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Conserved domains on  [gi|27735085|ref|NP_775763|]
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phosphatidylinositol 4-phosphate 5-kinase-like protein 1 isoform 2 [Homo sapiens]

Protein Classification

phosphatidylinositol phosphate kinase family protein( domain architecture ID 1000257)

phosphatidylinositol phosphate kinase (PIPK) family protein may catalyze the phosphorylation of phosphatidylinositol phosphate on the fourth or fifth hydroxyl of the inositol ring, to form phosphatidylinositol bisphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIPKc super family cl28923
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 1-189 7.29e-114

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.


The actual alignment was detected with superfamily member cd17304:

Pssm-ID: 475131  Cd Length: 319  Bit Score: 326.62  E-value: 7.29e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNFQGKTINLGPQRSWFLRQMELDTTFLRELNVLDYSLL 80
Cdd:cd17304 158 MQSVFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLL 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  81 IAFQRLHEDErgpgsslifrtarsvqgaqspeesraqNRRLLPDAPNALHILDGPEQRYFLGVVDLATVYGLRKRLEHLW 160
Cdd:cd17304 238 VGFQPLHSDE---------------------------NRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVYGLRKRLEHLW 290

                       170       180
                ....*....|....*....|....*....
gi 27735085 161 KTLRYPGRTFSTVSPARYARRLCQWVEAH 189
Cdd:cd17304 291 KSLRYPGQSFSTVSPEKYARRFCQWVEDH 319
 
Name Accession Description Interval E-value
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1-189 7.29e-114

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: 326.62  E-value: 7.29e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNFQGKTINLGPQRSWFLRQMELDTTFLRELNVLDYSLL 80
Cdd:cd17304 158 MQSVFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLL 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  81 IAFQRLHEDErgpgsslifrtarsvqgaqspeesraqNRRLLPDAPNALHILDGPEQRYFLGVVDLATVYGLRKRLEHLW 160
Cdd:cd17304 238 VGFQPLHSDE---------------------------NRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVYGLRKRLEHLW 290

                       170       180
                ....*....|....*....|....*....
gi 27735085 161 KTLRYPGRTFSTVSPARYARRLCQWVEAH 189
Cdd:cd17304 291 KSLRYPGQSFSTVSPEKYARRFCQWVEDH 319
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 1-189 2.46e-51

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: 164.56  E-value: 2.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085     1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNF--QGKTINLGPQ-RSWFLRQMELDTTFLRELNVLDY 77
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFleRKLKLRLGPEkREALLKQLERDCEFLESLNIMDY 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085    78 SLLIAFQRLHEDERgpgsslifrtarsvqgaqspeesraqnrrllpdapnalhildgpeQRYFLGVVDLATVYGLRKRLE 157
Cdd:pfam01504 161 SLLLGIHDLDEDGK---------------------------------------------EIYYLGIIDILTEYNLKKKLE 195

                         170       180       190
                  ....*....|....*....|....*....|..
gi 27735085   158 HLWKTLRYPGRTFSTVSPARYARRLCQWVEAH 189
Cdd:pfam01504 196 HAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1-187 3.77e-33

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 120.95  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085      1 MQSVFYPAGRISERYDIKGCEVSRWVDPaPEGSPLVlVLKDLNF---QGKTINLGPQ-RSWFLRQMELDTTFLRELNVLD 76
Cdd:smart00330 140 MENLFYSDLKVHRKYDLKGSTRGREADK-KKVKELP-VLKDLDLvemWNQPIYVDPLaKKALLKQIKRDCEFLESLKIMD 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085     77 YSLLIAfqrLHEDERGPGSSLIFRTARSVQGAQS------PEESRAQNRRLLPDAPNALHILDGPEQR--------YFLG 142
Cdd:smart00330 218 YSLLVG---IHDIERGQREEIELPPVYGSDESPSsessngGKAPDITGNLLVSNSPDGDGPFGGIPARairarrvvLYLG 294

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 27735085    143 VVDLATVYGLRKRLEHLWKTLRYPGRTFSTVSPARYARRLCQWVE 187
Cdd:smart00330 295 IIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMD 339
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1-189 1.82e-15

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 73.44  E-value: 1.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAgRISERYDIKGCEVSRWVDP-APEGSPLvLVLKDLNF--QGKTINLGPQRSWFLRQMELDTTFLRELNVLDY 77
Cdd:COG5253 448 MENLFYPH-GIHRIFDLKGSMRNRHVERtGKSMSVL-LDMNDVEWirESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDY 525

