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Conserved domains on  [gi|20130093|ref|NP_611269|]
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Protein Classification

Fab1_TCP and PIPKc_PIKfyve domain-containing protein (domain architecture ID 13004850)

protein containing domains FYVE_PIKfyve_Fab1, DEP, Fab1_TCP, and PIPKc_PIKfyve

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
1479-1796 1.07e-125

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: 394.57  E-value: 1.07e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1479 CQFQCKIYFAREFDAMRSKSLKppkldkslyrrlekskmreelrisqsrtgsemelvrkpsdvgaprtTEDDsnqeedar 1558
Cdd:cd17300    1 TKFTCTIYFAEQFHALRSLYCG----------------------------------------------GEDD-------- 26
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1559 iaLARSLCKSVQWEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQQQPTLLAKIFGVFRVSVK 1638
Cdd:cd17300   27 --FIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHKRPSLLAKILGVYRISVK 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1639 KKDSFVERS--VMVMENLFYGCNIENKFDLKGSERNRLVDpSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQR 1716
Cdd:cd17300  105 NSTTNKTSKqdLLVMENLFYGRNISQVYDLKGSLRNRYVN-VAEDEDSVLLDENFLEYTKGSPLYLREHSKAVLMAAIWN 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1717 DSSFLEKNLVMDYSLLVGLDKKNGVLVLGIIDYIRTFTLDKRVESIIKGSGILGGkGKDPTVVNPERYKQRFIDAMDRYF 1796
Cdd:cd17300  184 DTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGILGG-GGEPTVISPELYKKRFREAMDKYF 262
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
464-717 6.37e-125

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


:

Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 392.36  E-value: 6.37e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  464 EQLLAQMLRAHNL--DQEWDKVLQMLCSTAANHFKPEHCSNDLMDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDM 541
Cdd:cd03334    1 RALLAQLLKDEGIsnDESWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  542 ATHVPFPRILLLQCPIVYERIEGKFVTIETVLLQEKEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVK 621
Cdd:cd03334   81 PSKIKNPRILLLQGPLEYQRVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  622 LSVMERLSRTLQCDIVSSIESNITMPKLGYCNDFYIRNYN-----GKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKRVA 696
Cdd:cd03334  161 PSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVeehgrSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVV 240
                        250       260
                 ....*....|....*....|.
gi 20130093  697 SALLFARYNWRLEMSFLLNEF 717
Cdd:cd03334  241 EFMVFAAYHLKLETSFLADEF 261
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
182-243 5.21e-40

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that 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] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). 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. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays 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 (hERG) channels. This family also includes the yeast and plant orthologs 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 lipid kinase domain related to PtdInsP kinases.


:

Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 142.08  E-value: 5.21e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20130093  182 FWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCSK 243
Cdd:cd15725    1 YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
329-397 6.42e-10

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


:

Pssm-ID: 214489  Cd Length: 77  Bit Score: 56.91  E-value: 6.42e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093     329 ITLHEEMQRDLPAQNCGQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMDFDSSLHYKF 397
Cdd:smart00049    7 LRDRKYFLKTYPNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRF 75
 
Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
1479-1796 1.07e-125

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: 394.57  E-value: 1.07e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1479 CQFQCKIYFAREFDAMRSKSLKppkldkslyrrlekskmreelrisqsrtgsemelvrkpsdvgaprtTEDDsnqeedar 1558
Cdd:cd17300    1 TKFTCTIYFAEQFHALRSLYCG----------------------------------------------GEDD-------- 26
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1559 iaLARSLCKSVQWEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQQQPTLLAKIFGVFRVSVK 1638
Cdd:cd17300   27 --FIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHKRPSLLAKILGVYRISVK 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1639 KKDSFVERS--VMVMENLFYGCNIENKFDLKGSERNRLVDpSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQR 1716
Cdd:cd17300  105 NSTTNKTSKqdLLVMENLFYGRNISQVYDLKGSLRNRYVN-VAEDEDSVLLDENFLEYTKGSPLYLREHSKAVLMAAIWN 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1717 DSSFLEKNLVMDYSLLVGLDKKNGVLVLGIIDYIRTFTLDKRVESIIKGSGILGGkGKDPTVVNPERYKQRFIDAMDRYF 1796
Cdd:cd17300  184 DTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGILGG-GGEPTVISPELYKKRFREAMDKYF 262
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
464-717 6.37e-125

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 392.36  E-value: 6.37e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  464 EQLLAQMLRAHNL--DQEWDKVLQMLCSTAANHFKPEHCSNDLMDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDM 541
Cdd:cd03334    1 RALLAQLLKDEGIsnDESWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  542 ATHVPFPRILLLQCPIVYERIEGKFVTIETVLLQEKEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVK 621
Cdd:cd03334   81 PSKIKNPRILLLQGPLEYQRVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  622 LSVMERLSRTLQCDIVSSIESNITMPKLGYCNDFYIRNYN-----GKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKRVA 696
Cdd:cd03334  161 PSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVeehgrSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVV 240
                        250       260
                 ....*....|....*....|.
gi 20130093  697 SALLFARYNWRLEMSFLLNEF 717
Cdd:cd03334  241 EFMVFAAYHLKLETSFLADEF 261
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1452-1796 1.86e-96

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623  Cd Length: 342  Bit Score: 315.09  E-value: 1.86e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1452 SESEEKSKERIKQPPSPHITLAFQDHSCQFQCKIYFAREFDAMRskslkppkldkslyrrlekskmreelrisqsrtgse 1531
Cdd:smart00330    1 LPSDFKATEKIKFPTPGHLELTPSHGSADFKFKDYCPEVFRNLR------------------------------------ 44
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1532 melvrkpsdvgaprtteddsNQEEDARIALARSLCKSVQ-WEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKY 1610
Cdd:smart00330   45 --------------------ELFGIDPADYLRSLCRSPPlELSSGGKSGSFFYLSLDDRFIIKTVSKSEIKSLLPMLPNY 104
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1611 FEYIdrcqQQQQPTLLAKIFGVFRVSVKKKDsFVERSVMVMENLFY-GCNIENKFDLKGSERNRLVDPSNQQGEIVLLDE 1689
Cdd:smart00330  105 YEHI----VQNPNTLLPKFFGLYRVKVKGGT-EKKIYFLVMENLFYsDLKVHRKYDLKGSTRGREADKKKVKELPVLKDL 179
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1690 NLVQMsWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYSLLVGLDKKNG----------------------------- 1740
Cdd:smart00330  180 DLVEM-WNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERgqreeielppvygsdespssessnggkap 258
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1741 -------------------------------VLVLGIIDYIRTFTLDKRVESIIKGSGILggkGKDPTVVNPERYKQRFI 1789
Cdd:smart00330  259 ditgnllvsnspdgdgpfggiparairarrvVLYLGIIDILQTYTWDKKLEHWVKSIGHD---GKTISVVHPEQYAKRFR 335

                    ....*..
gi 20130093    1790 DAMDRYF 1796
Cdd:smart00330  336 DFMDKYF 342
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1329-1805 6.85e-48

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


Pssm-ID: 227578  Cd Length: 612  Bit Score: 182.45  E-value: 6.85e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1329 SDKKSIRKILTQLLPSGNQVNPLQSPFPAQDHLTLPLGSIPIhVRETDLSSVIAYSLTSMDYQKAideaeaNSNAAHSSP 1408
Cdd:COG5253  206 PDKSLLKRTLSNFWAERNSYNWKPLVYPSCPSEHIFSDSDVI-IREDEPSSLIAFCLSTSDYRNK------MMRLRDSET 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1409 QLKRKIplaesvsdaeDSPSLSRTSSNTSAAPNASvpspaTAASESEEKSKERIKQPPSPHITLAFQDHSCQFQCKIYFA 1488
Cdd:COG5253  279 MDERLL----------NGMPLEGGHRNPQESYNML-----TGIRVTLSRIEEIMIKKTDTHLNEQFEEGLYEFSCKDYFP 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1489 REFDAMRskslkppkldkslyrrlekskmreelrisqsrtgsemelvrKPSDVGAprtteddsnqeedariALARSLCKS 1568
Cdd:COG5253  344 EVFRELR-----------------------------------------ALCGCDE----------------ALVSLLSRY 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1569 VQWEARGGKSGSRFCKTLDDRFVLKEMnSRDMTIFepFAPKYFEYIDRCQQQQQpTLLAKIFGVFRVSVK---KKDSFVE 1645
Cdd:COG5253  367 ILWESNGGKSGSFFLFTRDYKFIIKTI-SHSEHIC--FRPMIFEYYVHVLFNPL-TLLCKIFGFYRVKSRssiSSSKSRK 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1646 RSVMVMENLFYGCNIENKFDLKGSERNRLVDpSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNL 1725
Cdd:COG5253  443 IYFIVMENLFYPHGIHRIFDLKGSMRNRHVE-RTGKSMSVLLDMNDVEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLN 521
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1726 VMDYSLLVGLDKKNGVLVLG-IIDYIRT-FTLDKRVESIIKGSGILGG--KGKDPTVVNPERYKQRFIDAMDRYFLTVPD 1801
Cdd:COG5253  522 IMDYSLLVGIDDEREEASVGlIIDFIRTrMTGDKKLESGIKDKLTVGSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPD 601

