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Conserved domains on  [gi|767917152|ref|XP_011509082|]
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1-phosphatidylinositol 3-phosphate 5-kinase isoform X2 [Homo sapiens]

Protein Classification

1-phosphatidylinositol 3-phosphate 5-kinase( domain architecture ID 13004803)

1-phosphatidylinositol 3-phosphate 5-kinase is part of a complex that 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

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 ...
1829-2095 1.24e-152

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: 471.61  E-value: 1.24e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1829 AKFYCRLYYAGEFHKMREVILDSsEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1908
Cdd:cd17300     1 TKFTCTIYFAEQFHALRSLYCGG-EDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1909 ITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTdtgKESCDVVLLDE 1988
Cdd:cd17300    80 MAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRNRYVNV---AEDEDSVLLDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1989 NLLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGIL 2068
Cdd:cd17300   157 NFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGIL 236
                         250       260
                  ....*....|....*....|....*..
gi 767917152 2069 GGQGkMPTVVSPELYRTRFCEAMDKYF 2095
Cdd:cd17300   237 GGGG-EPTVISPELYKKRFREAMDKYF 262
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
628-888 2.17e-134

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: 420.47  E-value: 2.17e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  628 MALLQQ--LLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNqDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKK 705
Cdd:cd03334     1 RALLAQllKDEGISNDESWLDILLPLVWKAASNVKPDVRA-GDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  706 MSSCIKNPKILLLKCSIEYLyREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVIN 785
Cdd:cd03334    80 MPSKIKNPRILLLQGPLEYQ-RVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  786 VKSQVLERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKE 865
Cdd:cd03334   159 VKPSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKR 238
                         250       260
                  ....*....|....*....|...
gi 767917152  866 ILIFMICVAYHSQLEISFLMDEF 888
Cdd:cd03334   239 VVEFMVFAAYHLKLETSFLADEF 261
MSS4 super family cl28924
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1519-2106 5.35e-64

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


The actual alignment was detected with superfamily member COG5253:

Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 230.60  E-value: 5.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1519 LQDLFQQEKGRKRPSVP--PSPGRLRQGEESKISAMDA--SPRNISPGLQNGEKEDrflttlSSQSSTSSTHLQLPTPPE 1594
Cdd:COG5253   100 IVEIFKNNKDAVDPPNHtrSSGNNLSNANVKTLSAPVGehSRSNNPPNLDQNLDTE------PESSISQWGELQLNPSGK 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1595 VMSEQSVGGPpeLDTASSSEdVFDGHLLGSTDSQVKEKSTMKAIFANL-LPGNSYNPIP--FPFDPDKHylMYEHERVPI 1671
Cdd:COG5253   174 TLSSQPSRKP--TSENPKSE-SDNSKLPTSVNSPLPDKSLLKRTLSNFwAERNSYNWKPlvYPSCPSEH--IFSDSDVII 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1672 AvcEKEPSSIIAFALSCKEYRNALEELSKAtqwnsaeeglptnSTSDSRPkssspIRLPEMSGGQTNRTTetepqptkkA 1751
Cdd:COG5253   249 R--EDEPSSLIAFCLSTSDYRNKMMRLRDS-------------ETMDERL-----LNGMPLEGGHRNPQE---------S 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1752 SGMLSFFRGTAGKSPDLSSQKRETlrgadsayyqvgqTGKEgtenqgvepqdevdggdtqkkqlinphvelQFSDANAKF 1831
Cdd:COG5253   300 YNMLTGIRVTLSRIEEIMIKKTDT-------------HLNE------------------------------QFEEGLYEF 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1832 YCRLYYAGEFHKMREviLDSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEvqsFLDFAPHYFNYItN 1911
Cdd:COG5253   337 SCKDYFPEVFRELRA--LCGCDEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSE---HICFRPMIFEYY-V 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1912 AVQQKRPTALAKILGVYRIGYKNS-QNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKtDTGKesCDVVLLDENL 1990
Cdd:COG5253   411 HVLFNPLTLLCKIFGFYRVKSRSSiSSSKSRKIYFIVMENLFYPHGIHRIFDLKGSMRNRHVE-RTGK--SMSVLLDMND 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1991 LKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVG-IIDYIRT-FTWDKKLEMVVKSTGIL 2068
Cdd:COG5253   488 VEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGlIIDFIRTrMTGDKKLESGIKDKLTV 567
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 767917152 2069 GG--QGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLG 2106
Cdd:COG5253   568 GSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEG 607
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
368-449 4.37e-50

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: 171.86  E-value: 4.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  368 DLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDqLFRDEYALY 447
Cdd:cd04448     1 DLWEKICRSSTGIEFQDHRYRLRTYTNCILGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDD-LFRDEYALY 79