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAFqrlhEDERgpgsslifrtarsvqgaqspEESraqNRRLLPDAPNALHILDgpeQRYFLGVVDLATVYGLRKRLE 157
Cdd:COG5253 526 SLLVGI----DDER--------------------EEA---SVGLIIDFIRTRMTGD---KKLESGIKDKLTVGSFTKRKE 575

                       170       180       190
                ....*....|....*....|....*....|..
gi 27735085 158 HlwktlrypgrtfSTVSPARYARRLCQWVEAH 189
Cdd:COG5253 576 P------------TAVTPRQYKNRFRKAMEAY 595
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1-187 2.15e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 55.99  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085    1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNFQgktINLGPqrSW---FLRQMELDTTFLRELNVLDY 77
Cdd:PLN03185 513 MGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENTTLKDLDLNYS---FYLEP--SWrdaLLRQIEIDSKFLEAQRIMDY 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   78 SLLI-----AFQRLH-----------------------EDE------------RGPGSSLI-----FRTARSVQGAQSPE 112
Cdd:PLN03185 588 SLLLgvhfrAPQHLRsllpysrsitadglevvaeedtiEDEelsypeglvlvpRGADDGSTvpgphIRGSRLRASAAGDE 667

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  113 ES----------RAQNRRLLPDAPNALHILDGPEQRYF---------LGVVDLATVYGLRKRLEHLWKTLRYPGRTFSTV 173
Cdd:PLN03185 668 EVdlllpgtarlQIQLGVNMPARAERIPGREDKEKQSFhevydvvlyLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAV 747

                        250
                 ....*....|....
gi 27735085  174 SPARYARRLCQWVE 187
Cdd:PLN03185 748 DPTFYSKRFLEFIQ 761
 
Name Accession Description Interval E-value
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1-189 7.29e-114

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: 326.62  E-value: 7.29e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNFQGKTINLGPQRSWFLRQMELDTTFLRELNVLDYSLL 80
Cdd:cd17304 158 MQSVFYPDERINERYDIKGCQVSRYTDPEPEGSQIIVVLKDLNFEGNSINLGQQRSWFLRQVEIDTEFLKGLNVLDYSLL 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  81 IAFQRLHEDErgpgsslifrtarsvqgaqspeesraqNRRLLPDAPNALHILDGPEQRYFLGVVDLATVYGLRKRLEHLW 160
Cdd:cd17304 238 VGFQPLHSDE---------------------------NRRLLPNYKNALHVVDGPEYRYFVGIIDIFTVYGLRKRLEHLW 290

                       170       180
                ....*....|....*....|....*....
gi 27735085 161 KTLRYPGRTFSTVSPARYARRLCQWVEAH 189
Cdd:cd17304 291 KSLRYPGQSFSTVSPEKYARRFCQWVEDH 319
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
 1-189 2.46e-51

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: 164.56  E-value: 2.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085     1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNF--QGKTINLGPQ-RSWFLRQMELDTTFLRELNVLDY 77
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTTLKDLDFleRKLKLRLGPEkREALLKQLERDCEFLESLNIMDY 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085    78 SLLIAFQRLHEDERgpgsslifrtarsvqgaqspeesraqnrrllpdapnalhildgpeQRYFLGVVDLATVYGLRKRLE 157
Cdd:pfam01504 161 SLLLGIHDLDEDGK---------------------------------------------EIYYLGIIDILTEYNLKKKLE 195

                         170       180       190
                  ....*....|....*....|....*....|..
gi 27735085   158 HLWKTLRYPGRTFSTVSPARYARRLCQWVEAH 189
Cdd:pfam01504 196 HAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
 1-187 2.02e-45

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: 150.42  E-value: 2.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNF--QGKTINLGP-QRSWFLRQMELDTTFLRELNVLDY 77
Cdd:cd00139 113 MENVFPTDLKIHERYDLKGSTVGRRVSKEKEKKKGLKVLKDLDFleKGEKIILGPeDRAELLEQLEKDVEFLRSLNIMDY 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAFQRLhedergpgsslifrtarsvqgaqspeesraqnrrllpdapnalhildgpeqRYFLGVVDLATVYGLRKRLE 157
Cdd:cd00139 193 SLLVGIHRL---------------------------------------------------VYYLGIIDILQEYNLRKKLE 221