                 ....
gi 20130093 1802 RWEG 1805
Cdd:COG5253  602 KKTQ 605
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
182-243 5.21e-40

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that 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] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). 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. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays 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 (hERG) channels. This family also includes the yeast and plant orthologs 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 lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 142.08  E-value: 5.21e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20130093  182 FWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCSK 243
Cdd:cd15725    1 YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
1576-1795 4.51e-38

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: 334569  Cd Length: 283  Bit Score: 144.65  E-value: 4.51e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqqQQQP-TLLAKIFGVFRVSVK--KKDSFVersvmVME 1652
Cdd:pfam01504   12 GKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHV-----KQNPnTLLTRFYGLHRVKLPggKKIYFV-----VMN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   1653 NLFYGC-NIENKFDLKGSERNRLVDPSNQQ-GEIVLLDENLVQMSwsKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYS 1730
Cdd:pfam01504   82 NLFPTDlDIHERYDLKGSTVGRKAKKKEREkNTPTLKDLDFLERK--KKLRLGPEKREALLKQLERDCEFLESLNIMDYS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   1731 LLVGL--------------------------------------------------------------DKKNGVLVLGIID 1748
Cdd:pfam01504  160 LLLGIhdldrgnreslrsstlssfspsgssssssssssrlslnqssersgtvfylddgggraggensEDGDEIYYLGIID 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 20130093   1749 YIRTFTLDKRVESIIKGsgiLGGKGKDPTVVNPERYKQRFIDAMDRY 1795
Cdd:pfam01504  240 ILQEYNLKKKLEHAWKS---LQHDGDSISAVPPKEYAERFLKFIEKI 283
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
511-694 7.60e-29

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 333853  Cd Length: 488  Bit Score: 122.69  E-value: 7.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    511 VNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIE--GKFVT-----IETVLLQEKEYLRNV 583
Cdd:pfam00118  163 IRVVKIKGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKILLLNCSLEYEKTEtkATVVLsdaeeLERFLKAEEEQLLEI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    584 CARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYCNDFYIRNYNGK 663
Cdd:pfam00118  243 VEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGATAVSSLD-DLTPDDLGTAGLVEEREIGDE 321
                          170       180       190
                   ....*....|....*....|....*....|.
gi 20130093    664 TLMFFEKLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:pfam00118  322 KYTFIEGCKSPKAATILLRGATDHVLDEIER 352
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
505-694 1.20e-27

T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274085  Cd Length: 524  Bit Score: 119.46  E-value: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    505 MDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIEGKfVTIE--------TVLLQE 576
Cdd:TIGR02344  188 IDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQ-TNIEitkeedwnRILQME 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    577 KEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGY-CNDF 655
Cdd:TIGR02344  267 EEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPE-ELRESDVGTgCGLF 345
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 20130093    656 YIRNYNGKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:TIGR02344  346 EVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVER 384
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
183-246 4.02e-23

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 334508 [Multi-domain]  Cd Length: 66  Bit Score: 93.97  E-value: 4.02e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130093    183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPG-MIIRCDGDLKVCNYCSKIVL 246
Cdd:pfam01363    2 WVPDSDASNCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKAPLlPHLGSNKPVRVCDACYDTLQ 66
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
183-241 9.61e-20

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 84.41  E-value: 9.61e-20
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093     183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:smart00064    4 WIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDC 62
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1576-1735 1.62e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 79.11  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqQQQQPTLLAKIFGVFRV--SVKKKDSFVersvmVMEN 1653
Cdd:PLN03185  445 GKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHV----KTYENTLITKFFGLHRIkpSSGQKFRFV-----VMGN 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  1654 LFygCN---IENKFDLKGSERNRLVDPsnqqgeiVLLDEN--LVQMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMD 1728
Cdd:PLN03185  516 MF--CTelrIHRRFDLKGSSLGRSADK-------VEIDENttLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMD 586

                  ....*..
gi 20130093  1729 YSLLVGL 1735
Cdd:PLN03185  587 YSLLLGV 593
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
509-694 1.36e-12

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223535  Cd Length: 524  Bit Score: 72.25  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  509 NYVNFKKVPGGRRKDSKIVHGVAFSK-NVAHKDMaTHVPF--PRILLLQCPIVYERIE---GKFVTIETVLL-----QEK 577
Cdd:COG0459  178 DGIIIVKESGGSETELEVVEGMVFDKgYLSPYFM-PDKRLenPKILLLDKKLEIKKPElplEIVISSGKPLLiiaedEEG 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  578 EYLRNVCARIMSFKPNVVLVhkNVAGI---AQDLLRSYEVTLVLDVKLS-VMERLSRTLQCDIVSSIESNITmPKLGY-- 651
Cdd:COG0459  257 EALATLVVNILRGGANVVVV--KAPGIddlAKAYLEDIAILTGRRVKKEdLGERLAKLGGAKIVSVLKDLTT-IVLGEga 333
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20130093  652 CNDFYIRNYNGKTLMFFE--KLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:COG0459  334 AGLVEETKTGDYDMEKLQerKAKAGGVATILVRGATEVELDEKER 378
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
329-397 6.42e-10

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 56.91  E-value: 6.42e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093     329 ITLHEEMQRDLPAQNCGQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMDFDSSLHYKF 397
Cdd:smart00049    7 LRDRKYFLKTYPNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRF 75
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
343-388 4.24e-04

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) PIKfyve-like proteins. PIKfyve contains N-terminal Fyve finger and DEP domains, a central chaperonin-like domain and a C-terminal PIPK (phosphatidylinositol phosphate kinase) domain. PIKfyve-like proteins are important phosphatidylinositol (3)-monophosphate (PtdIns(3)P)-5-kinases, producing PtdIns(3,5)P2, which plays a major role in multivesicular body (MVB) sorting and control of retrograde traffic from the vacuole back to the endosome and/or Golgi. PIKfyve itself has been shown to be play a role in regulating early-endosome-to-trans-Golgi network (TGN) retrograde trafficking.


Pssm-ID: 239895  Cd Length: 81  Bit Score: 40.50  E-value: 4.24e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 20130093  343 NC--GQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMD 388
Cdd:cd04448   27 NCilGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDDLFRD 74
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
449-652 1.80e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 42.71  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   449 TTATSKLLAsyceHEEQLLAQMLRahnldqewDKVLQMlcstaanhfkpeHCSNDLmdirNYVNFKKVPGGRRKDSKIVH 528
Cdd:PTZ00212  167 TTLSSKLLT----VEKDHFAKLAV--------DAVLRL------------KGSGNL----DYIQIIKKPGGTLRDSYLED 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   529 GVAFSKNVA---HKDMAThvpfPRILLLQCPIVYERIE--GKFVTIETVL------LQEKEYLRNVCARIMSFKPNVVLV 597
Cdd:PTZ00212  219 GFILEKKIGvgqPKRLEN----CKILVANTPMDTDKIKiyGAKVKVDSMEkvaeieAAEKEKMKNKVDKILAHGCNVFIN 294
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 20130093   598 HKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYC 652
Cdd:PTZ00212  295 RQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFD-TPEKVKLGHC 348
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
329-397 9.44e-03

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 334170  Cd Length: 72  Bit Score: 36.41  E-value: 9.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20130093    329 ITLHEEMQRDLPAQNC--GQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMDFDSSLHYKF 397
Cdd:pfam00610    2 VKLKDRRKHLKTYPNCftGSEAVDWLMDNLSIIDREEAVELGQLLLDQGLIHHVGDKHGTFKDSSYAFYRF 72
 
Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
1479-1796 1.07e-125

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: 394.57  E-value: 1.07e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1479 CQFQCKIYFAREFDAMRSKSLKppkldkslyrrlekskmreelrisqsrtgsemelvrkpsdvgaprtTEDDsnqeedar 1558
Cdd:cd17300    1 TKFTCTIYFAEQFHALRSLYCG----------------------------------------------GEDD-------- 26
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1559 iaLARSLCKSVQWEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQQQPTLLAKIFGVFRVSVK 1638
Cdd:cd17300   27 --FIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEYMAKALFHKRPSLLAKILGVYRISVK 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1639 KKDSFVERS--VMVMENLFYGCNIENKFDLKGSERNRLVDpSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQR 1716
Cdd:cd17300  105 NSTTNKTSKqdLLVMENLFYGRNISQVYDLKGSLRNRYVN-VAEDEDSVLLDENFLEYTKGSPLYLREHSKAVLMAAIWN 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1717 DSSFLEKNLVMDYSLLVGLDKKNGVLVLGIIDYIRTFTLDKRVESIIKGSGILGGkGKDPTVVNPERYKQRFIDAMDRYF 1796
Cdd:cd17300  184 DTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGILGG-GGEPTVISPELYKKRFREAMDKYF 262
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
464-717 6.37e-125

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 392.36  E-value: 6.37e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  464 EQLLAQMLRAHNL--DQEWDKVLQMLCSTAANHFKPEHCSNDLMDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDM 541
Cdd:cd03334    1 RALLAQLLKDEGIsnDESWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  542 ATHVPFPRILLLQCPIVYERIEGKFVTIETVLLQEKEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVK 621
Cdd:cd03334   81 PSKIKNPRILLLQGPLEYQRVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  622 LSVMERLSRTLQCDIVSSIESNITMPKLGYCNDFYIRNYN-----GKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKRVA 696
Cdd:cd03334  161 PSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVeehgrSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVV 240
                        250       260
                 ....*....|....*....|.
gi 20130093  697 SALLFARYNWRLEMSFLLNEF 717
Cdd:cd03334  241 EFMVFAAYHLKLETSFLADEF 261
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1452-1796 1.86e-96

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623  Cd Length: 342  Bit Score: 315.09  E-value: 1.86e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1452 SESEEKSKERIKQPPSPHITLAFQDHSCQFQCKIYFAREFDAMRskslkppkldkslyrrlekskmreelrisqsrtgse 1531
Cdd:smart00330    1 LPSDFKATEKIKFPTPGHLELTPSHGSADFKFKDYCPEVFRNLR------------------------------------ 44
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1532 melvrkpsdvgaprtteddsNQEEDARIALARSLCKSVQ-WEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKY 1610
Cdd:smart00330   45 --------------------ELFGIDPADYLRSLCRSPPlELSSGGKSGSFFYLSLDDRFIIKTVSKSEIKSLLPMLPNY 104
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1611 FEYIdrcqQQQQPTLLAKIFGVFRVSVKKKDsFVERSVMVMENLFY-GCNIENKFDLKGSERNRLVDPSNQQGEIVLLDE 1689
Cdd:smart00330  105 YEHI----VQNPNTLLPKFFGLYRVKVKGGT-EKKIYFLVMENLFYsDLKVHRKYDLKGSTRGREADKKKVKELPVLKDL 179
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1690 NLVQMsWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYSLLVGLDKKNG----------------------------- 1740
Cdd:smart00330  180 DLVEM-WNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIERgqreeielppvygsdespssessnggkap 258
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    1741 -------------------------------VLVLGIIDYIRTFTLDKRVESIIKGSGILggkGKDPTVVNPERYKQRFI 1789
Cdd:smart00330  259 ditgnllvsnspdgdgpfggiparairarrvVLYLGIIDILQTYTWDKKLEHWVKSIGHD---GKTISVVHPEQYAKRFR 335

                    ....*..
gi 20130093    1790 DAMDRYF 1796
Cdd:smart00330  336 DFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
1575-1794 3.14e-54

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: 190.09  E-value: 3.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1575 GGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQqqqpTLLAKIFGVFRVSVKKKDSFverSVMVMENL 1654
Cdd:cd00139   44 EGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYYEHIKKNPN----SLLTRFYGLYSIKLQKGKKV---YFVVMENV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1655 FYGCN-IENKFDLKGSERNRLVDPSNQQ--GEIVLLDENLVQMSWSkpLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYSL 1731
Cdd:cd00139  117 FPTDLkIHERYDLKGSTVGRRVSKEKEKkkGLKVLKDLDFLEKGEK--IILGPEDRAELLEQLEKDVEFLRSLNIMDYSL 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130093 1732 LVGLDKKngVLVLGIIDYIRTFTLDKRVESIIKgsGILGGKGKDPTVVNPERYKQRFIDAMDR 1794
Cdd:cd00139  195 LVGIHRL--VYYLGIIDILQEYNLRKKLERFLK--SLLYGKDSGISCVPPDEYAERFLKFMES 253
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
464-709 1.12e-48

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 172.65  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  464 EQLLAQMLR--AHNLDQEWDKVLQMLCSTAANHFKPEhcsnDLMDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDM 541
Cdd:cd03333    1 RELLLQVATtsLNSKLSSWDDFLGKLVVDAVLKVGPD----NRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  542 ATHVPFPRILLLQCPIVYeriegkfvtietvllqekeylrnvcarimsfkpnVVLVHKNVAGIAQDLLRSYEVTLVLDVK 621
Cdd:cd03333   77 PKRLENAKILLLDCPLEY----------------------------------VVIAEKGIDDLALHYLAKAGIMAVRRVK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  622 LSVMERLSRTLQCDIVSSIEsNITMPKLGYCNDFYIRNYNGKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKRVASALLF 701
Cdd:cd03333  123 KEDLERIARATGATIVSSLE-DLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALC 201

                 ....*...
gi 20130093  702 ARYNWRLE 709
Cdd:cd03333  202 AVRAAVEE 209
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1329-1805 6.85e-48

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


Pssm-ID: 227578  Cd Length: 612  Bit Score: 182.45  E-value: 6.85e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1329 SDKKSIRKILTQLLPSGNQVNPLQSPFPAQDHLTLPLGSIPIhVRETDLSSVIAYSLTSMDYQKAideaeaNSNAAHSSP 1408
Cdd:COG5253  206 PDKSLLKRTLSNFWAERNSYNWKPLVYPSCPSEHIFSDSDVI-IREDEPSSLIAFCLSTSDYRNK------MMRLRDSET 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1409 QLKRKIplaesvsdaeDSPSLSRTSSNTSAAPNASvpspaTAASESEEKSKERIKQPPSPHITLAFQDHSCQFQCKIYFA 1488
Cdd:COG5253  279 MDERLL----------NGMPLEGGHRNPQESYNML-----TGIRVTLSRIEEIMIKKTDTHLNEQFEEGLYEFSCKDYFP 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1489 REFDAMRskslkppkldkslyrrlekskmreelrisqsrtgsemelvrKPSDVGAprtteddsnqeedariALARSLCKS 1568
Cdd:COG5253  344 EVFRELR-----------------------------------------ALCGCDE----------------ALVSLLSRY 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1569 VQWEARGGKSGSRFCKTLDDRFVLKEMnSRDMTIFepFAPKYFEYIDRCQQQQQpTLLAKIFGVFRVSVK---KKDSFVE 1645
Cdd:COG5253  367 ILWESNGGKSGSFFLFTRDYKFIIKTI-SHSEHIC--FRPMIFEYYVHVLFNPL-TLLCKIFGFYRVKSRssiSSSKSRK 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1646 RSVMVMENLFYGCNIENKFDLKGSERNRLVDpSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNL 1725
Cdd:COG5253  443 IYFIVMENLFYPHGIHRIFDLKGSMRNRHVE-RTGKSMSVLLDMNDVEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLN 521
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1726 VMDYSLLVGLDKKNGVLVLG-IIDYIRT-FTLDKRVESIIKGSGILGG--KGKDPTVVNPERYKQRFIDAMDRYFLTVPD 1801
Cdd:COG5253  522 IMDYSLLVGIDDEREEASVGlIIDFIRTrMTGDKKLESGIKDKLTVGSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPD 601

                 ....
gi 20130093 1802 RWEG 1805
Cdd:COG5253  602 KKTQ 605
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
182-243 5.21e-40

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that 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] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). 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. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays 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 (hERG) channels. This family also includes the yeast and plant orthologs 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 lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 142.08  E-value: 5.21e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20130093  182 FWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCSK 243
Cdd:cd15725    1 YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
1576-1795 4.51e-38