                  ..
gi 767917152  448 RP 449
Cdd:cd04448    80 KP 81
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
165-226 4.11e-44

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: 154.02  E-value: 4.11e-44
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRK 226
Cdd:cd15725     1 YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
 
Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
1829-2095 1.24e-152

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: 471.61  E-value: 1.24e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1829 AKFYCRLYYAGEFHKMREVILDSsEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1908
Cdd:cd17300     1 TKFTCTIYFAEQFHALRSLYCGG-EDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1909 ITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTdtgKESCDVVLLDE 1988
Cdd:cd17300    80 MAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRNRYVNV---AEDEDSVLLDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1989 NLLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGIL 2068
Cdd:cd17300   157 NFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGIL 236
                         250       260
                  ....*....|....*....|....*..
gi 767917152 2069 GGQGkMPTVVSPELYRTRFCEAMDKYF 2095
Cdd:cd17300   237 GGGG-EPTVISPELYKKRFREAMDKYF 262
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
628-888 2.17e-134

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: 420.47  E-value: 2.17e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  628 MALLQQ--LLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNqDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKK 705
Cdd:cd03334     1 RALLAQllKDEGISNDESWLDILLPLVWKAASNVKPDVRA-GDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  706 MSSCIKNPKILLLKCSIEYLyREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVIN 785
Cdd:cd03334    80 MPSKIKNPRILLLQGPLEYQ-RVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  786 VKSQVLERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKE 865
Cdd:cd03334   159 VKPSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKR 238
                         250       260
                  ....*....|....*....|...
gi 767917152  866 ILIFMICVAYHSQLEISFLMDEF 888
Cdd:cd03334   239 VVEFMVFAAYHLKLETSFLADEF 261
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1802-2095 9.08e-103

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 333.58  E-value: 9.08e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   1802 QDEVDGGDTQKKQLINPHVELQFSDANAKFYCRLYYAGEFHKMREvILDSSEEDFIRSLSHSSP-WQARGGKSGAAFYAT 1880
Cdd:smart00330    1 LPSDFKATEKIKFPTPGHLELTPSHGSADFKFKDYCPEVFRNLRE-LFGIDPADYLRSLCRSPPlELSSGGKSGSFFYLS 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   1881 EDDRFILKQMPRLEVQSFLdfaPHYFNYITNAVQQKrPTALAKILGVYRIGYKNSqnnTEKKLDLLVMENLFY-GRKMAQ 1959
Cdd:smart00330   80 LDDRFIIKTVSKSEIKSLL---PMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGG---TEKKIYFLVMENLFYsDLKVHR 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   1960 VFDLKGSLRNRNVktDTGKESCDVVLLDENLLKMvRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSN 2039
Cdd:smart00330  153 KYDLKGSTRGREA--DKKKVKELPVLKDLDLVEM-WNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIER 229
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   2040 ------------------------------------------------------------ELVVGIIDYIRTFTWDKKLE 2059
Cdd:smart00330  230 gqreeielppvygsdespssessnggkapditgnllvsnspdgdgpfggiparairarrvVLYLGIIDILQTYTWDKKLE 309
                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 767917152   2060 MVVKSTGILggqGKMPTVVSPELYRTRFCEAMDKYF 2095
Cdd:smart00330  310 HWVKSIGHD---GKTISVVHPEQYAKRFRDFMDKYF 342
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1519-2106 5.35e-64

