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Conserved domains on  [gi|12848794|dbj|BAB28093|]
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unnamed protein product [Mus musculus]

Protein Classification

phosphatidylinositol 5-phosphate 4-kinase type-2 alpha( domain architecture ID 13022738)

phosphatidylinositol 5-phosphate 4-kinase type-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)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-403 0e+00

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: 588.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309   1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNV 186
Cdd:cd17309  81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 187 DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFL 266
Cdd:cd17309 161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 267 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchen 346
Cdd:cd17309 241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12848794 347 aprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 403
Cdd:cd17309 258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-403 0e+00

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: 588.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309   1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNV 186
Cdd:cd17309  81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 187 DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFL 266
Cdd:cd17309 161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 267 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchen 346
Cdd:cd17309 241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12848794 347 aprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 403
Cdd:cd17309 258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
62-405 2.43e-130

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 378.26  E-value: 2.43e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794     62 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTS 137
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    138 YDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGvTLLPQFLGMYRLNVDG---VEIYVIVTRNVSSHRLSVYRKYDLKG 214
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPN-TLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    215 STVAREASnKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVEC 293
Cdd:smart00330 159 STRGREAD-KKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    294 EENDGEEEGESDSTHPIGTPPDSPGNTLNSSPPLAPGEFDPnIDVYAIKCHEnaprkEVYFMAIIDILTHYDAKKKAAHA 373
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHW 311
                          330       340       350
                   ....*....|....*....|....*....|..
gi 12848794    374 AKTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 405
Cdd:smart00330 312 VKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
126-404 3.78e-71

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: 222.73  E-value: 3.78e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   126 SQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVEcHGVTLLPQFLGMYRLNVDGVEIYVIVTRNVSSHRLS 205
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   206 VYRKYDLKGSTVAREASNKEKAKELPT-LKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 284
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   285 RaeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaPRKEVYFMAIIDILTHY 364
Cdd:pfam01504 171 E--------------------------------------------------------------DGKEIYYLGIIDILTEY 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 12848794   365 DAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIGHI 404
Cdd:pfam01504 189 NLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1-401 1.18e-39

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 150.75  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    1 MATPGNLGSSVLASKTKTKKKHFVAQK-----VKLFRASDPLLSvLMWGVNHSINELSHVQiPVMLMPDDFKAYSKIKVD 75
Cdd:PLN03185 310 LVLNNSFSSTSRRAKRRQKKLVKEIKRpgetiIKGHRSYDLMLS-LQLGIRYTVGKITPIQ-RREVRPSDFGPRASFWMN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   76 nhlFNKEN---MPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYVIKTI 147
Cdd:PLN03185 388 ---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRElSSPGKSGSVFFLSQDDRFMIKTL 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  148 TSEDVAEMHNILKKYHQYiVECHGVTLLPQFLGMYRLN-VDGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEk 226
Cdd:PLN03185 465 RKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVE- 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  227 AKELPTLKDNDFINEgqkIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEEND 297
Cdd:PLN03185 543 IDENTTLKDLDLNYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVV 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  298 GEEEGESDSTH---------PIGTPPDS--PGNTLNSSPPLAPGEFDPNIDV-------YAIKCHENAP-RKE------- 351
Cdd:PLN03185 620 AEEDTIEDEELsypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDLllpgtarLQIQLGVNMPaRAEripgred 699
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12848794  352 ------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 401
Cdd:PLN03185 700 kekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
73-284 8.24e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 132.76  E-value: 8.24e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  73 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDdQDFQNSLTRSApLPNDSQARSGARFHTSYDKRYVIKTITS 149
Cdd:COG5253 320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-EALVSLLSRYI-LWESNGGKSGSFFLFTRDYKFIIKTISH 395
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 150 edvAEMHNILKKYHQYIVEC--HGVTLLPQFLGMYRLNV-------DGVEIYVIVTRNV-SSHRlsVYRKYDLKGSTVAR 219
Cdd:COG5253 396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVKSrssisssKSRKIYFIVMENLfYPHG--IHRIFDLKGSMRNR 470
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12848794 220 EASNKEKAKE-LPTLKDNDFINEGQKIyIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 284
Cdd:COG5253 471 HVERTGKSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
 
Name Accession Description Interval E-value
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
27-403 0e+00

