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Conserved domains on  [gi|1720360709|ref|XP_030100812|]
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phosphatidylinositol 4-phosphate 5-kinase type-1 gamma isoform X2 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
1-342 0e+00

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinases (PIP5KI) and similar proteins; PIP5KIs, also known as PIPKIs, or PI4P5KIs, phosphorylate the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes. Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K1alpha, PIP5K1beta, and PIP5K1gamma isoforms.


:

Pssm-ID: 340438  Cd Length: 320  Bit Score: 628.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   1 MQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17301    28 MQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNEPLRELSNPGASGSLFYLTHDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17301   108 EFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 SKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskad 240
Cdd:cd17301   188 SKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGVHNL----------------- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 241 ekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTV 320
Cdd:cd17301   251 ----------------------------------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTV 296
                         330       340
                  ....*....|....*....|..
gi 1720360709 321 SVHRPSFYAERFFKFMSSTVFR 342
Cdd:cd17301   297 SVHRPSFYAERFQNFMANTVFK 318
 
Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
1-342 0e+00

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinases (PIP5KI) and similar proteins; PIP5KIs, also known as PIPKIs, or PI4P5KIs, phosphorylate the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes. Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K1alpha, PIP5K1beta, and PIP5K1gamma isoforms.


Pssm-ID: 340438  Cd Length: 320  Bit Score: 628.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   1 MQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17301    28 MQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNEPLRELSNPGASGSLFYLTHDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17301   108 EFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 SKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskad 240
Cdd:cd17301   188 SKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGVHNL----------------- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 241 ekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTV 320
Cdd:cd17301   251 ----------------------------------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTV 296
                         330       340
                  ....*....|....*....|..
gi 1720360709 321 SVHRPSFYAERFFKFMSSTVFR 342
Cdd:cd17301   297 SVHRPSFYAERFQNFMANTVFK 318
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1-340 6.12e-153

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 441.82  E-value: 6.12e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709    1 MQDFYVVESIFFPSEGS-NLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSD 79
Cdd:smart00330   2 PSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   80 DEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGK---NIRVVVMNNVLPRVVKMHLKFDLKGSTY 156
Cdd:smart00330  82 DRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGSTR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  157 KRRASKKeKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQ 236
Cdd:smart00330 162 GREADKK-KVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPPV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  237 SKADEKRPVAQKALYSTamESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHD 316
Cdd:smart00330 241 YGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHD 318
                          330       340
                   ....*....|....*....|....
gi 1720360709  317 GDTVSVHRPSFYAERFFKFMSSTV 340
Cdd:smart00330 319 GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
55-339 4.00e-125

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: 366.02  E-value: 4.00e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  55 SLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVV 134
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 135 MNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPT-YKDLDFMQDMPEgLLLDSDTFGALVKTLQRDCLVLESFKIMD 213
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 214 YSLLLGVHNIDQqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmggipavngrGERLLLHIGI 293
Cdd:pfam01504 160 YSLLLGIHDLDE----------------------------------------------------------DGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1720360709 294 IDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSST 339
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
12-341 2.15e-69

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 237.81  E-value: 2.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  12 FPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-NEPLIELSNPGASGSVFYVTSDDEFIIKTVMHK 90
Cdd:PLN03185  388 FPKAGSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKS 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  91 EAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSl 169
Cdd:PLN03185  468 EVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN- 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 170 PTYKDLdfmqDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKA 249
Cdd:PLN03185  547 TTLKDL----DLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITADGLEVVAEE 622
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 250 L--------YSTAMESIQGGAA----------RGEAI--------ETDDTMGGIP------AVN--GRGER--------- 286
Cdd:PLN03185  623 DtiedeelsYPEGLVLVPRGADdgstvpgphiRGSRLrasaagdeEVDLLLPGTArlqiqlGVNmpARAERipgredkek 702
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360709 287 --------LLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMsSTVF 341
Cdd:PLN03185  703 qsfhevydVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
27-342 3.98e-37