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 230.60  E-value: 5.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1519 LQDLFQQEKGRKRPSVP--PSPGRLRQGEESKISAMDA--SPRNISPGLQNGEKEDrflttlSSQSSTSSTHLQLPTPPE 1594
Cdd:COG5253   100 IVEIFKNNKDAVDPPNHtrSSGNNLSNANVKTLSAPVGehSRSNNPPNLDQNLDTE------PESSISQWGELQLNPSGK 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1595 VMSEQSVGGPpeLDTASSSEdVFDGHLLGSTDSQVKEKSTMKAIFANL-LPGNSYNPIP--FPFDPDKHylMYEHERVPI 1671
Cdd:COG5253   174 TLSSQPSRKP--TSENPKSE-SDNSKLPTSVNSPLPDKSLLKRTLSNFwAERNSYNWKPlvYPSCPSEH--IFSDSDVII 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1672 AvcEKEPSSIIAFALSCKEYRNALEELSKAtqwnsaeeglptnSTSDSRPkssspIRLPEMSGGQTNRTTetepqptkkA 1751
Cdd:COG5253   249 R--EDEPSSLIAFCLSTSDYRNKMMRLRDS-------------ETMDERL-----LNGMPLEGGHRNPQE---------S 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1752 SGMLSFFRGTAGKSPDLSSQKRETlrgadsayyqvgqTGKEgtenqgvepqdevdggdtqkkqlinphvelQFSDANAKF 1831
Cdd:COG5253   300 YNMLTGIRVTLSRIEEIMIKKTDT-------------HLNE------------------------------QFEEGLYEF 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1832 YCRLYYAGEFHKMREviLDSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEvqsFLDFAPHYFNYItN 1911
Cdd:COG5253   337 SCKDYFPEVFRELRA--LCGCDEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSE---HICFRPMIFEYY-V 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1912 AVQQKRPTALAKILGVYRIGYKNS-QNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKtDTGKesCDVVLLDENL 1990
Cdd:COG5253   411 HVLFNPLTLLCKIFGFYRVKSRSSiSSSKSRKIYFIVMENLFYPHGIHRIFDLKGSMRNRHVE-RTGK--SMSVLLDMND 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1991 LKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVG-IIDYIRT-FTWDKKLEMVVKSTGIL 2068
Cdd:COG5253   488 VEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGlIIDFIRTrMTGDKKLESGIKDKLTV 567
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 767917152 2069 GG--QGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLG 2106
Cdd:COG5253   568 GSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEG 607
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
368-449 4.37e-50

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: 171.86  E-value: 4.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  368 DLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDqLFRDEYALY 447
Cdd:cd04448     1 DLWEKICRSSTGIEFQDHRYRLRTYTNCILGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDD-LFRDEYALY 79

                  ..
gi 767917152  448 RP 449
Cdd:cd04448    80 KP 81
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
165-226 4.11e-44

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: 154.02  E-value: 4.11e-44
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRK 226
Cdd:cd15725     1 YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
644-867 3.92e-38

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


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 150.82  E-value: 3.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   644 WRDIIVSLVCQVVQTVRPDVKNQDDDMdirqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:pfam00118  137 ESDFLAKLVVDAVLAIPKNDGSFDLGN-----IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   724 YlYREETK--FTCIDP-----IVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISR 796
Cdd:pfam00118  212 Y-EKTETKatVVLSDAeqlerFLKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAK 290
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152   797 MTQGDLVMSMDQlLTKPHLGTCHKFYMQIFqlpneQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEIL 867
Cdd:pfam00118  291 ATGARAVSSLDD-LTPDDLGTAGKVEEEKI-----GDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSI 355
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
1863-2094 1.02e-37

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: 426295  Cd Length: 283  Bit Score: 143.89  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  1863 SSPwqargGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIgyKNSQnnteKK 1942
Cdd:pfam01504   10 SSP-----GKSGSFFYLSSDDRFIIKTITKSEHKFLRKILPDYYEH----VKQNPNTLLPRFYGLHRV--KPGG----KK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  1943 LDLLVMENLFY-GRKMAQVFDLKGSLRNRNVKtDTGKESCDVVLLDENLLKmvRDNPLYIRSHSKAVLRTSIHSDSHFLS 2021
Cdd:pfam01504   75 IYFVVMNNLFPtDLKIHERYDLKGSTVGRKAS-KKEREKDEPTLKDLDFLE--RKLKLRLGPEKREALLKQLERDCEFLE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  2022 SHLIIDYSLLVG------------------------------------------------------------RDDTSNEL 2041
Cdd:pfam01504  152 SLNIMDYSLLLGihdldrgeqeslrsstlsssspssssskssssssslsliqsaersggafylddgggraggENSEDGKE 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  2042 V--VGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMDKY 2094
Cdd:pfam01504  232 IyyLGIIDILQEYNLKKKLEHAWKS---LVHDGDSISAVPPKEYAERFLKFIEKI 283
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
644-867 3.88e-32

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 [Multi-domain]  Cd Length: 524  Bit Score: 133.71  E-value: 3.88e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   644 WRDIIVSLVCQVVQTVRPDvKNQDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:TIGR02344  163 WSDLMCDLALDAVRTVQRD-ENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLE 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   724 YLYRE---------ETKFTcidPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERI 794
Cdd:TIGR02344  242 YKKGEsqtnieitkEEDWN---RILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRI 318
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917152   795 SRMTQGDLVMSMDQlLTKPHLGT-CHKFYMQIFqlpneQTKTLMFFEGCPQHLGCTIKLRGGSdyelarvKEIL 867
Cdd:TIGR02344  319 ARACGATIVNRPEE-LRESDVGTgCGLFEVKKI-----GDEYFTFITECKDPKACTILLRGAS-------KDIL 379
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
165-224 1.18e-22