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: 588.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  27 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 106
Cdd:cd17309   1 KVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNV 186
Cdd:cd17309  81 IDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGNTLLPQFLGMYRLTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 187 DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFL 266
Cdd:cd17309 161 DGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINDGQKIYIDENNKKMFLEKLKKDVEFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 267 AQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchen 346
Cdd:cd17309 241 AQLKLMDYSLLVGIHDV--------------------------------------------------------------- 257
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12848794 347 aprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 403
Cdd:cd17309 258 -----VYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
36-403 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: 562.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNS 115
Cdd:cd17305   1 PLLSVFMWGINHSINELSHVPIPVMLMPDDFKAYSKIKVDNHLFNKENLPSHFKVKEYCPLVFRNLRERFGIDDDDYLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 116 LTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNVDGVEIYVIV 195
Cdd:cd17305  81 LTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGKTLLPQYLGMYRITVNGVETYLVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 196 TRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYS 275
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDNDFLNDGTKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 276 LLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaprkeVYFM 355
Cdd:cd17305 241 LLVGIHDC--------------------------------------------------------------------IYFM 252
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 12848794 356 AIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGH 403
Cdd:cd17305 253 AIIDILTHYGAKKRAAHAAKTVKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
25-401 0e+00

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: 556.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  25 AQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRER 104
Cdd:cd17310   1 CQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 105 FGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRL 184
Cdd:cd17310  81 FGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 185 NVDGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVE 264
Cdd:cd17310 161 TVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 265 FLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikch 344
Cdd:cd17310 241 FLAQLKIMDYSLLVGIHDV------------------------------------------------------------- 259
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12848794 345 enaprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 401
Cdd:cd17310 260 -------VYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
36-401 1.82e-156

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: 442.77  E-value: 1.82e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNS 115
Cdd:cd17311   1 PLVSVFMWGVNHSINELSQVPVPVMLLPDDFKANSKIKVNNHLFNRENLPSHFKFKEYCPQVFRNLRERFGIDDQDYQVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 116 LTRSAPLPNDSQarSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNVDGVEIYVIV 195
Cdd:cd17311  81 LTRSPPYSESEG--SDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGNTLLPQFLGMYRLSVDNEDSYMLV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 196 TRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYS 275
Cdd:cd17311 159 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 276 LLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaprkeVYFM 355
Cdd:cd17311 239 LLLGIHDV--------------------------------------------------------------------VYFM 250
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 12848794 356 AIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 401
Cdd:cd17311 251 GLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFI 296
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
62-405 2.43e-130

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 378.26  E-value: 2.43e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794     62 MPDDFKAYSKIKVDNHLfNKENMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTS 137
Cdd:smart00330   1 LPSDFKATEKIKFPTPG-HLELTPSHgsadFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    138 YDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGvTLLPQFLGMYRLNVDG---VEIYVIVTRNVSSHRLSVYRKYDLKG 214
Cdd:smart00330  80 LDDRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPN-TLLPKFFGLYRVKVKGgteKKIYFLVMENLFYSDLKVHRKYDLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    215 STVAREASnKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVEC 293
Cdd:smart00330 159 STRGREAD-KKKVKELPVLKDLDLVEMwNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIEL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    294 EENDGEEEGESDSTHPIGTPPDSPGNTLNSSPPLAPGEFDPnIDVYAIKCHEnaprkEVYFMAIIDILTHYDAKKKAAHA 373
Cdd:smart00330 238 PPVYGSDESPSSESSNGGKAPDITGNLLVSNSPDGDGPFGG-IPARAIRARR-----VVLYLGIIDILQTYTWDKKLEHW 311
                          330       340       350
                   ....*....|....*....|....*....|..
gi 12848794    374 AKTVKHGaGAEISTVNPEQYSKRFLDFIGHIL 405
Cdd:smart00330 312 VKSIGHD-GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
87-401 2.82e-84

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: 257.50  E-value: 2.82e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  87 HFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPND--SQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQ 164
Cdd:cd00139   2 KFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELkeSEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 165 YIVEcHGVTLLPQFLGMYRLNV-DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREAS-NKEKAKELPTLKDNDFINEG 242
Cdd:cd00139  82 HIKK-NPNSLLTRFYGLYSIKLqKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSkEKEKKKGLKVLKDLDFLEKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 243 QKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVeraeqeeveceendgeeegesdsthpigtppdspgntln 322
Cdd:cd00139 161 EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHRL--------------------------------------- 201
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12848794 323 sspplapgefdpnidvyaikchenaprkeVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFI 401
Cdd:cd00139 202 -----------------------------VYYLGIIDILQEYNLRKKLERFLKSLLYGKDSGISCVPPDEYAERFLKFM 251
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
126-404 3.78e-71