                       170       180       190
                ....*....|....*....|....*....|.
gi 27735085 158 HLWKTLRYPGRT-FSTVSPARYARRLCQWVE 187
Cdd:cd00139 222 RFLKSLLYGKDSgISCVPPDEYAERFLKFME 252
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1-187 3.77e-33

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 120.95  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085      1 MQSVFYPAGRISERYDIKGCEVSRWVDPaPEGSPLVlVLKDLNF---QGKTINLGPQ-RSWFLRQMELDTTFLRELNVLD 76
Cdd:smart00330 140 MENLFYSDLKVHRKYDLKGSTRGREADK-KKVKELP-VLKDLDLvemWNQPIYVDPLaKKALLKQIKRDCEFLESLKIMD 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085     77 YSLLIAfqrLHEDERGPGSSLIFRTARSVQGAQS------PEESRAQNRRLLPDAPNALHILDGPEQR--------YFLG 142
Cdd:smart00330 218 YSLLVG---IHDIERGQREEIELPPVYGSDESPSsessngGKAPDITGNLLVSNSPDGDGPFGGIPARairarrvvLYLG 294

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 27735085    143 VVDLATVYGLRKRLEHLWKTLRYPGRTFSTVSPARYARRLCQWVE 187
Cdd:smart00330 295 IIDILQTYTWDKKLEHWVKSIGHDGKTISVVHPEQYAKRFRDFMD 339
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
 1-181 1.72e-29

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: 110.46  E-value: 1.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNF--QGKTINLGP-QRSWFLRQMELDTTFLRELNVLDY 77
Cdd:cd17303 163 MNNLFPPHRDIHQTFDLKGSTVGRETPEDKLAKGPRATLKDLNWlrRKRKLALGPeKRKQFLTQLKRDVEFLASLNIMDY 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAFQRLHedergpgsslifrtarsvQGAQSPEEsraqnrrllpdAPNALHILdgpeqrYFLGVVDLATVYGLRKRLE 157
Cdd:cd17303 243 SLLVGIHDLD------------------GGFQATDE-----------NNEPGDEI------YYLGIIDILTPYNAKKKLE 287

                       170       180
                ....*....|....*....|....
gi 27735085 158 HLWKTLRYPGRTFSTVSPARYARR 181
Cdd:cd17303 288 HFFKSLRHDRHTISAVPPKEYARR 311
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
 1-183 1.02e-21

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: 89.66  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVD-PAPEGSPLVlVLKDLNFQGKtinLGPQRSW---FLRQMELDTTFLRELNVLD 76
Cdd:cd17302 166 MGNLFCTELRIHRRFDLKGSTHGRTTGkPESEIDPNT-TLKDLDLDFK---FRLEKGWrdaLMRQIDADCAFLEALRIMD 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  77 YSLLIAFQRLHEDERGpgsslifrTARSVqgaqspeesraqnrrllpdapnalhILdgpeqryFLGVVDLATVYGLRKRL 156
Cdd:cd17302 242 YSLLLGVHFRAGDSTG--------EPYDV-------------------------VL-------YFGIIDILQEYNISKKL 281

                       170       180
                ....*....|....*....|....*..
gi 27735085 157 EHLWKTLRYPGRTFSTVSPARYARRLC 183
Cdd:cd17302 282 EHAYKSLQYDPASISAVDPKLYSRRFR 308
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
 1-187 2.59e-18

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: 80.39  E-value: 2.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRwVDPAPEGSPLVLVLKDLNF--QGKTINLGP-QRSWFLRQMELDTTFLRELNVLDY 77
Cdd:cd17305 161 MRNVFSPRLPIHKKYDLKGSTVDR-QASDKEKAKDLPTLKDNDFlnDGTKIYIGDeAKAKLLETLKRDVEFLAKLNLMDY 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAfqrLHEdergpgssLIfrtarsvqgaqspeesraqnrrllpdapnalhildgpeqrYFLGVVDLATVYGLRKRLE 157
Cdd:cd17305 240 SLLVG---IHD--------CI----------------------------------------YFMAIIDILTHYGAKKRAA 268

                       170       180       190
                ....*....|....*....|....*....|.
gi 27735085 158 HLWKTLRY-PGRTFSTVSPARYARRLCQWVE 187
Cdd:cd17305 269 HAAKTVKHgAGAEISTVKPEQYAKRFLEFIS 299
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1-189 1.82e-15