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: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 93.21  E-value: 1.18e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152   165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPG-KFMGYTGDLRACTYC 224
Cdd:pfam01363    2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLlPELGSNKPVRVCDAC 62
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
165-224 2.17e-21

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: 89.41  E-value: 2.17e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152    165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:smart00064    3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDC 62
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
377-449 6.53e-21

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: 88.49  E-value: 6.53e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917152    377 SSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSH-HDQLFRDEYALYRP 449
Cdd:smart00049    2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGpNKHTFKDSKALYRF 75
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
646-864 4.77e-19

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


Pssm-ID: 223535 [Multi-domain]  Cd Length: 524  Bit Score: 93.05  E-value: 4.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  646 DIIVSLVCQVVQTVRPDVKNQDDdmdirqfVHIKKIPGGKKFDSVVVNGFVCTK-NIAHKKMSSC-IKNPKILLLKCSIE 723
Cdd:COG0459   157 EEIGELVVEAVEKVGKEQSDLDG-------IIIVKESGGSETELEVVEGMVFDKgYLSPYFMPDKrLENPKILLLDKKLE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  724 YLyREE--TKFTCIDPIVLQ------EREFLKNYVQRIVDVRPTLVLV-EKTVSRIAQDMLLEHGITLVINVKSQ-VLER 793
Cdd:COG0459   230 IK-KPElpLEIVISSGKPLLiiaedeEGEALATLVVNILRGGANVVVVkAPGIDDLAKAYLEDIAILTGRRVKKEdLGER 308
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  794 ISRMTQGDLVMSMDQlLTKPHLGT--CHKFYMQIFqlpNEQTKTlmFFEGCPQHLG--CTIKLRGGSDYELARVK 864
Cdd:COG0459   309 LAKLGGAKIVSVLKD-LTTIVLGEgaAGLVEETKT---GDYDME--KLQERKAKAGgvATILVRGATEVELDEKE 377
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1814-2033 1.04e-18

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 92.97  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1814 QLINPHvelQFSDANAKFYCRLYyageFHKMREVI-LDSSE-------EDFIRSLShsSPwqargGKSGAAFYATEDDRF 1885
Cdd:PLN03185  394 QLTPSH---QSEDFKWKDYCPMV----FRNLREMFkIDAADymmsicgNDALRELS--SP-----GKSGSVFFLSQDDRF 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1886 ILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIGYKNSQnntekKLDLLVMENLFYGR-KMAQVFDLK 1964
Cdd:PLN03185  460 MIKTLRKSEVKVLLRMLPDYHHH----VKTYENTLITKFFGLHRIKPSSGQ-----KFRFVVMGNMFCTElRIHRRFDLK 530
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152 1965 GSLRNRnvktdtgkeSCDVVLLDEN--LLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVG 2033
Cdd:PLN03185  531 GSSLGR---------SADKVEIDENttLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLG 592
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
379-448 5.55e-18

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: 425776 [Multi-domain]  Cd Length: 70  Bit Score: 79.92  E-value: 5.55e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152   379 GMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVS-HHDqlFRDEYALYR 448
Cdd:pfam00610    1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDNLSIITREEAVELGQLLLDQGLIHHVGdKHG--FKDSYYFYR 69
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
676-856 7.41e-08

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 57.35  E-value: 7.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  676 VHIKKIPGGKKFDSVVVNGFVCTKNIA---HKKMSscikNPKILLLKCSIEY----LYREETK---FTCIDPIVLQEREF 745
Cdd:PTZ00212  201 IQIIKKPGGTLRDSYLEDGFILEKKIGvgqPKRLE----NCKILVANTPMDTdkikIYGAKVKvdsMEKVAEIEAAEKEK 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  746 LKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMDQLLtKPHLGTCHKfyMQI 825
Cdd:PTZ00212  277 MKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPE-KVKLGHCDL--IEE 353
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767917152  826 FQLPNEqtkTLMFFEGCPQHLGCTIKLRGGS 856
Cdd:PTZ00212  354 IMIGED---KLIRFSGCAKGEACTIVLRGAS 381
 
Name Accession Description Interval E-value
PIPKc_PIKfyve cd17300
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in ...
1829-2095 1.24e-152