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: 334569  Cd Length: 283  Bit Score: 144.65  E-value: 4.51e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqqQQQP-TLLAKIFGVFRVSVK--KKDSFVersvmVME 1652
Cdd:pfam01504   12 GKSGSFFYFSRDDRFIIKTITKSEHKFLRKILPDYYEHV-----KQNPnTLLTRFYGLHRVKLPggKKIYFV-----VMN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   1653 NLFYGC-NIENKFDLKGSERNRLVDPSNQQ-GEIVLLDENLVQMSwsKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYS 1730
Cdd:pfam01504   82 NLFPTDlDIHERYDLKGSTVGRKAKKKEREkNTPTLKDLDFLERK--KKLRLGPEKREALLKQLERDCEFLESLNIMDYS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   1731 LLVGL--------------------------------------------------------------DKKNGVLVLGIID 1748
Cdd:pfam01504  160 LLLGIhdldrgnreslrsstlssfspsgssssssssssrlslnqssersgtvfylddgggraggensEDGDEIYYLGIID 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 20130093   1749 YIRTFTLDKRVESIIKGsgiLGGKGKDPTVVNPERYKQRFIDAMDRY 1795
Cdd:pfam01504  240 ILQEYNLKKKLEHAWKS---LQHDGDSISAVPPKEYAERFLKFIEKI 283
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
1576-1794 1.80e-30

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: 123.55  E-value: 1.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqQQQQPTLLAKIFGVFRVSVK--KKDSFVersvmVMEN 1653
Cdd:cd17302   98 GKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKHV----KAYENTLLTKFFGVHRVKPVggRKVRFV-----VMGN 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1654 LFygCN---IENKFDLKGSERNRLVDPSNQQGE--IVLLDENL-----VQMSWskplyvlshsKTVLRDAIQRDSSFLEK 1723
Cdd:cd17302  169 LF--CTelrIHRRFDLKGSTHGRTTGKPESEIDpnTTLKDLDLdfkfrLEKGW----------RDALMRQIDADCAFLEA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1724 NLVMDYSLLVGLDKKNG---------VLVLGIIDYIRTFTLDKRVESIIKGsgiLGGKGKDPTVVNPERYKQRFIDAMDR 1794
Cdd:cd17302  237 LRIMDYSLLLGVHFRAGdstgepydvVLYFGIIDILQEYNISKKLEHAYKS---LQYDPASISAVDPKLYSRRFRDFIRK 313
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
1563-1794 1.14e-29

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: 120.84  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1563 RSLCKSV-QWEARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQqqpTLLAKIFGVFRVSVKKKD 1641
Cdd:cd17305   79 NSLTRSQpLASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQYIVERHGK---TLLPQYLGMYRITVNGVE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1642 SFVersvMVMENLF-YGCNIENKFDLKGSERNRLVDPSNQQGEI-VLLDENLVQMSWSkpLYVLSHSKTVLRDAIQRDSS 1719
Cdd:cd17305  156 TYL----VVMRNVFsPRLPIHKKYDLKGSTVDRQASDKEKAKDLpTLKDNDFLNDGTK--IYIGDEAKAKLLETLKRDVE 229
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130093 1720 FLEKNLVMDYSLLVGLdkKNGVLVLGIIDYIRTFTLDKRVESIIKgsGILGGKGKDPTVVNPERYKQRFIDAMDR 1794
Cdd:cd17305  230 FLAKLNLMDYSLLVGI--HDCIYFMAIIDILTHYGAKKRAAHAAK--TVKHGAGAEISTVKPEQYAKRFLEFISK 300
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
511-694 7.60e-29

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 333853  Cd Length: 488  Bit Score: 122.69  E-value: 7.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    511 VNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIE--GKFVT-----IETVLLQEKEYLRNV 583
Cdd:pfam00118  163 IRVVKIKGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKILLLNCSLEYEKTEtkATVVLsdaeeLERFLKAEEEQLLEI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    584 CARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYCNDFYIRNYNGK 663
Cdd:pfam00118  243 VEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGATAVSSLD-DLTPDDLGTAGLVEEREIGDE 321
                          170       180       190
                   ....*....|....*....|....*....|.
gi 20130093    664 TLMFFEKLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:pfam00118  322 KYTFIEGCKSPKAATILLRGATDHVLDEIER 352
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
505-694 1.20e-27

T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274085  Cd Length: 524  Bit Score: 119.46  E-value: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    505 MDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIEGKfVTIE--------TVLLQE 576
Cdd:TIGR02344  188 IDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQ-TNIEitkeedwnRILQME 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    577 KEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGY-CNDF 655
Cdd:TIGR02344  267 EEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPE-ELRESDVGTgCGLF 345
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 20130093    656 YIRNYNGKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:TIGR02344  346 EVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVER 384
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1576-1792 3.18e-26

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: 110.91  E-value: 3.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQqqpTLLAKIFGVFRVSVKKkdsfVERSVMVMENLF 1655
Cdd:cd17310  104 GRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGN---TLLPQFLGMYRLTVDG----VETYMVVTRNVF 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1656 -YGCNIENKFDLKGSERNRLVDPSNQQGEIVLLDENLVqMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYSLLVG 1734
Cdd:cd17310  177 sHRLTVHRKYDLKGSTVSREASDKEKAKDLPTFKDNDF-LNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVG 255
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20130093 1735 LdkKNGVLVLGIIDYIRTFTLDKRVESIIKgsGILGGKGKDPTVVNPERYKQRFIDAM 1792
Cdd:cd17310  256 I--HDVVYFMAIIDILTPYDAKKKAAHAAK--TVKHGAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1576-1790 3.15e-23

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: 102.36  E-value: 3.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQqqpTLLAKIFGVFRVSVKKkdsfVERSVMVMENLF 1655
Cdd:cd17309  102 ARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGN---TLLPQFLGMYRLTVDG----VETYMIVTRNVF 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1656 -YGCNIENKFDLKGSERNRLVDPSNQQGEIVLLDENLVqMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDYSLLVG 1734
Cdd:cd17309  175 sHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDF-INDGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVG 253
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20130093 1735 LdkKNGVLVLGIIDYIRTFTLDKRVESIIKgsGILGGKGKDPTVVNPERYKQRFID 1790
Cdd:cd17309  254 I--HDVVYFMAIIDILTHYDAKKKAAHAAK--TVKHGAGAEISTVNPEQYSKRFLD 305
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
183-246 4.02e-23

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 334508 [Multi-domain]  Cd Length: 66  Bit Score: 93.97  E-value: 4.02e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130093    183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPG-MIIRCDGDLKVCNYCSKIVL 246
Cdd:pfam01363    2 WVPDSDASNCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKAPLlPHLGSNKPVRVCDACYDTLQ 66
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1577-1793 4.76e-23

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: 102.05  E-value: 4.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1577 KSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqqQQQP-TLLAKIFGVFRVSV--KKKDSFVersvmVMEN 1653
Cdd:cd17304   91 KSGQDFFLTNDKRFFLKTQTKREAKFLLSILRKYVQHL-----ENYPhSLLVKFLGVHSIKLpgKKKKYFI-----VMQS 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1654 LFY-GCNIENKFDLKGSERNRLVDPSNQ--QGEIVLLDENLVqmswSKPLYvLSHSKTVLRDAIQRDSSFLEKNLVMDYS 1730
Cdd:cd17304  161 VFYpDERINERYDIKGCQVSRYTDPEPEgsQIIVVLKDLNFE----GNSIN-LGQQRSWFLRQVEIDTEFLKGLNVLDYS 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1731 LLVGL-------------DKKNGVLVL---------GIIDYIRTFTLDKRVESIIKgsgILGGKGKDPTVVNPERYKQRF 1788
Cdd:cd17304  236 LLVGFqplhsdenrrllpNYKNALHVVdgpeyryfvGIIDIFTVYGLRKRLEHLWK---SLRYPGQSFSTVSPEKYARRF 312

                 ....*
gi 20130093 1789 IDAMD 1793
Cdd:cd17304  313 CQWVE 317
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
1564-1792 9.46e-23

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: 101.17  E-value: 9.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1564 SLCKSVQWE-ARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqQQQQPTLLAKIFGVFRVSVKKKD- 1641
Cdd:cd17301   82 SLCNEPLRElSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYYMNL----NQNPRTLLPKFYGLYCYQSGGKNi 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1642 SFVersvmVMENLF-YGCNIENKFDLKGSERNRLVDPSNQQGEI-VLLDENLVQMsWSKPLYVLSHSKTVLRDAIQRDSS 1719
Cdd:cd17301  158 RFV-----VMNNLLpSNIKMHEKYDLKGSTYKRKASKKERQKKSpTLKDLDFMED-HPEGILLEPDTYDALLKTIQRDCR 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1720 FLEKNLVMDYSLLVGLDKKNGV-----------LVLGIIDYIRTFTLDKRVESIIKgSGILGGkgkDP-TVVNPERYKQR 1787
Cdd:cd17301  232 VLESFKIMDYSLLLGVHNLGGIparnskgerllLFIGIIDILQSYRLKKKLEHTWK-SVVHDG---DTvSVHRPSFYAER 307

                 ....*
gi 20130093 1788 FIDAM 1792
Cdd:cd17301  308 FQNFM 312
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1554-1790 1.77e-21