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 73.44  E-value: 1.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAgRISERYDIKGCEVSRWVDP-APEGSPLvLVLKDLNF--QGKTINLGPQRSWFLRQMELDTTFLRELNVLDY 77
Cdd:COG5253 448 MENLFYPH-GIHRIFDLKGSMRNRHVERtGKSMSVL-LDMNDVEWirESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDY 525

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAFqrlhEDERgpgsslifrtarsvqgaqspEESraqNRRLLPDAPNALHILDgpeQRYFLGVVDLATVYGLRKRLE 157
Cdd:COG5253 526 SLLVGI----DDER--------------------EEA---SVGLIIDFIRTRMTGD---KKLESGIKDKLTVGSFTKRKE 575

                       170       180       190
                ....*....|....*....|....*....|..
gi 27735085 158 HlwktlrypgrtfSTVSPARYARRLCQWVEAH 189
Cdd:COG5253 576 P------------TAVTPRQYKNRFRKAMEAY 595
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
 1-181 1.62e-13

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: 67.27  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFyPAG-RISERYDIKGCEVSRwvdPAPE-----GSPlvlVLKDLNFQ---GKTINLGPQ-RSWFLRQMELDTTFLR 70
Cdd:cd17301 162 MNNLL-PSNiKMHEKYDLKGSTYKR---KASKkerqkKSP---TLKDLDFMedhPEGILLEPDtYDALLKTIQRDCRVLE 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  71 ELNVLDYSLLIAfqrLHEDERGPgsslifrtARSVQGAqspeesraqnrRLLpdapnalhildgpeqrYFLGVVDLATVY 150
Cdd:cd17301 235 SFKIMDYSLLLG---VHNLGGIP--------ARNSKGE-----------RLL----------------LFIGIIDILQSY 276

                       170       180       190
                ....*....|....*....|....*....|.
gi 27735085 151 GLRKRLEHLWKTLRYPGRTFSTVSPARYARR 181
Cdd:cd17301 277 RLKKKLEHTWKSVVHDGDTVSVHRPSFYAER 307
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-186 2.49e-10

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: 58.14  E-value: 2.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVlVLKDLNF--QGKTINLGPQ-RSWFLRQMELDTTFLRELNVLDY 77
Cdd:cd17310 172 TRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLP-TFKDNDFlnEGQKLHVGEEsKKNFLEKLKRDVEFLAQLKIMDY 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAfqrLHedergpgsslifrtarsvqgaqspeesraqnrrllpdapnalhildgpEQRYFLGVVDLATVYGLRKRLE 157
Cdd:cd17310 251 SLLVG---IH------------------------------------------------DVVYFMAIIDILTPYDAKKKAA 279

                       170       180       190
                ....*....|....*....|....*....|
gi 27735085 158 HLWKTLRY-PGRTFSTVSPARYARRLCQWV 186
Cdd:cd17310 280 HAAKTVKHgAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 1-186 2.05e-09

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: 55.64  E-value: 2.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVlVLKDLNFQGKTINL---GPQRSWFLRQMELDTTFLRELNVLDY 77
Cdd:cd17311 159 MRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELP-TLKDMDFLNKNQKVyvgEEQKRIFLEKLKRDVEFLVQLKIMDY 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  78 SLLIAFQrlhedergpgsslifrtarsvqgaqspeesraqnrrllpdapnalhildgpEQRYFLGVVDLATVYGLRKRLE 157
Cdd:cd17311 238 SLLLGIH---------------------------------------------------DVVYFMGLIDILTQYDAKKKAA 266

                       170       180       190
                ....*....|....*....|....*....|
gi 27735085 158 HLWKTLRY-PGRTFSTVSPARYARRLCQWV 186
Cdd:cd17311 267 HAAKTVKHgAGAEISTVHPEQYAKRFLDFI 296
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1-187 2.15e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 55.99  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085    1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNFQgktINLGPqrSW---FLRQMELDTTFLRELNVLDY 77
Cdd:PLN03185 513 MGNMFCTELRIHRRFDLKGSSLGRSADKVEIDENTTLKDLDLNYS---FYLEP--SWrdaLLRQIEIDSKFLEAQRIMDY 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   78 SLLI-----AFQRLH-----------------------EDE------------RGPGSSLI-----FRTARSVQGAQSPE 112
Cdd:PLN03185 588 SLLLgvhfrAPQHLRsllpysrsitadglevvaeedtiEDEelsypeglvlvpRGADDGSTvpgphIRGSRLRASAAGDE 667