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: 471.61  E-value: 1.24e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1829 AKFYCRLYYAGEFHKMREVILDSsEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1908
Cdd:cd17300     1 TKFTCTIYFAEQFHALRSLYCGG-EDDFIRSLSRCVKWDASGGKSGASFFKTLDDRFILKQISKAELQSFLDFAPAYFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1909 ITNAVQQKRPTALAKILGVYRIGYKNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTdtgKESCDVVLLDE 1988
Cdd:cd17300    80 MAKALFHKRPSLLAKILGVYRISVKNSTTNKTSKQDLLVMENLFYGRNISQVYDLKGSLRNRYVNV---AEDEDSVLLDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1989 NLLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTFTWDKKLEMVVKSTGIL 2068
Cdd:cd17300   157 NFLEYTKGSPLYLREHSKAVLMAAIWNDTLFLSSQNVMDYSLLVGIDEEKKELVVGIIDYIRTYTWDKKLESWVKSLGIL 236
                         250       260
                  ....*....|....*....|....*..
gi 767917152 2069 GGQGkMPTVVSPELYRTRFCEAMDKYF 2095
Cdd:cd17300   237 GGGG-EPTVISPELYKKRFREAMDKYF 262
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
628-888 2.17e-134

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: 420.47  E-value: 2.17e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  628 MALLQQ--LLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNqDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKK 705
Cdd:cd03334     1 RALLAQllKDEGISNDESWLDILLPLVWKAASNVKPDVRA-GDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  706 MSSCIKNPKILLLKCSIEYLyREETKFTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVIN 785
Cdd:cd03334    80 MPSKIKNPRILLLQGPLEYQ-RVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  786 VKSQVLERISRMTQGDLVMSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKE 865
Cdd:cd03334   159 VKPSVLERISRCTGADIISSMDDLLTSPKLGTCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKR 238
                         250       260
                  ....*....|....*....|...
gi 767917152  866 ILIFMICVAYHSQLEISFLMDEF 888
Cdd:cd03334   239 VVEFMVFAAYHLKLETSFLADEF 261
PIPKc smart00330
Phosphatidylinositol phosphate kinases;
1802-2095 9.08e-103

Phosphatidylinositol phosphate kinases;


Pssm-ID: 214623 [Multi-domain]  Cd Length: 342  Bit Score: 333.58  E-value: 9.08e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   1802 QDEVDGGDTQKKQLINPHVELQFSDANAKFYCRLYYAGEFHKMREvILDSSEEDFIRSLSHSSP-WQARGGKSGAAFYAT 1880
Cdd:smart00330    1 LPSDFKATEKIKFPTPGHLELTPSHGSADFKFKDYCPEVFRNLRE-LFGIDPADYLRSLCRSPPlELSSGGKSGSFFYLS 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   1881 EDDRFILKQMPRLEVQSFLdfaPHYFNYITNAVQQKrPTALAKILGVYRIGYKNSqnnTEKKLDLLVMENLFY-GRKMAQ 1959
Cdd:smart00330   80 LDDRFIIKTVSKSEIKSLL---PMLPNYYEHIVQNP-NTLLPKFFGLYRVKVKGG---TEKKIYFLVMENLFYsDLKVHR 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   1960 VFDLKGSLRNRNVktDTGKESCDVVLLDENLLKMvRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSN 2039
Cdd:smart00330  153 KYDLKGSTRGREA--DKKKVKELPVLKDLDLVEM-WNQPIYVDPLAKKALLKQIKRDCEFLESLKIMDYSLLVGIHDIER 229
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   2040 ------------------------------------------------------------ELVVGIIDYIRTFTWDKKLE 2059
Cdd:smart00330  230 gqreeielppvygsdespssessnggkapditgnllvsnspdgdgpfggiparairarrvVLYLGIIDILQTYTWDKKLE 309
                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 767917152   2060 MVVKSTGILggqGKMPTVVSPELYRTRFCEAMDKYF 2095
Cdd:smart00330  310 HWVKSIGHD---GKTISVVHPEQYAKRFRDFMDKYF 342
PIPKc cd00139
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain family; The Phosphatidylinositol ...
1830-2093 1.27e-68

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: 232.08  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1830 KFYCRLYYAGEFHKMREvILDSSEEDFIRSLSHSSPW---QARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYF 1906
Cdd:cd00139     2 KFKFKDYAPEVFRKLRE-LFGISEEDYLESLSPEENLrelKESEGKSGSFFFFTSDGKFIIKTITKSELKFLLKILPDYY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1907 NYItnavQQKRPTALAKILGVYRIGYKNSqnnteKKLDLLVMENLFY-GRKMAQVFDLKGSLRNRNVKTDTGKESCDVVL 1985
Cdd:cd00139    81 EHI----KKNPNSLLTRFYGLYSIKLQKG-----KKVYFVVMENVFPtDLKIHERYDLKGSTVGRRVSKEKEKKKGLKVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1986 LDENLLKMVRDnpLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDtsNELVVGIIDYIRTFTWDKKLEMVVKSt 2065
Cdd:cd00139   152 KDLDFLEKGEK--IILGPEDRAELLEQLEKDVEFLRSLNIMDYSLLVGIHR--LVYYLGIIDILQEYNLRKKLERFLKS- 226
                         250       260
                  ....*....|....*....|....*...
gi 767917152 2066 gILGGQGKMPTVVSPELYRTRFCEAMDK 2093
Cdd:cd00139   227 -LLYGKDSGISCVPPDEYAERFLKFMES 253
MSS4 COG5253
Phosphatidylinositol-4-phosphate 5-kinase [Signal transduction mechanisms];
1519-2106 5.35e-64