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: 96.86  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1554 EEDARIALARSlckSVQWEARGgkSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDRCQQQqqpTLLAKIFGVF 1633
Cdd:cd17311   74 DQDYQVSLTRS---PPYSESEG--SDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYIVKCHGN---TLLPQFLGMY 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1634 RVSVKKKDSFVersvMVMENLF-YGCNIENKFDLKGSERNRLVDPSNQQGEIVLLdENLVQMSWSKPLYVLSHSKTVLRD 1712
Cdd:cd17311  146 RLSVDNEDSYM----LVMRNMFsHRLPVHRKYDLKGSLVSREASDKEKVKELPTL-KDMDFLNKNQKVYVGEEQKRIFLE 220
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20130093 1713 AIQRDSSFLEKNLVMDYSLLVGLdkKNGVLVLGIIDYIRTFTLDKRVESIIKgsGILGGKGKDPTVVNPERYKQRFID 1790
Cdd:cd17311  221 KLKRDVEFLVQLKIMDYSLLLGI--HDVVYFMGLIDILTQYDAKKKAAHAAK--TVKHGAGAEISTVHPEQYAKRFLD 294
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
1576-1794 3.15e-21

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: 96.60  E-value: 3.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqqQQQP-TLLAKIFGVFRVSVKK--KDSFVersvmVME 1652
Cdd:cd17303   95 GKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHV-----KENPnTLLSQFYGLHRVKMPRgrKIHFV-----VMN 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1653 NLF-YGCNIENKFDLKGSERNRLVDPSN--QQGEIVLLDENLVQMSwsKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMDY 1729
Cdd:cd17303  165 NLFpPHRDIHQTFDLKGSTVGRETPEDKlaKGPRATLKDLNWLRRK--RKLALGPEKRKQFLTQLKRDVEFLASLNIMDY 242
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093 1730 SLLVGLDKKNG--------------VLVLGIIDYIRTFTLDKRVESIIKGsgiLGGKGKDPTVVNPERYKQRFIDAMDR 1794
Cdd:cd17303  243 SLLVGIHDLDGgfqatdennepgdeIYYLGIIDILTPYNAKKKLEHFFKS---LRHDRHTISAVPPKEYARRFLKFIED 318
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
183-241 9.61e-20

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 84.41  E-value: 9.61e-20
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093     183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:smart00064    4 WIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDC 62
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
508-746 1.09e-19

cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239459  Cd Length: 517  Bit Score: 94.64  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  508 RNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIEGKF---VT----IETVLLQEKEYL 580
Cdd:cd03343  189 LDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAkirITspdqLQAFLEQEEAML 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  581 RNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYCNDFYIRNY 660
Cdd:cd03343  269 KEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNID-DLTPEDLGEAELVEERKV 347
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  661 NGKTLMFFEKLTNPRGYTCLLRGGSN---AELTR-----VKRVASALLFARYNW-----RLEMSFLLNEFAQPLSPKPSI 727
Cdd:cd03343  348 GDDKMVFVEGCKNPKAVTILLRGGTEhvvDELERaledaLRVVADALEDGKVVAgggavEIELAKRLREYARSVGGREQL 427
                        250       260       270
                 ....*....|....*....|....*....|....
gi 20130093  728 ----F-DSKETSPKT----------ETEAELRSK 746
Cdd:cd03343  428 aveaFaDALEEIPRTlaenagldpiDTLVELRAA 461
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
502-694 1.88e-19

chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 238189  Cd Length: 464  Bit Score: 93.65  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  502 NDLMDIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYeriegkfvtietvllqekeylr 581
Cdd:cd00309  173 ENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------------------- 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  582 nvcarimsfkpnVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYCNDFYIRNYN 661
Cdd:cd00309  231 ------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLE-DLTPEDLGTAGLVEETKIG 297
                        170       180       190
                 ....*....|....*....|....*....|...
gi 20130093  662 GKTLMFFEKLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:cd00309  298 DEKYTFIEGCKGGKVATILLRGATEVELDEAER 330
thermosome_arch TIGR02339
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
448-724 4.86e-19

thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274080  Cd Length: 519  Bit Score: 92.83  E-value: 4.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    448 YTTATSKLLAsycEHEEQLLAQMLrahnldqeWDKVLQMLcstaanhfkpEHCSND--LMDIRNyVNFKKVPGGRRKDSK 525
Cdd:TIGR02339  152 YTSLTSKASA---EVAKDKLADLV--------VEAVKQVA----------ELRGDGkyYVDLDN-IKIVKKKGGSIEDTE 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    526 IVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIEGKF-VTIETV------LLQEKEYLRNVCARIMSFKPNVVLVH 598
Cdd:TIGR02339  210 LVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAkIRITDPdqikkfLDQEEAMLKEMVDKIASAGANVVICQ 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    599 KNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIESnITMPKLGYCNDFYIRNYNGKTLMFFEKLTNPRGYT 678
Cdd:TIGR02339  290 KGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDE-ITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVT 368
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093    679 CLLRGGSNAELTRVKR--------VASALLFARY-----NWRLEMSFLLNEFAQPLSPK 724
Cdd:TIGR02339  369 ILLRGGTEHVVDELERsiqdalhvVANALEDGKIvagggAVEIELALRLRSYARSVGGR 427
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
191-241 3.35e-17

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 76.80  E-value: 3.35e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20130093  191 ECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:cd00065    1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSC 51
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1564-1793 3.81e-17

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: 84.27  E-value: 3.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1564 SLCKSVQWE-ARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDrcqqQQQPTLLAKIFGVFRVsvkkKDS 1642
Cdd:cd17307   82 SICSEPLIElSNPGASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLN----QNPRTLLPKFYGLYCM----QSG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1643 FVERSVMVMENLF-YGCNIENKFDLKGSE-RNRLVDPSNQQGEIVLLDENLVQMSwSKPLYVLSHSKTVLRDAIQRDSSF 1720
Cdd:cd17307  154 GINIRIVVMNNVLpRSVKMHYKYDLKGSTyKRRASRKEREKSCPTYKDLDFLQDM-HDGLYFDPETYNALMKTLQRDCRV 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1721 LEKNLVMDYSLLVGLDKKNGV-----------LVLGIIDYIRTFTLDKRVESIIKGsgiLGGKGKDPTVVNPERYKQRFI 1789
Cdd:cd17307  233 LESFKIMDYSLLLGIHVLGGIpaknhkgekllLFMGIIDILQSYRLMKKLEHSWKA---LVYDGDTVSVHRPSFYADRFL 309

                 ....
gi 20130093 1790 DAMD 1793
Cdd:cd17307  310 KFMN 313
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
183-241 3.54e-16

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 74.30  E-value: 3.54e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:cd15731    5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHC 63
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1564-1792 3.69e-16

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: 81.58  E-value: 3.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1564 SLCKSVQWE-ARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDrcqqQQQPTLLAKIFGVFRVSVKKKDS 1642
Cdd:cd17308   83 SLCNEPLIElSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLN----QNPRTLLPKFYGLYCVQSGGKNI 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1643 fverSVMVMENLF-YGCNIENKFDLKGSERNRLVDPSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQRDSSFL 1721
Cdd:cd17308  159 ----RVVVMNNILpRVVKMHLKFDLKGSTYKRRASKKEREKSKPTFKDLDFMQDMPEGLMLDADTFSALVKTLQRDCLVL 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1722 EKNLVMDYSLLVGLDKKNGV-----------LVLGIIDYIRTFTLDKRVESIIKGsgiLGGKGKDPTVVNPERYKQRFID 1790
Cdd:cd17308  235 ESFKIMDYSLLLGVHNIGGIpavngkgerllLYIGIIDILQSYRLIKKLEHTWKA---LVHDGDTVSVHRPSFYAERFFK 311

                 ..
gi 20130093 1791 AM 1792
Cdd:cd17308  312 FM 313
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
181-245 4.42e-16

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 73.97  E-value: 4.42e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20130093  181 RFWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCC--NQVVPGMiircDGDLKVCNYCSKIV 245
Cdd:cd15730    1 RKWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSskTATTPSS----KKPVRVCDACFDDL 63
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
183-243 4.83e-16

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 73.95  E-value: 4.83e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVV--PGMiirCDGD-LKVCNYCSK 243
Cdd:cd15727    4 WVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVplPRM---CFVDpVRVCNECAL 64
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
183-235 7.85e-16

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276  Cd Length: 83  Bit Score: 74.08  E-value: 7.85e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCS----KCCNQVVPGMIIRCDGDL 235
Cdd:cd15737    2 WEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTEVPLDLLSSALPDL 58
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
182-222 8.27e-16