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: 222.73  E-value: 3.78e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   126 SQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVEcHGVTLLPQFLGMYRLNVDGVEIYVIVTRNVSSHRLS 205
Cdd:pfam01504  12 SPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQ-NPNTLLPRFYGLHRVKPGGKKIYFVVMNNLFPTDLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   206 VYRKYDLKGSTVAREASNKEKAKELPT-LKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 284
Cdd:pfam01504  91 IHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLKLRLGPEKREALLKQLERDCEFLESLNIMDYSLLLGIHDLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   285 RaeqeeveceendgeeegesdsthpigtppdspgntlnsspplapgefdpnidvyaikchenaPRKEVYFMAIIDILTHY 364
Cdd:pfam01504 171 E--------------------------------------------------------------DGKEIYYLGIIDILTEY 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 12848794   365 DAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIGHI 404
Cdd:pfam01504 189 NLKKKLEHAWKSLVHD-GDSISAVPPKEYAERFLKFIEKI 227
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
61-402 1.53e-68

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: 219.47  E-value: 1.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  61 LMPDDFKAYSKIKVDnHLFNKENMPSH--FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTS 137
Cdd:cd17303  26 LTDADFKAVHKFSFD-ITGNELTPSSKydFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKYILSElGSPGKSGSFFYFS 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 138 YDKRYVIKTITSEDVAEMHNILKKYHQYIVEcHGVTLLPQFLGMYRLNV-DGVEIYVIVTRNVSSHRLSVYRKYDLKGST 216
Cdd:cd17303 105 RDYRFIIKTIHHSEHKFLRKILPDYYNHVKE-NPNTLLSQFYGLHRVKMpRGRKIHFVVMNNLFPPHRDIHQTFDLKGST 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 217 VAREAS-NKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVEraeqeevecee 295
Cdd:cd17303 184 VGRETPeDKLAKGPRATLKDLNWLRRKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD----------- 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 296 ndgeeegesdsthpigtppdspgntlnsspplapGEFDPnIDVyaikchENAPRKEVYFMAIIDILTHYDAKKKAAHAAK 375
Cdd:cd17303 253 ----------------------------------GGFQA-TDE------NNEPGDEIYYLGIIDILTPYNAKKKLEHFFK 291
                       330       340
                ....*....|....*....|....*..
gi 12848794 376 TVKHgAGAEISTVNPEQYSKRFLDFIG 402
Cdd:cd17303 292 SLRH-DRHTISAVPPKEYARRFLKFIE 317
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
83-404 3.12e-51

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: 174.40  E-value: 3.12e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  83 NMPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYVIKTITSEDVAEMHN 157
Cdd:cd17302  48 TPPPHqssdFKWKDYCPMVFRNLRELFGIDAADYMLSLCGDDALRElSSPGKSGSVFYLSHDDRFMIKTMRKSEMKVLLR 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 158 ILKKYHQYiVECHGVTLLPQFLGMYRLN-VDGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEK-AKELPTLKD 235
Cdd:cd17302 128 MLPAYYKH-VKAYENTLLTKFFGVHRVKpVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRTTGKPESeIDPNTTLKD 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 236 NDFineGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDveraeqeeveceendgeeegesdsthpigTPPD 315
Cdd:cd17302 207 LDL---DFKFRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVHF-----------------------------RAGD 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 316 SPGntlnsspplapgefdpnidvyaikchenAPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAeISTVNPEQYSK 395
Cdd:cd17302 255 STG----------------------------EPYDVVLYFGIIDILQEYNISKKLEHAYKSLQYDPAS-ISAVDPKLYSR 305

                ....*....
gi 12848794 396 RFLDFIGHI 404
Cdd:cd17302 306 RFRDFIRKV 314
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
35-402 1.46e-49