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 145.47  E-value: 3.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  27 DFRFKTYAPVAFRYFRELFGIrpDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNL 106
Cdd:COG5253   335 EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHV 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 107 NQNPRTLLPKFYGLYCVQ-------SGGKNIRVVVMNNVLPRvVKMHLKFDLKGSTYKRRASKKEKEKS-LPTYKDLDFM 178
Cdd:COG5253   413 LFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYP-HGIHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWI 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 179 QdmpEGLLLDSDTFGALVKT-LQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkaLYSTAMES 257
Cdd:COG5253   492 R---ESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDDE--------------------------REEASVGL 542
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 258 IQggaargEAIETDDTMGGIpavngrgerllLHIGIIDILQSYRFIKKLEhtwkalvhdgdtVSVHRPSFYAERFFKFMS 337
Cdd:COG5253   543 II------DFIRTRMTGDKK-----------LESGIKDKLTVGSFTKRKE------------PTAVTPRQYKNRFRKAME 593

                  ....*
gi 1720360709 338 STVFR 342
Cdd:COG5253   594 AYIDP 598
 
Name Accession Description Interval E-value
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
1-342 0e+00

Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinases (PIP5KI) and similar proteins; PIP5KIs, also known as PIPKIs, or PI4P5KIs, phosphorylate the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), an essential lipid molecule in various cellular processes. Three distinct PIP5KIs have been characterized in erythrocytes, PIP5K1alpha, PIP5K1beta, and PIP5K1gamma isoforms.


Pssm-ID: 340438  Cd Length: 320  Bit Score: 628.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   1 MQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17301    28 MQDFEVVESVFFPSEGSTLTPAHHYSDFRFKTYAPVAFRYFRELFGIKPDDYLLSLCNEPLRELSNPGASGSLFYLTHDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17301   108 EFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCYQSGGKNIRFVVMNNLLPSNIKMHEKYDLKGSTYKRKA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 SKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskad 240
Cdd:cd17301   188 SKKERQKKSPTLKDLDFMEDHPEGILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGVHNL----------------- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 241 ekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTV 320
Cdd:cd17301   251 ----------------------------------GGIPARNSKGERLLLFIGIIDILQSYRLKKKLEHTWKSVVHDGDTV 296
                         330       340
                  ....*....|....*....|..
gi 1720360709 321 SVHRPSFYAERFFKFMSSTVFR 342
Cdd:cd17301   297 SVHRPSFYAERFQNFMANTVFK 318
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1-342 0e+00

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: 627.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   1 MQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17308    29 MQDFYVVESIFFPSEGSNLTPAHHYPDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17308   109 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 SKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNidqqererqaegaqskad 240
Cdd:cd17308   189 SKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHN------------------ 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 241 ekrpvaqkalystamesiqggaargeaietddtMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTV 320
Cdd:cd17308   251 ---------------------------------IGGIPAVNGKGERLLLYIGIIDILQSYRLIKKLEHTWKALVHDGDTV 297
                         330       340
                  ....*....|....*....|..
gi 1720360709 321 SVHRPSFYAERFFKFMSSTVFR 342
Cdd:cd17308   298 SVHRPSFYAERFFKFMSNTVFR 319
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1-342 0e+00

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: 581.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   1 MQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17307    28 MQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFYVTSDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17307   108 EFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSVKMHYKYDLKGSTYKRRA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 SKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskad 240
Cdd:cd17307   188 SRKEREKSCPTYKDLDFLQDMHDGLYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGIHVL----------------- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 241 ekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTV 320
Cdd:cd17307   251 ----------------------------------GGIPAKNHKGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTV 296
                         330       340
                  ....*....|....*....|..
gi 1720360709 321 SVHRPSFYAERFFKFMSSTVFR 342
Cdd:cd17307   297 SVHRPSFYADRFLKFMNSRVFK 318
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1-342 0e+00