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 73.16  E-value: 8.27e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 20130093  182 FWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQ 222
Cdd:cd15729    6 VWVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSL 46
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
506-746 3.64e-15

TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239453  Cd Length: 480  Bit Score: 80.03  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  506 DIRNYVNFKKVPGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIvyeriegkfvtietvllqekEYLrnvca 585
Cdd:cd03337  190 DIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL--------------------EYL----- 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  586 rimsfkpnvVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLG-YCNDFYIRNYNGKT 664
Cdd:cd03337  245 ---------VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPE-ELTESDVGtGAGLFEVKKIGDEY 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  665 LMFFEKLTNPRGYTCLLRGGSNAELTRVKR-VASALLFAR---YNWRL-------EM--SFLLNEFAQPL-----SPKPS 726
Cdd:cd03337  315 FTFITECKDPKACTILLRGASKDVLNEVERnLQDAMAVARniiLNPKLvpgggatEMavSHALSEKAKSIegveqWPYKA 394
                        250       260       270
                 ....*....|....*....|....*....|
gi 20130093  727 IFDSKETSPKT----------ETEAELRSK 746
Cdd:cd03337  395 VASALEVIPRTlaqncganviRTLTELRAK 424
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
183-241 9.03e-15

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 70.15  E-value: 9.03e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:cd15733    1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSC 59
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
182-242 1.00e-14

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 70.05  E-value: 1.00e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20130093  182 FWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCS 242
Cdd:cd15734    1 YWVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPCA 61
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
182-241 1.14e-14

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 69.93  E-value: 1.14e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  182 FWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:cd15732    1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSC 60
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1576-1735 1.62e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 79.11  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  1576 GKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIdrcqQQQQPTLLAKIFGVFRV--SVKKKDSFVersvmVMEN 1653
Cdd:PLN03185  445 GKSGSVFFLSQDDRFMIKTLRKSEVKVLLRMLPDYHHHV----KTYENTLITKFFGLHRIkpSSGQKFRFV-----VMGN 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  1654 LFygCN---IENKFDLKGSERNRLVDPsnqqgeiVLLDEN--LVQMSWSKPLYVLSHSKTVLRDAIQRDSSFLEKNLVMD 1728
Cdd:PLN03185  516 MF--CTelrIHRRFDLKGSSLGRSADK-------VEIDENttLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMD 586

                  ....*..
gi 20130093  1729 YSLLVGL 1735
Cdd:PLN03185  587 YSLLLGV 593
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
183-246 1.72e-14

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256  Cd Length: 61  Bit Score: 69.29  E-value: 1.72e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGmiIRCdgdlkvCNYCSKIVL 246
Cdd:cd15716    4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPLH--IRC------CHHCKDLLE 59
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
183-241 7.13e-14

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 67.32  E-value: 7.13e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  183 WMPDSkakECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDL-KVCNYC 241
Cdd:cd15760    2 WKPDS---RCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLGPLGVPqRVCDRC 58
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
183-225 2.03e-13

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 66.25  E-value: 2.03e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVP 225
Cdd:cd15721    1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMP 43
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
183-242 2.48e-13

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265  Cd Length: 58  Bit Score: 66.04  E-value: 2.48e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVpgMIIRCDGDLKVCNYCS 242
Cdd:cd15726    1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYV--LTAHGGKKERCCKACF 58
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
191-241 9.40e-13

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 64.33  E-value: 9.40e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20130093  191 ECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQ--VVPGMIIrcDGDLKVCNYC 241
Cdd:cd15720    7 ECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKssTIPKFGI--EKEVRVCDPC 57
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
192-241 1.20e-12

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 63.98  E-value: 1.20e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPgmIIRCDGD--LKVCNYC 241
Cdd:cd15728   10 CYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVP--IIKFDLNkpVRVCDVC 59
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
509-694 1.36e-12

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223535  Cd Length: 524  Bit Score: 72.25  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  509 NYVNFKKVPGGRRKDSKIVHGVAFSK-NVAHKDMaTHVPF--PRILLLQCPIVYERIE---GKFVTIETVLL-----QEK 577
Cdd:COG0459  178 DGIIIVKESGGSETELEVVEGMVFDKgYLSPYFM-PDKRLenPKILLLDKKLEIKKPElplEIVISSGKPLLiiaedEEG 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  578 EYLRNVCARIMSFKPNVVLVhkNVAGI---AQDLLRSYEVTLVLDVKLS-VMERLSRTLQCDIVSSIESNITmPKLGY-- 651
Cdd:COG0459  257 EALATLVVNILRGGANVVVV--KAPGIddlAKAYLEDIAILTGRRVKKEdLGERLAKLGGAKIVSVLKDLTT-IVLGEga 333
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20130093  652 CNDFYIRNYNGKTLMFFE--KLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:COG0459  334 AGLVEETKTGDYDMEKLQerKAKAGGVATILVRGATEVELDEKER 378
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1564-1788 3.93e-12

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: 69.64  E-value: 3.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1564 SLCKSVQWE-ARGGKSGSRFCKTLDDRFVLKEMNSRDMTIFEPFAPKYFEYIDrcqqQQQPTLLAKIFGVFRVSVKKKDS 1642
Cdd:cd17306   85 SLCSEPLIElSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLN----QNPRTLLPKFYGLYCVQAGGKNI 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1643 fverSVMVMENLF-YGCNIENKFDLKGSERNRLVDPSNQQGEIVLLDENLVQMSWSKPLYVLSHSKTVLRDAIQRDSSFL 1721
Cdd:cd17306  161 ----RIVVMNNLLpRSVKMHLKYDLKGSTYKRRASQKEREKPLPTYKDLDFLQDIPDGLFLDSDMYNALCKTLQRDCLVL 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093 1722 EKNLVMDYSLLVG---LDKKNG----------------------VLVLGIIDYIRTFTLDKRVESIIKGsgiLGGKGKDP 1776
Cdd:cd17306  237 QSFKIMDYSLLVGihnIDARRGgtietddqmggiparnskgerlLLYIGIIDILQSYRFVKKLEHSWKA---LVHDGDTV 313
                        250
                 ....*....|..
gi 20130093 1777 TVVNPERYKQRF 1788
Cdd:cd17306  314 SVHRPGFYAERF 325
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
183-219 4.04e-12

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 62.79  E-value: 4.04e-12
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKC 219
Cdd:cd15719    3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKC 39
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
183-241 4.44e-12

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 62.74  E-value: 4.44e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVP-GMIIRcdgDLKVCNYC 241
Cdd:cd15739    4 WQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPsGPNRR---PARVCDVC 60
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
183-246 1.72e-11

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 61.23  E-value: 1.72e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPgmIIRCDGDLKVCNYCSKIVL 246
Cdd:cd15758    6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELA--LPSYPKPVRVCDSCHTLLL 67
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
192-242 4.32e-11

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 59.44  E-value: 4.32e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCS 242
Cdd:cd15745    2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY 52
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
183-225 1.23e-10

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277  Cd Length: 61  Bit Score: 58.49  E-value: 1.23e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 20130093  183 WMPDSKAKECyDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVP 225
Cdd:cd15738    3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRA 44
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
183-222 1.94e-10

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 57.76  E-value: 1.94e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 20130093  183 WMPDSKAKECYDCSQ-KFSTFRRKHHCRLCGQIFCSKCCNQ 222
Cdd:cd15717    2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSK 42
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
329-397 6.42e-10

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 56.91  E-value: 6.42e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093     329 ITLHEEMQRDLPAQNCGQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMDFDSSLHYKF 397
Cdd:smart00049    7 LRDRKYFLKTYPNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGPNKHTFKDSKALYRF 75
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
445-687 1.11e-09

TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239454  Cd Length: 515  Bit Score: 62.69  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  445 DRCYTTATSKLLASYceheEQLLAQMLRahnldqewDKVLQMLcstaanhfKPEHCSN-DLMDIRNyvnFKKVpGGRRKD 523
Cdd:cd03338  141 KSATTSLNSKVVSQY----SSLLAPIAV--------DAVLKVI--------DPATATNvDLKDIRI---VKKL-GGTIED 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  524 SKIVHGVAFSKNVAHKD-MATHVPFPRILLLQCPIVYER--IEGKFV-----TIETVLLQEKEYLRNVCARIMSFKPNVV 595
Cdd:cd03338  197 TELVDGLVFTQKASKKAgGPTRIEKAKIGLIQFCLSPPKtdMDNNIVvndyaQMDRILREERKYILNMCKKIKKSGCNVL 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  596 LVHKN-----VAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIESnITMPKLGYCNDFYIRNYNGKTLMFFEK 670
Cdd:cd03338  277 LIQKSilrdaVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDH-FTEDKLGSADLVEEVSLGDGKIVKITG 355
                        250
                 ....*....|....*....
gi 20130093  671 LTNPrGYTC--LLRgGSNA 687
Cdd:cd03338  356 VKNP-GKTVtiLVR-GSNK 372
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
192-241 1.35e-09