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


Pssm-ID: 227578 [Multi-domain]  Cd Length: 612  Bit Score: 230.60  E-value: 5.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1519 LQDLFQQEKGRKRPSVP--PSPGRLRQGEESKISAMDA--SPRNISPGLQNGEKEDrflttlSSQSSTSSTHLQLPTPPE 1594
Cdd:COG5253   100 IVEIFKNNKDAVDPPNHtrSSGNNLSNANVKTLSAPVGehSRSNNPPNLDQNLDTE------PESSISQWGELQLNPSGK 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1595 VMSEQSVGGPpeLDTASSSEdVFDGHLLGSTDSQVKEKSTMKAIFANL-LPGNSYNPIP--FPFDPDKHylMYEHERVPI 1671
Cdd:COG5253   174 TLSSQPSRKP--TSENPKSE-SDNSKLPTSVNSPLPDKSLLKRTLSNFwAERNSYNWKPlvYPSCPSEH--IFSDSDVII 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1672 AvcEKEPSSIIAFALSCKEYRNALEELSKAtqwnsaeeglptnSTSDSRPkssspIRLPEMSGGQTNRTTetepqptkkA 1751
Cdd:COG5253   249 R--EDEPSSLIAFCLSTSDYRNKMMRLRDS-------------ETMDERL-----LNGMPLEGGHRNPQE---------S 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1752 SGMLSFFRGTAGKSPDLSSQKRETlrgadsayyqvgqTGKEgtenqgvepqdevdggdtqkkqlinphvelQFSDANAKF 1831
Cdd:COG5253   300 YNMLTGIRVTLSRIEEIMIKKTDT-------------HLNE------------------------------QFEEGLYEF 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1832 YCRLYYAGEFHKMREviLDSSEEDFIRSLSHSSPWQARGGKSGAAFYATEDDRFILKQMPRLEvqsFLDFAPHYFNYItN 1911
Cdd:COG5253   337 SCKDYFPEVFRELRA--LCGCDEALVSLLSRYILWESNGGKSGSFFLFTRDYKFIIKTISHSE---HICFRPMIFEYY-V 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1912 AVQQKRPTALAKILGVYRIGYKNS-QNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKtDTGKesCDVVLLDENL 1990
Cdd:COG5253   411 HVLFNPLTLLCKIFGFYRVKSRSSiSSSKSRKIYFIVMENLFYPHGIHRIFDLKGSMRNRHVE-RTGK--SMSVLLDMND 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1991 LKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSNELVVG-IIDYIRT-FTWDKKLEMVVKSTGIL 2068
Cdd:COG5253   488 VEWIRESPKIVFGLKKKLLLSQVWNDVLFLSKLNIMDYSLLVGIDDEREEASVGlIIDFIRTrMTGDKKLESGIKDKLTV 567
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 767917152 2069 GG--QGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLG 2106
Cdd:COG5253   568 GSftKRKEPTAVTPRQYKNRFRKAMEAYIDPFPDKKTQEG 607
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
644-880 6.43e-58

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: 199.23  E-value: 6.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  644 WRDIIVSLVCQVVQTVRPDVKNQDDDMdirqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:cd03333    19 WDDFLGKLVVDAVLKVGPDNRMDDLGV-----IKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKRLENAKILLLDCPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  724 YLyreetkftcidpivlqereflknyvqrivdvrptlVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLV 803
Cdd:cd03333    94 YV-----------------------------------VIAEKGIDDLALHYLAKAGIMAVRRVKKEDLERIARATGATIV 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917152  804 MSMDQLlTKPHLGTCHKFYMQIFQlpneqTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICVAYHSQLE 880
Cdd:cd03333   139 SSLEDL-TPEDLGTAELVEETKIG-----EEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
368-449 4.37e-50

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: 171.86  E-value: 4.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  368 DLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDqLFRDEYALY 447
Cdd:cd04448     1 DLWEKICRSSTGIEFQDHRYRLRTYTNCILGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDD-LFRDEYALY 79

                  ..
gi 767917152  448 RP 449
Cdd:cd04448    80 KP 81
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
165-226 4.11e-44

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: 154.02  E-value: 4.11e-44
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRK 226
Cdd:cd15725     1 YWMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
644-867 3.92e-38