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  113 ES----------RAQNRRLLPDAPNALHILDGPEQRYF---------LGVVDLATVYGLRKRLEHLWKTLRYPGRTFSTV 173
Cdd:PLN03185 668 EVdlllpgtarlQIQLGVNMPARAERIPGREDKEKQSFhevydvvlyLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAV 747

                        250
                 ....*....|....
gi 27735085  174 SPARYARRLCQWVE 187
Cdd:PLN03185 748 DPTFYSKRFLEFIQ 761
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1-186 3.41e-08

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: 51.92  E-value: 3.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPlVLVLKDLNFQGKT---INLGPQR-SWFLRQMELDTTFLRELNVLD 76
Cdd:cd17307 162 MNNVLPRSVKMHYKYDLKGSTYKRRASRKEREKS-CPTYKDLDFLQDMhdgLYFDPETyNALMKTLQRDCRVLESFKIMD 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  77 YSLLIAFQRLhedergpgsslifrtarsvqgAQSPEESRAQNRRLLpdapnalhildgpeqryFLGVVDLATVYGLRKRL 156
Cdd:cd17307 241 YSLLLGIHVL---------------------GGIPAKNHKGEKLLL-----------------FMGIIDILQSYRLMKKL 282

                       170       180       190
                ....*....|....*....|....*....|
gi 27735085 157 EHLWKTLRYPGRTFSTVSPARYARRLCQWV 186
Cdd:cd17307 283 EHSWKALVYDGDTVSVHRPSFYADRFLKFM 312
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
 2-186 1.20e-07

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: 50.36  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   2 QSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVlVLKDLNF--QGKTINLGPQ-RSWFLRQMELDTTFLRELNVLDYS 78
Cdd:cd17309 171 RNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELP-TLKDNDFinDGQKIYIDENnKKMFLEKLKKDVEFLAQLKLMDYS 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  79 LLIAFQrlhedergpgsslifrtarsvqgaqspeesraqnrrllpdapnalhildgpEQRYFLGVVDLATVYGLRKRLEH 158
Cdd:cd17309 250 LLVGIH---------------------------------------------------DVVYFMAIIDILTHYDAKKKAAH 278

                       170       180
                ....*....|....*....|....*....
gi 27735085 159 LWKTLRY-PGRTFSTVSPARYARRLCQWV 186
Cdd:cd17309 279 AAKTVKHgAGAEISTVNPEQYSKRFLDFI 307
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 10-182 2.24e-07

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: 49.61  E-value: 2.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  10 RISERYDIKGCEVSRWVDPAPEGSPLVlVLKDLNFQ---GKTINLGPQ-RSWFLRQMELDTTFLRELNVLDYSLLIAFQR 85
Cdd:cd17306 174 KMHLKYDLKGSTYKRRASQKEREKPLP-TYKDLDFLqdiPDGLFLDSDmYNALCKTLQRDCLVLQSFKIMDYSLLVGIHN 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  86 LheDERGPGSsliFRTARSVQGAqsPEESRAQNRRLLpdapnalhildgpeqryFLGVVDLATVYGLRKRLEHLWKTLRY 165
Cdd:cd17306 253 I--DARRGGT---IETDDQMGGI--PARNSKGERLLL-----------------YIGIIDILQSYRFVKKLEHSWKALVH 308

                       170
                ....*....|....*..
gi 27735085 166 PGRTFSTVSPARYARRL 182
Cdd:cd17306 309 DGDTVSVHRPGFYAERF 325
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
 1-182 1.91e-05

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: 43.83  E-value: 1.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085   1 MQSVFYPAGRISERYDIKGCEVSRWVDpAPEGSPLVLVLKDLNFQGKT---INLGPQR-SWFLRQMELDTTFLRELNVLD 76
Cdd:cd17308 163 MNNILPRVVKMHLKFDLKGSTYKRRAS-KKEREKSKPTFKDLDFMQDMpegLMLDADTfSALVKTLQRDCLVLESFKIMD 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735085  77 YSLLIAfqrLHEDERGPgsslifrtarSVQGaqspeesraQNRRLLpdapnalhildgpeqrYFLGVVDLATVYGLRKRL 156
Cdd:cd17308 242 YSLLLG---VHNIGGIP----------AVNG---------KGERLL----------------LYIGIIDILQSYRLIKKL 283

                       170       180
                ....*....|....*....|....*.
gi 27735085 157 EHLWKTLRYPGRTFSTVSPARYARRL 182
Cdd:cd17308 284 EHTWKALVHDGDTVSVHRPSFYAERF 309
 
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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