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: 170.12  E-value: 1.46e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  35 DPLLSVLMWGVNHSINELSHVQIPVMLMpDDFKayskiKVDNHLFNKE---NMPSH----FKFKEYCPMVFRNLRERFGI 107
Cdd:cd17301   1 SELMGAIQLGIGHSVGSLSSKPERDVLM-QDFE-----VVESVFFPSEgstLTPAHhysdFRFKTYAPVAFRYFRELFGI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 108 DDQDFQNSLTRSaPLPNDSQ-ARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVEcHGVTLLPQFLGMYRLNV 186
Cdd:cd17301  75 KPDDYLLSLCNE-PLRELSNpGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCYQS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 187 DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINEGQK-IYIDDNNKKIFLEKLKKDVEF 265
Cdd:cd17301 153 GGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKASKKERQKKSPTLKDLDFMEDHPEgILLEPDTYDALLKTIQRDCRV 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 266 LAQLKLMDYSLLVGIHDveraeqeeveceendgeeegesdsthPIGTPpdspgnTLNSSpplapGEfdpnidvyaikche 345
Cdd:cd17301 233 LESFKIMDYSLLLGVHN--------------------------LGGIP------ARNSK-----GE-------------- 261
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12848794 346 naprKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFIG 402
Cdd:cd17301 262 ----RLLLFIGIIDILQSYRLKKKLEHTWKSVVHD-GDTVSVHRPSFYAERFQNFMA 313
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
85-281 2.91e-40

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: 145.52  E-value: 2.91e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  85 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILK 160
Cdd:cd17307  48 PAHhypdFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 161 KYHQYIVEcHGVTLLPQFLGMYRLNVDGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFIN 240
Cdd:cd17307 128 GYYMNLNQ-NPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKSCPTYKDLDFLQ 206
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 12848794 241 EGQK-IYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIH 281
Cdd:cd17307 207 DMHDgLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIH 248
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1-401 1.18e-39

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 150.75  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794    1 MATPGNLGSSVLASKTKTKKKHFVAQK-----VKLFRASDPLLSvLMWGVNHSINELSHVQiPVMLMPDDFKAYSKIKVD 75
Cdd:PLN03185 310 LVLNNSFSSTSRRAKRRQKKLVKEIKRpgetiIKGHRSYDLMLS-LQLGIRYTVGKITPIQ-RREVRPSDFGPRASFWMN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794   76 nhlFNKEN---MPSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPN-DSQARSGARFHTSYDKRYVIKTI 147
Cdd:PLN03185 388 ---FPKAGsqlTPSHqsedFKWKDYCPMVFRNLREMFKIDAADYMMSICGNDALRElSSPGKSGSVFFLSQDDRFMIKTL 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  148 TSEDVAEMHNILKKYHQYiVECHGVTLLPQFLGMYRLN-VDGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEk 226
Cdd:PLN03185 465 RKSEVKVLLRMLPDYHHH-VKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVE- 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  227 AKELPTLKDNDFINEgqkIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIH---------DVERAEQEEVECEEND 297
Cdd:PLN03185 543 IDENTTLKDLDLNYS---FYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHfrapqhlrsLLPYSRSITADGLEVV 619
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  298 GEEEGESDSTH---------PIGTPPDS--PGNTLNSSPPLAPGEFDPNIDV-------YAIKCHENAP-RKE------- 351
Cdd:PLN03185 620 AEEDTIEDEELsypeglvlvPRGADDGStvPGPHIRGSRLRASAAGDEEVDLllpgtarLQIQLGVNMPaRAEripgred 699
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12848794  352 ------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGAgAEISTVNPEQYSKRFLDFI 401
Cdd:PLN03185 700 kekqsfhevydvVLYLGIIDILQEYNMSKKIEHAYKSLQFDS-LSISAVDPTFYSKRFLEFI 760
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
34-284 2.19e-38

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: 141.29  E-value: 2.19e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  34 SDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFG 106
Cdd:cd17306   3 SSALKGAIQLGITHTVGSLSTKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhyndFRFKTYAPVAFRYFRELFG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVEcHGVTLLPQFLGMYRLNV 186
Cdd:cd17306  77 IRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 187 DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEF 265
Cdd:cd17306 156 GGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDiPDGLFLDSDMYNALCKTLQRDCLV 235
                       250
                ....*....|....*....
gi 12848794 266 LAQLKLMDYSLLVGIHDVE 284
Cdd:cd17306 236 LQSFKIMDYSLLVGIHNID 254
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
34-283 5.29e-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: 139.74  E-value: 5.29e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  34 SDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKayskikVDNHLFNKEN---MPSH----FKFKEYCPMVFRNLRERFG 106
Cdd:cd17308   1 SSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYV------VESIFFPSEGsnlTPAHhypdFRFKTYAPVAFRYFRELFG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 107 IDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVEcHGVTLLPQFLGMYRLNV 186
Cdd:cd17308  75 IRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQ-NPRTLLPKFYGLYCVQS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 187 DGVEIYVIVTRNVSSHRLSVYRKYDLKGSTVAREASNKEKAKELPTLKDNDFINE-GQKIYIDDNNKKIFLEKLKKDVEF 265
Cdd:cd17308 154 GGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDmPEGLMLDADTFSALVKTLQRDCLV 233
                       250
                ....*....|....*...
gi 12848794 266 LAQLKLMDYSLLVGIHDV 283
Cdd:cd17308 234 LESFKIMDYSLLLGVHNI 251
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
36-401 4.31e-35