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


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 150.82  E-value: 3.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   644 WRDIIVSLVCQVVQTVRPDVKNQDDDMdirqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:pfam00118  137 ESDFLAKLVVDAVLAIPKNDGSFDLGN-----IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   724 YlYREETK--FTCIDP-----IVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISR 796
Cdd:pfam00118  212 Y-EKTETKatVVLSDAeqlerFLKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAK 290
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152   797 MTQGDLVMSMDQlLTKPHLGTCHKFYMQIFqlpneQTKTLMFFEGCPQHLGCTIKLRGGSDYELARVKEIL 867
Cdd:pfam00118  291 ATGARAVSSLDD-LTPDDLGTAGKVEEEKI-----GDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSI 355
PIP5K pfam01504
Phosphatidylinositol-4-phosphate 5-Kinase; This family contains a region from the common ...
1863-2094 1.02e-37

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: 426295  Cd Length: 283  Bit Score: 143.89  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  1863 SSPwqargGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIgyKNSQnnteKK 1942
Cdd:pfam01504   10 SSP-----GKSGSFFYLSSDDRFIIKTITKSEHKFLRKILPDYYEH----VKQNPNTLLPRFYGLHRV--KPGG----KK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  1943 LDLLVMENLFY-GRKMAQVFDLKGSLRNRNVKtDTGKESCDVVLLDENLLKmvRDNPLYIRSHSKAVLRTSIHSDSHFLS 2021
Cdd:pfam01504   75 IYFVVMNNLFPtDLKIHERYDLKGSTVGRKAS-KKEREKDEPTLKDLDFLE--RKLKLRLGPEKREALLKQLERDCEFLE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  2022 SHLIIDYSLLVG------------------------------------------------------------RDDTSNEL 2041
Cdd:pfam01504  152 SLNIMDYSLLLGihdldrgeqeslrsstlsssspssssskssssssslsliqsaersggafylddgggraggENSEDGKE 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  2042 V--VGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMDKY 2094
Cdd:pfam01504  232 IyyLGIIDILQEYNLKKKLEHAWKS---LVHDGDSISAVPPKEYAERFLKFIEKI 283
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
644-867 3.88e-32

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 [Multi-domain]  Cd Length: 524  Bit Score: 133.71  E-value: 3.88e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   644 WRDIIVSLVCQVVQTVRPDvKNQDDDMDIRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:TIGR02344  163 WSDLMCDLALDAVRTVQRD-ENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLE 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   724 YLYRE---------ETKFTcidPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERI 794
Cdd:TIGR02344  242 YKKGEsqtnieitkEEDWN---RILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRI 318
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917152   795 SRMTQGDLVMSMDQlLTKPHLGT-CHKFYMQIFqlpneQTKTLMFFEGCPQHLGCTIKLRGGSdyelarvKEIL 867
Cdd:TIGR02344  319 ARACGATIVNRPEE-LRESDVGTgCGLFEVKKI-----GDEYFTFITECKDPKACTILLRGAS-------KDIL 379
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
610-867 8.76e-29

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 [Multi-domain]  Cd Length: 480  Bit Score: 122.79  E-value: 8.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  610 NGEKQAMERLLSA-----------NHNHMMALLQqLLHSDSLSSSWRDIIVSLVCQVVQTVRPDVKNQDDDMDIRQFVHI 678
Cdd:cd03337   119 KAYRKALEDALKIleeisipvdvnDRAQMLKIIK-SCIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIDIKRYAKV 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  679 KKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYlyreetkftcidpivlqereflknyvqrivdvrp 758
Cdd:cd03337   198 EKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY---------------------------------- 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  759 tLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTqGDLVMSMDQLLTKPHLGTCHKFYmqIFQLPNEQTKTlmF 838
Cdd:cd03337   244 -LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARAC-GATIVNRPEELTESDVGTGAGLF--EVKKIGDEYFT--F 317
                         250       260
                  ....*....|....*....|....*....
gi 767917152  839 FEGCPQHLGCTIKLRGGSdyelarvKEIL 867
Cdd:cd03337   318 ITECKDPKACTILLRGAS-------KDVL 339
PIPKc_PIP5KL1 cd17304
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1813-2092 3.92e-28