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: 571.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   1 MQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17306    31 MQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17306   111 EFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHLKYDLKGSTYKRRA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 SKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDqqererqaegaqskad 240
Cdd:cd17306   191 SQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGIHNID---------------- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 241 ekrpvaqkalystamesiqggAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTV 320
Cdd:cd17306   255 ---------------------ARRGGTIETDDQMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTV 313
                         330       340
                  ....*....|....*....|..
gi 1720360709 321 SVHRPSFYAERFFKFMSSTVFR 342
Cdd:cd17306   314 SVHRPGFYAERFQRFMCNTVFK 335
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1-340 6.12e-153

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 441.82  E-value: 6.12e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709    1 MQDFYVVESIFFPSEGS-NLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSD 79
Cdd:smart00330   2 PSDFKATEKIKFPTPGHlELTPSHGSADFKFKDYCPEVFRNLRELFGIDPADYLRSLCRSPPLELSSGGKSGSFFYLSLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   80 DEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGK---NIRVVVMNNVLPRVVKMHLKFDLKGSTY 156
Cdd:smart00330  82 DRFIIKTVSKSEIKSLLPMLPNYYEHIVQNPNTLLPKFFGLYRVKVKGGtekKIYFLVMENLFYSDLKVHRKYDLKGSTR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  157 KRRASKKeKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQ 236
Cdd:smart00330 162 GREADKK-KVKELPVLKDLDLVEMWNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERGQREEIELPPV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  237 SKADEKRPVAQKALYSTamESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHD 316
Cdd:smart00330 241 YGSDESPSSESSNGGKA--PDITGNLLVSNSPDGDGPFGGIPARAIRARRVVLYLGIIDILQTYTWDKKLEHWVKSIGHD 318
                          330       340
                   ....*....|....*....|....
gi 1720360709  317 GDTVSVHRPSFYAERFFKFMSSTV 340
Cdd:smart00330 319 GKTISVVHPEQYAKRFRDFMDKYF 342
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
55-339 4.00e-125

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: 366.02  E-value: 4.00e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  55 SLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVV 134
Cdd:pfam01504   1 LTGKSILSELSSPGKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHVKQNPNTLLPRFYGLHRVKPGGKKIYFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 135 MNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPT-YKDLDFMQDMPEgLLLDSDTFGALVKTLQRDCLVLESFKIMD 213
Cdd:pfam01504  81 MNNLFPTDLDIHERYDLKGSTVGRTAKKKEREKDEPTtLKDLDFLERKLK-LRLGPEKREALLKQLERDCEFLESLNIMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 214 YSLLLGVHNIDQqererqaegaqskadekrpvaqkalystamesiqggaargeaietddtmggipavngrGERLLLHIGI 293
Cdd:pfam01504 160 YSLLLGIHDLDE----------------------------------------------------------DGKEIYYLGI 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1720360709 294 IDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSST 339
Cdd:pfam01504 182 IDILTEYNLKKKLEHAWKSLVHDGDSISAVPPKEYAERFLKFIEKI 227
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
26-338 1.33e-96

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: 294.10  E-value: 1.33e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  26 QDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSN--PGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYY 103
Cdd:cd00139     1 GKFKFKDYAPEVFRKLRELFGISEEDYLESLSPEENLRELKesEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 104 MNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASK-KEKEKSLPTYKDLDFMQDM 181
Cdd:cd00139    81 EHIKKNPNSLLTRFYGLYSIKlQKGKKVYFVVMENVFPTDLKIHERYDLKGSTVGRRVSKeKEKKKGLKVLKDLDFLEKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 182 pEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHnidqqererqaegaqskadekrpvaqkalystamesiqgg 261
Cdd:cd00139   161 -EKIILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIH---------------------------------------- 199
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360709 262 aargeaietddtmggipavngrgeRLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDT-VSVHRPSFYAERFFKFMSS 338
Cdd:cd00139   200 ------------------------RLVYYLGIIDILQEYNLRKKLERFLKSLLYGKDSgISCVPPDEYAERFLKFMES 253
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
3-337 5.77e-88

