcNLAGPPAlvgsygtspegiggyiHSHRplgpGEfesfidvya 355
Cdd:cd17307 236 FKIMDYSLLLGIH-------------------------VLGGIPA----------------KNHK----GE--------- 261
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17298686 356 irsaegapqKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFI 416
Cdd:cd17307 262 ---------KLLLFMGIIDILQSYRLMKKLEHSWKALVYD-GDTVSVHRPSFYADRFLKFM 312
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
47-419 5.66e-38

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: 140.13  E-value: 5.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  47 LVGVFLWGVAHSINELSQVPPPVMLLPDDFKasskikVNNHFFHRE--NL-PSH----FKFKEYCPQVFRNLRDRFAIDD 119
Cdd:cd17308   4 LKGAIQLGIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhypdFRFKTYAPVAFRYFRELFGIRP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 120 HDYLVSLTRSPPSE--TEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVENE 196
Cdd:cd17308  78 DDYLYSLCNEPLIElsNPGASGSlFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQSGGK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 197 DSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKVFLEKLKRDVEFLVQ 275
Cdd:cd17308 157 NIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLVLES 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 276 LKIMDYSLLLGIHdiirgsepeeegpvreeesewdgdcNLAGPPALvgsygtspegiggyihshrplgpgefesfidvya 355
Cdd:cd17308 237 FKIMDYSLLLGVH-------------------------NIGGIPAV---------------------------------- 257
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17298686 356 irsaEGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIANI 419
Cdd:cd17308 258 ----NGKGERLLLYIGIIDILQSYRLIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSNT 316
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
47-418 1.14e-37

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: 139.36  E-value: 1.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  47 LVGVFLWGVAHSINELSQVPPPVMLLPDDFKasskikVNNHFFHRE--NL-PSH----FKFKEYCPQVFRNLRDRFAIDD 119
Cdd:cd17306   6 LKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEgsNLtPAHhyndFRFKTYAPVAFRYFRELFGIRP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 120 HDYLVSLTRSPPSE--TEGSDGR-FLISYDRTLVIKEVSSEDIADMHSNLSNYHQYiVKCHGNTLLPQFLGMYRVSVENE 196
Cdd:cd17306  80 DDYLYSLCSEPLIElsNSGASGSlFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMN-LNQNPRTLLPKFYGLYCVQAGGK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 197 DSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNK-NQKVYIGEEEKKVFLEKLKRDVEFLVQ 275
Cdd:cd17306 159 NIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLVLQS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 276 LKIMDYSLLLGIHDI--IRGSEPeeegpvreeesewDGDCNLAGPPAlvgsygtspegiggyihshrplgpgefesfidv 353
Cdd:cd17306 239 FKIMDYSLLVGIHNIdaRRGGTI-------------ETDDQMGGIPA--------------------------------- 272
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17298686 354 yaiRSAEGapQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17306 273 ---RNSKG--ERLLLYIGIIDILQSYRFVKKLEHSWKALVHD-GDTVSVHRPGFYAERFQRFMCN 331
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
108-287 1.27e-33

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: 126.47  E-value: 1.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 108 FRNLRDRFAIDDHDYLVSLTRSPPSETEG--SDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGN---TLL 182
Cdd:cd17300  13 FHALRSLYCGGEDDFIRSLSRCVKWDASGgkSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHkrpSLL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 183 PQFLGMYRVSVENEDS------YMLVMRNMFsHRLPVHRKYDLKGSLVSREASDKEKVKElpTLKDMDFLN--KNQKVYI 254
Cdd:cd17300  93 AKILGVYRISVKNSTTnktskqDLLVMENLF-YGRNISQVYDLKGSLRNRYVNVAEDEDS--VLLDENFLEytKGSPLYL 169
                       170       180       190
                ....*....|....*....|....*....|...
gi 17298686 255 GEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGI 287
Cdd:cd17300 170 REHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
91-290 1.07e-32

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 130.07  E-value: 1.07e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  91 RENLPS---HFKFKEYCPQVFRNLRDRFAIDDHdyLVSLT-RSPPSETEG--SDGRFLISYDRTLVIKEVSSEDIADMHS 164
Cdd:COG5253 326 NEQFEEglyEFSCKDYFPEVFRELRALCGCDEA--LVSLLsRYILWESNGgkSGSFFLFTRDYKFIIKTISHSEHICFRP 403
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 165 NLSNYHQYiVKCHGNTLLPQFLGMYRVSVENEDS-------YMLVMRNMFSHRLPvHRKYDLKGSLVSREASDKEKVKE- 236
Cdd:COG5253 404 MIFEYYVH-VLFNPLTLLCKIFGFYRVKSRSSISssksrkiYFIVMENLFYPHGI-HRIFDLKGSMRNRHVERTGKSMSv 481
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17298686 237 LPTLKDMDFLNKNQKVYIGEEeKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDI 290
Cdd:COG5253 482 LLDMNDVEWIRESPKIVFGLK-KKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDE 534
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
54-418 5.20e-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: 107.06  E-value: 5.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686  54 GVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHffhrenlpSHFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPS- 132
Cdd:cd17304  13 GLRAAIQNSIDVPPKESLSDDDYTEVLTQVIPKH--------KGFEFRTYAGPVFATLRQSLGISEKEYQNSLSPDEPYl 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 133 ---ETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKcHGNTLLPQFLGMYRVSVE-NEDSYMLVMRNMFS 208
Cdd:cd17304  85 qfiSNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHLEN-YPHSLLVKFLGVHSIKLPgKKKKYFIVMQSVFY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 209 HRLPVHRKYDLKGSLVSR-EASDKEKVKELPTLKDMDFLNKnqKVYIGEEeKKVFLEKLKRDVEFLVQLKIMDYSLLLGI 287
Cdd:cd17304 164 PDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNFEGN--SINLGQQ-RSWFLRQVEIDTEFLKGLNVLDYSLLVGF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17298686 288 HDiirgsepeeegpvreeesewdgdcnlagppalvgsygtspegiggyIHS--HRPLGPGEFEsfidvyAIRSAEGAPQK 365
Cdd:cd17304 241 QP----------------------------------------------LHSdeNRRLLPNYKN------ALHVVDGPEYR 268
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 17298686 366 evYFMGLIDILTQYDAKKKAAHAAKTVKHgAGAEISTVHPEQYAKRFLDFIAN 418
Cdd:cd17304 269 --YFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWVED 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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