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 55.23  E-value: 1.35e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:cd15735    9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGC 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
183-246 3.40e-09

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 54.65  E-value: 3.40e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPgmIIRCDGDLKVCNYCSKIVL 246
Cdd:cd15759    4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELP--LPSSPKPVRVCDSCHAMLI 65
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
183-245 3.67e-09

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 54.27  E-value: 3.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20130093  183 WMPDSKAKECYDCSQ-KFSTFRRKHHCRLCGQIFCSKCCNQ--VVPGmiiRCDGDLKVCNYCSKIV 245
Cdd:cd15755    2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKkfLLPS---QSSKPVRVCDFCYDLL 64
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
183-243 9.18e-09

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 53.04  E-value: 9.18e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130093  183 WMPDSKAKECYDCSQ-KFSTFRRKHHCRLCGQIFCSKCCNQ--VVPGMIIRcdgDLKVCNYCSK 243
Cdd:cd15754    2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRQrfLIPRLSPK---PVRVCSLCYR 62
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
183-241 9.86e-09

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 52.90  E-value: 9.86e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  183 WMPDSKAKECYDCS-QKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRcDGDLKVCNYC 241
Cdd:cd15724    1 WVPDEAVSVCMVCQvERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYR-ENPVRVCDQC 59
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
183-241 1.53e-08

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 52.44  E-value: 1.53e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20130093  183 WMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRcDGDLKVCNYC 241
Cdd:cd15743    3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLK-NKSARVCDEC 60
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
191-225 3.42e-08

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 51.35  E-value: 3.42e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 20130093  191 ECYDCSQKFSTF-RRKHHCRLCGQIFCSKCCNQVVP 225
Cdd:cd15723    1 NCTGCGASFSVLlKKRRSCNNCGNAFCSRCCSKKVP 36
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
449-694 3.42e-08

T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274086  Cd Length: 523  Bit Score: 58.23  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    449 TTATSKLLAsyceHEEQLLAQMLRahnldqewDKVLQMlcstaanhfkpehcSNDLMDiRNYVNFKKVPGGRRKDSKIVH 528
Cdd:TIGR02345  158 TALSSKLIS----HNKEFFSKMIV--------DAVLSL--------------DRDDLD-LKLIGIKKVQGGALEDSQLVN 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    529 GVAFSKN---VAHKDMATHVPFPRILLLQCPIVY--ERiEGKFVTIETVllqeKEYLRNVCA----------RIMSFKPN 593
Cdd:TIGR02345  211 GVAFKKTfsyAGFEQQPKKFANPKILLLNVELELkaEK-DNAEIRVEDV----EDYQAIVDAewaiifrkleKIVESGAN 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    594 VVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIeSNITMPKLGYCNDFYIRNYNGKTLMFFEKLTN 673
Cdd:TIGR02345  286 VVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTT-SDLEADVLGTCALFEERQIGSERYNYFTGCPH 364
                          250       260
                   ....*....|....*....|.
gi 20130093    674 PRGYTCLLRGGSNAELTRVKR 694
Cdd:TIGR02345  365 AKTCTIILRGGAEQFIEEAER 385
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
183-245 1.21e-07

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 50.18  E-value: 1.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20130093  183 WMPDSKAKECYDCSQKFST-FRRKHHCRLCGQIFCSKCCNQVVPgmiIRCDGDL--KVCNYCSKIV 245
Cdd:cd15741    3 WVRDNEVTMCMRCKEPFNAlTRRRHHCRACGYVVCWKCSDYKAT---LEYDGNKlnRVCKHCYVIL 65
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
192-241 2.93e-07

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 48.66  E-value: 2.93e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKC--CNQVVPGmiiRCDGDLKVCNYC 241
Cdd:cd15749    2 CFGCAAKFSLFKKECGCKNCGRSFCKGCltFSAVVPR---KGNQKQKVCKQC 50
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
192-225 4.95e-07

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275  Cd Length: 56  Bit Score: 47.95  E-value: 4.95e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVP 225
Cdd:cd15736    2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIP 35
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
497-694 1.17e-06

T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274083  Cd Length: 517  Bit Score: 53.25  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    497 PEHCSN-DLMDIRNyvnFKKVpGGRRKDSKIVHGVAFSKNVAH-KDMATHVPFPRILLLQCPIVYER-------IEGKFV 567
Cdd:TIGR02342  174 PENAKNvDLNDIKV---VKKL-GGTIDDTELIEGLVFTQKASKsAGGPTRIEKAKIGLIQFQISPPKtdmenqiIVNDYA 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    568 TIETVLLQEKEYLRNVCARIMSFKPNVVLVHKN-----VAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIES 642
Cdd:TIGR02342  250 QMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSilrdaVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDH 329
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 20130093    643 nITMPKLGYCNDFYIRNYNGKTLMFFEKLTNPR-GYTCLLRGGSNAELTRVKR 694
Cdd:TIGR02342  330 -FTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAER 381
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
184-241 2.66e-06

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 46.47  E-value: 2.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20130093  184 MPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRcDGDLKVCNYC 241
Cdd:cd15742    4 VPVSHVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYLK-DRPAKVCDGC 60
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
522-693 1.36e-05

T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274088  Cd Length: 531  Bit Score: 49.73  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    522 KDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIE---GKFVTI----ETVLLQEKEYLRNVCARIMSFK--- 591
Cdd:TIGR02347  202 TDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEvnsGFFYSSaeqrEKLVKAERKFVDDRVKKIIELKkkv 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    592 ----PNVVLVHKNVAGIAQ---DLLRSYEVTLVLDVKLSVMERLsrTLQC--DIVSSIEsNITMPKLGYCNDFYIRNYNG 662
Cdd:TIGR02347  282 cgksPDKGFVVINQKGIDPpslDLLAKEGIMALRRAKRRNMERL--TLACggEALNSVE-DLTPECLGWAGLVYETTIGE 358
                          170       180       190
                   ....*....|....*....|....*....|.
gi 20130093    663 KTLMFFEKLTNPRGYTCLLRGGSNAELTRVK 693
Cdd:TIGR02347  359 EKYTFIEECKNPKSCTILIKGPNDHTIAQIK 389
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
192-241 3.57e-05

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 43.08  E-value: 3.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20130093  192 CYDCSQKF-----------STFRRKHHCRLCGQIFCSKCCNQ--VVPGMiircdG---DLKVCNYC 241
Cdd:cd15718    9 CQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNrsTIPVM-----GfefPVRVCNEC 69
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
508-694 5.24e-05

TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239455  Cd Length: 526  Bit Score: 47.68  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  508 RNYVNFK--KV---PGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCP-----------IVYERIEgKFVTIET 571
Cdd:cd03339  192 RKDVNFEliKVegkVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPfeppkpktkhkLDITSVE-DYKKLQE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  572 vllQEKEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGY 651
Cdd:cd03339  271 ---YEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFE-DLSPEKLGK 346
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 20130093  652 CNdfYIRNYNGKT----LMFFEKLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:cd03339  347 AG--LVREISFGTtkdkMLVIEGCPNSKAVTIFIRGGNKMIIEEAKR 391
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
192-219 9.23e-05

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289  Cd Length: 47  Bit Score: 41.19  E-value: 9.23e-05
                         10        20
                 ....*....|....*....|....*...
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKC 219
Cdd:cd15750    3 CESCGAKFSVFKRKRTCADCKRYFCSNC 30
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
186-219 1.00e-04

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 41.52  E-value: 1.00e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 20130093  186 DSKAKECYDCSQKF-STFRRKHHCRLCGQIFCSKC 219
Cdd:cd15740    2 EKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKC 36
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
449-684 1.19e-04

TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239456  Cd Length: 522  Bit Score: 46.51  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  449 TTATSKLLAsyceHEEQLLAQMLRahnldqewDKVLQMlcstaanhfkpehcsNDLMDIrNYVNFKKVPGGRRKDSKIVH 528
Cdd:cd03340  157 TALNSKLIA----SEKEFFAKMVV--------DAVLSL---------------DDDLDL-DMIGIKKVPGGSLEDSQLVN 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  529 GVAFSKNVA---HKDMATHVPFPRILLLQCPIVY--ERiEGKFVTIETVllqeKEYLRNVCA----------RIMSFKPN 593
Cdd:cd03340  209 GVAFKKTFSyagFEQQPKKFKNPKILLLNVELELkaEK-DNAEVRVEDP----EEYQAIVDAewkiiydkleKIVKSGAN 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  594 VVLVHKNVAGIA------QDLLRSYEVTlvldvklsvMERLSRTLQC--DIVSSIESNITMPKLGYCNDFYIRNYNGKTL 665
Cdd:cd03340  284 VVLSKLPIGDLAtqyfadRDIFCAGRVP---------EEDLKRVAQAtgGSIQTTVSNITDDVLGTCGLFEERQVGGERY 354
                        250
                 ....*....|....*....
gi 20130093  666 MFFEKLTNPRGYTCLLRGG 684
Cdd:cd03340  355 NIFTGCPKAKTCTIILRGG 373
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
523-693 1.19e-04