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: 274.17  E-value: 5.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   3 DFYVVESIFFPSEGSNLTPAHHFQ-DFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-NEPLIELSNPGASGSVFYVTSDD 80
Cdd:cd17302    31 DFDPKAKQWFPFPGSGSTPPPHQSsDFKWKDYCPMVFRNLRELFGIDAADYMLSLCgDDALRELSSPGKSGSVFYLSHDD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  81 EFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCV-QSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRR 159
Cdd:cd17302   111 RFMIKTMRKSEMKVLLRMLPAYYKHVKAYENTLLTKFFGVHRVkPVGGRKVRFVVMGNLFCTELRIHRRFDLKGSTHGRT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 160 ASKKEKE-KSLPTYKDLDFmqDMPegLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHnidqqererqaegaqsk 238
Cdd:cd17302   191 TGKPESEiDPNTTLKDLDL--DFK--FRLEKGWRDALMRQIDADCAFLEALRIMDYSLLLGVH----------------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 239 adekrpvaqkalystamesIQGGAARGEAIEtddtmggipavngrgerLLLHIGIIDILQSYRFIKKLEHTWKALVHDGD 318
Cdd:cd17302   250 -------------------FRAGDSTGEPYD-----------------VVLYFGIIDILQEYNISKKLEHAYKSLQYDPA 293
                         330
                  ....*....|....*....
gi 1720360709 319 TVSVHRPSFYAERFFKFMS 337
Cdd:cd17302   294 SISAVDPKLYSRRFRDFIR 312
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
3-338 2.51e-84

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: 264.93  E-value: 2.51e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709   3 DFYVVESIFFPSEGSNLTPAHHFqDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNE-PLIELSNPGASGSVFYVTSDDE 81
Cdd:cd17303    30 DFKAVHKFSFDITGNELTPSSKY-DFKFKDYAPWVFRFLRELFGIDPADYLMSLTGKyILSELGSPGKSGSFFYFSRDYR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  82 FIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRA 160
Cdd:cd17303   109 FIIKTIHHSEHKFLRKILPDYYNHVKENPNTLLSQFYGLHRVKmPRGRKIHFVVMNNLFPPHRDIHQTFDLKGSTVGRET 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 161 S-KKEKEKSLPTYKDLDFMQdMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDqqererqaegaqska 239
Cdd:cd17303   189 PeDKLAKGPRATLKDLNWLR-RKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYSLLVGIHDLD--------------- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 240 dekrpvaqkalystamesiqggaargeaietddtmGGIPAVNGRGER--LLLHIGIIDILQSYRFIKKLEHTWKALVHDG 317
Cdd:cd17303   253 -----------------------------------GGFQATDENNEPgdEIYYLGIIDILTPYNAKKKLEHFFKSLRHDR 297
                         330       340
                  ....*....|....*....|.
gi 1720360709 318 DTVSVHRPSFYAERFFKFMSS 338
Cdd:cd17303   298 HTISAVPPKEYARRFLKFIED 318
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
12-341 2.15e-69

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 237.81  E-value: 2.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  12 FPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLC-NEPLIELSNPGASGSVFYVTSDDEFIIKTVMHK 90
Cdd:PLN03185  388 FPKAGSQLTPSHQSEDFKWKDYCPMVFRNLREMFKIDAADYMMSICgNDALRELSSPGKSGSVFFLSQDDRFMIKTLRKS 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  91 EAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSl 169
Cdd:PLN03185  468 EVKVLLRMLPDYHHHVKTYENTLITKFFGLHRIKpSSGQKFRFVVMGNMFCTELRIHRRFDLKGSSLGRSADKVEIDEN- 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 170 PTYKDLdfmqDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKA 249
Cdd:PLN03185  547 TTLKDL----DLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLGVHFRAPQHLRSLLPYSRSITADGLEVVAEE 622
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 250 L--------YSTAMESIQGGAA----------RGEAI--------ETDDTMGGIP------AVN--GRGER--------- 286
Cdd:PLN03185  623 DtiedeelsYPEGLVLVPRGADdgstvpgphiRGSRLrasaagdeEVDLLLPGTArlqiqlGVNmpARAERipgredkek 702
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360709 287 --------LLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMsSTVF 341
Cdd:PLN03185  703 qsfhevydVVLYLGIIDILQEYNMSKKIEHAYKSLQFDSLSISAVDPTFYSKRFLEFI-QKVF 764
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
23-338 1.63e-64