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: 131.71  E-value: 4.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  36 PLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAyskiKVDNHLFNKENmpshFKFKEYCPMVFRNLRERFGIDDQDFQNS 115
Cdd:cd17304   5 SLTCMMKEGLRAAIQNSIDVPPKESLSDDDYTE----VLTQVIPKHKG----FEFRTYAGPVFATLRQSLGISEKEYQNS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 116 LTRSAP-LPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIvECHGVTLLPQFLGMYRLNVDG-VEIYV 193
Cdd:cd17304  77 LSPDEPyLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL-ENYPHSLLVKFLGVHSIKLPGkKKKYF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 194 IVTRNVSSHRLSVYRKYDLKGSTVAR-EASNKEKAKELPTLKDNDFinEGQKIYIDDNNkKIFLEKLKKDVEFLAQLKLM 272
Cdd:cd17304 156 IVMQSVFYPDERINERYDIKGCQVSRyTDPEPEGSQIIVVLKDLNF--EGNSINLGQQR-SWFLRQVEIDTEFLKGLNVL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 273 DYSLLVG---IHDVERAEQEeveceendgeeegesdsthpigtpPDSPgNTLNssppLAPGEfdpnidvyaikchenapr 349
Cdd:cd17304 233 DYSLLVGfqpLHSDENRRLL------------------------PNYK-NALH----VVDGP------------------ 265
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 12848794 350 KEVYFMAIIDILTHYDAKKKAAHAAKTVKHgAGAEISTVNPEQYSKRFLDFI 401
Cdd:cd17304 266 EYRYFVGIIDIFTVYGLRKRLEHLWKSLRY-PGQSFSTVSPEKYARRFCQWV 316
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
73-284 8.24e-34

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 132.76  E-value: 8.24e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  73 KVDNHLfnKENMPS---HFKFKEYCPMVFRNLRERFGIDdQDFQNSLTRSApLPNDSQARSGARFHTSYDKRYVIKTITS 149
Cdd:COG5253 320 KTDTHL--NEQFEEglyEFSCKDYFPEVFRELRALCGCD-EALVSLLSRYI-LWESNGGKSGSFFLFTRDYKFIIKTISH 395
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 150 edvAEMHNILKKYHQYIVEC--HGVTLLPQFLGMYRLNV-------DGVEIYVIVTRNV-SSHRlsVYRKYDLKGSTVAR 219
Cdd:COG5253 396 ---SEHICFRPMIFEYYVHVlfNPLTLLCKIFGFYRVKSrssisssKSRKIYFIVMENLfYPHG--IHRIFDLKGSMRNR 470
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12848794 220 EASNKEKAKE-LPTLKDNDFINEGQKIyIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVE 284
Cdd:COG5253 471 HVERTGKSMSvLLDMNDVEWIRESPKI-VFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDER 535
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
98-280 8.58e-30

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: 115.69  E-value: 8.58e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794  98 FRNLRERFGIDDQDFQNSLTRSAPLpnDSQ-ARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECH---GVT 173
Cdd:cd17300  13 FHALRSLYCGGEDDFIRSLSRCVKW--DASgGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALfhkRPS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12848794 174 LLPQFLGMYRLNV------DGVEIYVIVTRNVSsHRLSVYRKYDLKGSTVAReaSNKEKAKELPTLKDNDFINE--GQKI 245
Cdd:cd17300  91 LLAKILGVYRISVknsttnKTSKQDLLVMENLF-YGRNISQVYDLKGSLRNR--YVNVAEDEDSVLLDENFLEYtkGSPL 167
                       170       180       190
                ....*....|....*....|....*....|....*
gi 12848794 246 YIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGI 280
Cdd:cd17300 168 YLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGI 202
 
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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