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458  Cd Length: 484  Bit Score: 46.48  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  523 DSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCPIVYERIEgkfvtietvllqekeylrnVCArimSFKPNVVLVHKNVA 602
Cdd:cd03342  199 DTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTE-------------------VNS---GFFYSVVINQKGID 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093  603 GIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYCNDFYIRNYNGKTLMFFEKLTNPRGYTCLLR 682
Cdd:cd03342  257 PPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVD-DLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIK 335
                        170
                 ....*....|.
gi 20130093  683 GGSNAELTRVK 693
Cdd:cd03342  336 GPNDHTITQIK 346
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
508-703 1.46e-04

T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274084  Cd Length: 532  Bit Score: 46.33  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    508 RNYVNFK------KVpGGRRKDSKIVHGVAFSKNVAHKDMATHVPFPRILLLQCP-----------IVYERIEgKFVTIE 570
Cdd:TIGR02343  196 RRDVDFDlikvegKV-GGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPfeppkpktkhkLDISSVE-EYKKLQ 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    571 TvllQEKEYLRNVCARIMSFKPNVVLVHKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLG 650
Cdd:TIGR02343  274 K---YEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQ-ELSKDKLG 349
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 20130093    651 YCNDFYIRNYnGKT---LMFFEKLTNPRGYTCLLRGGSNAELTRVKR-VASALLFAR 703
Cdd:TIGR02343  350 KAGLVREISF-GTTkdrMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRsIHDALCVVR 405
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
483-694 2.44e-04

T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274087  Cd Length: 531  Bit Score: 45.48  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    483 VLQMLCSTAANHFKPEHCSN-DLMDIRnyvnFKKVPGGRRKDSKIVHGVAFSKNVahKDMATHVPFPRILLLQCPIVYER 561
Cdd:TIGR02346  169 FLAQLVAQACSTVLPKNPQNfNVDNIR----VCKILGGSLSNSEVLKGMVFNREA--EGSVKSVKNAKVAVFSCPLDTAT 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093    562 IEGKfvtiETVLLQEKEYLRN--------VCARIMSFKP---NVVLVHKNVAGIAQDLLRSYEVtLVLDVkLSVME--RL 628
Cdd:TIGR02346  243 TETK----GTVLIHNAEELLNyskgeenqIEAMIKAIADsgvNVIVTGGSVGDMALHYLNKYNI-MVLKI-PSKFElrRL 316
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20130093    629 SRTlqCDIVSSIESNITMPK-LGYCNDFYIRNYNGKTLMFFE-KLTNPRGYTCLLRGGSNAELTRVKR 694
Cdd:TIGR02346  317 CKT--VGATPLPRLGAPTPEeIGYVDSVYVSEIGGDKVTVFKqENGDSKISTIILRGSTDNLLDDIER 382
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
188-241 2.71e-04

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 40.82  E-value: 2.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130093  188 KAKECYDCSQKF-----------STFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYC 241
Cdd:cd15756    5 ESDSCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRSSYPIMGFEFQVRVCDSC 69
FYVE_SPIR cd15748
FYVE-related domain found in Spir proteins, Spire1 and Spire2; Spir proteins were originally ...
188-223 4.11e-04

FYVE-related domain found in Spir proteins, Spire1 and Spire2; Spir proteins were originally discovered as the protein products of the Drosophila spire gene. They are Jun N-terminal kinase (JNK)-interacting proteins that have exclusively been identified in metazoans. They may play roles in membrane trafficking and cortical filament crosslinking. This family includes Spire1 and Spire2, which function as new essential factors in asymmetric division of oocytes. They mediate asymmetric spindle positioning by assembling a cytoplasmic actin network. They are also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, they cooperate synergistically with Fmn2 to assemble F-actin in oocytes. Both Spire1 and Spire2 contain an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. Their FYVE domains resemble FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically bind the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277287  Cd Length: 42  Bit Score: 39.24  E-value: 4.11e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 20130093  188 KAKECYDC-SQKFSTFRRKHHCRLCGQIFCSKCCNQV 223
Cdd:cd15748    1 KGKVCFCCkKKKFSFFTWPNTCKLCKRVVCSKCCRDV 37
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
343-388 4.24e-04

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) PIKfyve-like proteins. PIKfyve contains N-terminal Fyve finger and DEP domains, a central chaperonin-like domain and a C-terminal PIPK (phosphatidylinositol phosphate kinase) domain. PIKfyve-like proteins are important phosphatidylinositol (3)-monophosphate (PtdIns(3)P)-5-kinases, producing PtdIns(3,5)P2, which plays a major role in multivesicular body (MVB) sorting and control of retrograde traffic from the vacuole back to the endosome and/or Golgi. PIKfyve itself has been shown to be play a role in regulating early-endosome-to-trans-Golgi network (TGN) retrograde trafficking.


Pssm-ID: 239895  Cd Length: 81  Bit Score: 40.50  E-value: 4.24e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 20130093  343 NC--GQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMD 388
Cdd:cd04448   27 NCilGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDDLFRD 74
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
181-223 1.60e-03

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 38.79  E-value: 1.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 20130093  181 RFWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFC-SKCCNQV 223
Cdd:cd15761    2 SHWKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCnEHCRNRI 45
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
449-652 1.80e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 42.71  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   449 TTATSKLLAsyceHEEQLLAQMLRahnldqewDKVLQMlcstaanhfkpeHCSNDLmdirNYVNFKKVPGGRRKDSKIVH 528
Cdd:PTZ00212  167 TTLSSKLLT----VEKDHFAKLAV--------DAVLRL------------KGSGNL----DYIQIIKKPGGTLRDSYLED 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130093   529 GVAFSKNVA---HKDMAThvpfPRILLLQCPIVYERIE--GKFVTIETVL------LQEKEYLRNVCARIMSFKPNVVLV 597
Cdd:PTZ00212  219 GFILEKKIGvgqPKRLEN----CKILVANTPMDTDKIKiyGAKVKVDSMEkvaeieAAEKEKMKNKVDKILAHGCNVFIN 294
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 20130093   598 HKNVAGIAQDLLRSYEVTLVLDVKLSVMERLSRTLQCDIVSSIEsNITMPKLGYC 652
Cdd:PTZ00212  295 RQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFD-TPEKVKLGHC 348
FYVE_CARP1 cd15769
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ...
192-219 3.43e-03

FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ubiquitin-protein ligase RNF34, or caspases-8 and -10-associated RING finger protein 1, or FYVE-RING finger protein Momo, or RING finger homologous to inhibitor of apoptosis protein (RFI), or RING finger protein 34, or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell, and negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric and colorectal cancers, suggesting a possible association with the development of the digestive tract cancers. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP1 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP1 harbors a C-terminal RING domain.


Pssm-ID: 277308  Cd Length: 47  Bit Score: 36.89  E-value: 3.43e-03
                         10        20
                 ....*....|....*....|....*...
gi 20130093  192 CYDCSQKFSTFRRKHHCRLCGQIFCSKC 219
Cdd:cd15769    4 CKACGLAFSVFRKKHVCCDCKKDFCSVC 31
FYVE_SPIR1 cd15767
FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is ...
188-223 8.68e-03

FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277306  Cd Length: 79  Bit Score: 36.81  E-value: 8.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 20130093  188 KAKECYDC-SQKFSTFRRKHHCRLCGQIFCSKCCNQV 223
Cdd:cd15767    3 KGKLCFSCrSKRFSLFTWSYTCQFCKRPVCSQCCKKM 39
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
329-397 9.44e-03

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 334170  Cd Length: 72  Bit Score: 36.41  E-value: 9.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20130093    329 ITLHEEMQRDLPAQNC--GQRLIEFLNSNNKSANEVQAVAILNAMLAAGFLEPIVPDPEQMDFDSSLHYKF 397
Cdd:pfam00610    2 VKLKDRRKHLKTYPNCftGSEAVDWLMDNLSIIDREEAVELGQLLLDQGLIHHVGDKHGTFKDSSYAFYRF 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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