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: 212.90  E-value: 1.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  23 HHFQD------FRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQ 96
Cdd:cd17305    42 HLFNKenlpshFKVKEYCPLVFRNLRERFGIDDDDYLNSLTRSQPLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  97 KLLPGYYMNL-NQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDL 175
Cdd:cd17305   122 HILKQYHQYIvERHGKTLLPQYLGMYRITVNGVETYLVVMRNVFSPRLPIHKKYDLKGSTVDRQASDKEKAKDLPTLKDN 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 176 DFMQDMpEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkaLYstam 255
Cdd:cd17305   202 DFLNDG-TKIYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHDC--------------------------IY---- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 256 esiqggaargeaietddtmggipavngrgerlllHIGIIDILQSYRFIKKLEHTWKALVHDGDT-VSVHRPSFYAERFFK 334
Cdd:cd17305   251 ----------------------------------FMAIIDILTHYGAKKRAAHAAKTVKHGAGAeISTVKPEQYAKRFLE 296

                  ....
gi 1720360709 335 FMSS 338
Cdd:cd17305   297 FISK 300
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
28-338 5.29e-43

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: 155.98  E-value: 5.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  28 FRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLN 107
Cdd:cd17310    64 FKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 108 Q-NPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDmPEGLL 186
Cdd:cd17310   144 EcHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDFLNE-GQKLH 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 187 LDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiqggaarge 266
Cdd:cd17310   223 VGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV------------------------------------------- 259
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360709 267 aietddtmggipavngrgerlLLHIGIIDILQSYRFIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSS 338
Cdd:cd17310   260 ---------------------VYFMAIIDILTPYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFNEFMSN 311
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
21-338 3.14e-40

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: 148.20  E-value: 3.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  21 PAHhfqdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLP 100
Cdd:cd17309    59 PSH----FKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLANDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILK 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 101 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQ 179
Cdd:cd17309   135 KYHQYIVEcHGNTLLPQFLGMYRLTVDGVETYMIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFIN 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 180 DmPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiq 259
Cdd:cd17309   215 D-GQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDV------------------------------------ 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 260 ggaargeaietddtmggipavngrgerlLLHIGIIDILQSYRFIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSS 338
Cdd:cd17309   258 ----------------------------VYFMAIIDILTHYDAKKKAAHAAKTVKHGaGAEISTVNPEQYSKRFLDFITS 309
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
28-338 1.69e-38

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: 141.88  E-value: 1.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  28 FRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNpGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGY--YM- 104
Cdd:cd17300     3 FTCTIYFAEQFHALRSLYCGGEDDFIRSLSRCVKWDASG-GKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYfeYMa 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 105 -NLNQNPRTLLPKFYGLYCVQ----SGGKNIR--VVVMNNVLPRvVKMHLKFDLKGSTYKRRASKKEKEKS-LPtykDLD 176
Cdd:cd17300    82 kALFHKRPSLLAKILGVYRISvknsTTNKTSKqdLLVMENLFYG-RNISQVYDLKGSLRNRYVNVAEDEDSvLL---DEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 177 FMQDMPEG-LLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGvhnIDQQERErqaegaqskadekrpvaqkalystam 255
Cdd:cd17300   158 FLEYTKGSpLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVG---IDEEKKE-------------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 256 esiqggaargeaietddtmggipavngrgerllLHIGIIDILQSYRFIKKLEHTWKALVHDGD----TVsVHrPSFYAER 331
Cdd:cd17300   209 ---------------------------------LVVGIIDYIRTYTWDKKLESWVKSLGILGGggepTV-IS-PELYKKR 253

                  ....*..
gi 1720360709 332 FFKFMSS 338
Cdd:cd17300   254 FREAMDK 260
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
21-338 1.54e-37

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: 140.39  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  21 PAHhfqdFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPliELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLP 100
Cdd:cd17311    50 PSH----FKFKEYCPQVFRNLRERFGIDDQDYQVSLTRSP--PYSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 101 GYYMNLNQ-NPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQ 179
Cdd:cd17311   124 HYHQYIVKcHGNTLLPQFLGMYRLSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLN 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 180 DMpEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkalystamesiq 259
Cdd:cd17311   204 KN-QKVYVGEEQKRIFLEKLKRDVEFLVQLKIMDYSLLLGIHDV------------------------------------ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 260 ggaargeaietddtmggipavngrgerlLLHIGIIDILQSYRFIKKLEHTWKALVHD-GDTVSVHRPSFYAERFFKFMSS 338
Cdd:cd17311   247 ----------------------------VYFMGLIDILTQYDAKKKAAHAAKTVKHGaGAEISTVHPEQYAKRFLDFITN 298
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
27-342 3.98e-37

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 145.47  E-value: 3.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  27 DFRFKTYAPVAFRYFRELFGIrpDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNL 106
Cdd:COG5253   335 EFSCKDYFPEVFRELRALCGC--DEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSEHICFRPMIFEYYVHV 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 107 NQNPRTLLPKFYGLYCVQ-------SGGKNIRVVVMNNVLPRvVKMHLKFDLKGSTYKRRASKKEKEKS-LPTYKDLDFM 178
Cdd:COG5253   413 LFNPLTLLCKIFGFYRVKsrssissSKSRKIYFIVMENLFYP-HGIHRIFDLKGSMRNRHVERTGKSMSvLLDMNDVEWI 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 179 QdmpEGLLLDSDTFGALVKT-LQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqskadekrpvaqkaLYSTAMES 257
Cdd:COG5253   492 R---ESPKIVFGLKKKLLLSqVWNDVLFLSKLNIMDYSLLVGIDDE--------------------------REEASVGL 542
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 258 IQggaargEAIETDDTMGGIpavngrgerllLHIGIIDILQSYRFIKKLEhtwkalvhdgdtVSVHRPSFYAERFFKFMS 337
Cdd:COG5253   543 II------DFIRTRMTGDKK-----------LESGIKDKLTVGSFTKRKE------------PTAVTPRQYKNRFRKAME 593

                  ....*
gi 1720360709 338 STVFR 342
Cdd:COG5253   594 AYIDP 598
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
26-338 3.53e-36

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: 137.49  E-value: 3.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709  26 QDFRFKTYAPVAFRYFRELFGIRPDDYLYSL-CNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYM 104
Cdd:cd17304    47 KGFEFRTYAGPVFATLRQSLGISEKEYQNSLsPDEPYLQFISNSKSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 105 NLNQNPRTLLPKFYGLYCVQ-SGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKrRASKKEKEKS--LPTYKDLDFmqdm 181
Cdd:cd17304   127 HLENYPHSLLVKFLGVHSIKlPGKKKKYFIVMQSVFYPDERINERYDIKGCQVS-RYTDPEPEGSqiIVVLKDLNF---- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 182 pEGLLLDSDTFGA-LVKTLQRDCLVLESFKIMDYSLLLGVHNIdqqererqaegaqsKADEKR---PVAQKALYstames 257
Cdd:cd17304   202 -EGNSINLGQQRSwFLRQVEIDTEFLKGLNVLDYSLLVGFQPL--------------HSDENRrllPNYKNALH------ 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360709 258 iqggaargeaietddtmggipAVNGRGERLLlhIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMS 337
Cdd:cd17304   261 ---------------------VVDGPEYRYF--VGIIDIFTVYGLRKRLEHLWKSLRYPGQSFSTVSPEKYARRFCQWVE 317

                  .
gi 1720360709 338 S 338
Cdd:cd17304   318 D 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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