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: 117.07  E-value: 3.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1813 KQLINPHVELQFSdanakfycrlYYAGE-FHKMREvILDSSEEDFIRSLSHSSPWQA--RGGKSGAAFYATEDDRFILKQ 1889
Cdd:cd17304    40 TQVIPKHKGFEFR----------TYAGPvFATLRQ-SLGISEKEYQNSLSPDEPYLQfiSNSKSGQDFFLTNDKRFFLKT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1890 MPRLEVQSFLDFAPHYFNYItnavqQKRP-TALAKILGVYRIGYKNsqnntEKKLDLLVMENLFY-GRKMAQVFDLKGSL 1967
Cdd:cd17304   109 QTKREAKFLLSILRKYVQHL-----ENYPhSLLVKFLGVHSIKLPG-----KKKKYFIVMQSVFYpDERINERYDIKGCQ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1968 RNRNVKTDTGKESCDVVLLDENLLkmvrDNPLYIRSHSKAVLRtSIHSDSHFLSSHLIIDYSLLVGRD------------ 2035
Cdd:cd17304   179 VSRYTDPEPEGSQIIVVLKDLNFE----GNSINLGQQRSWFLR-QVEIDTEFLKGLNVLDYSLLVGFQplhsdenrrllp 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917152 2036 DTSNEL----------VVGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMD 2092
Cdd:cd17304   254 NYKNALhvvdgpeyryFVGIIDIFTVYGLRKRLEHLWKS---LRYPGQSFSTVSPEKYARRFCQWVE 317
PIPKc_AtPIP5K_like cd17302
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Arabidopsis thaliana ...
1784-2093 5.19e-28

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: 116.62  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1784 YQVGQTGKEgtenqgVEPQDEVDGGDTQKKQLIN---------PHvelQFSDANAKFYCRLYyageFHKMREVI-LDSSE 1853
Cdd:cd17302    14 YSVGKIAPV------ARRDLKPSDFDPKAKQWFPfpgsgstppPH---QSSDFKWKDYCPMV----FRNLRELFgIDAAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1854 -------EDFIRSLShsSPwqargGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILG 1926
Cdd:cd17302    81 ymlslcgDDALRELS--SP-----GKSGSVFYLSHDDRFMIKTMRKSEMKVLLRMLPAYYKH----VKAYENTLLTKFFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1927 VYRIGYKNSqnnteKKLDLLVMENLFYGR-KMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENL-LKMVRDnplyiRSH 2004
Cdd:cd17302   150 VHRVKPVGG-----RKVRFVVMGNLFCTElRIHRRFDLKGSTHGRTTGKPESEIDPNTTLKDLDLdFKFRLE-----KGW 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 2005 SKAVLRTsIHSDSHFLSSHLIIDYSLLVG-------RDDTSNELVV--GIIDYIRTFTWDKKLEMVVKStgiLGGQGKMP 2075
Cdd:cd17302   220 RDALMRQ-IDADCAFLEALRIMDYSLLLGvhfragdSTGEPYDVVLyfGIIDILQEYNISKKLEHAYKS---LQYDPASI 295
                         330
                  ....*....|....*...
gi 767917152 2076 TVVSPELYRTRFCEAMDK 2093
Cdd:cd17302   296 SAVDPKLYSRRFRDFIRK 313
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
644-864 1.35e-26

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: 115.60  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  644 WRDIIVSLVCQVVQTVRPDVKNQDDDMdirqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:cd00309   155 GDDFLGELVVDAVLKVGKENGDVDLGV-----IRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  724 YLyreetkftcidpivlqereflknyvqrivdvrptlVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLV 803
Cdd:cd00309   230 YV-----------------------------------VIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIV 274
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152  804 MSMDQLlTKPHLGTCHKFYMQIFqlpNEQTKTlmFFEGCPQHLGCTIKLRGGSDYELARVK 864
Cdd:cd00309   275 SRLEDL-TPEDLGTAGLVEETKI---GDEKYT--FIEGCKGGKVATILLRGATEVELDEAE 329
PIPKc_PIP5KII cd17305
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type II ...
1830-2093 1.90e-24

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: 105.82  E-value: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1830 KFYCRLYyageFHKMREViLDSSEEDFIRSLSHSSP-WQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1908
Cdd:cd17305    56 KEYCPLV----FRNLRER-FGIDDDDYLNSLTRSQPlASDSPGRSGSRFLVSYDKKYVIKTISSEEVAQMHHILKQYHQY 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1909 ItnaVQQKRPTALAKILGVYRIgyknSQNNTEKKLdlLVMENLFYGR-KMAQVFDLKGSLRNRnVKTDTGKESCDVVLLD 1987
Cdd:cd17305   131 I---VERHGKTLLPQYLGMYRI----TVNGVETYL--VVMRNVFSPRlPIHKKYDLKGSTVDR-QASDKEKAKDLPTLKD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1988 ENLLKMVRDnpLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDtsnelVV---GIIDYIRTFTWDKKLEMVVKS 2064
Cdd:cd17305   201 NDFLNDGTK--IYIGDEAKAKLLETLKRDVEFLAKLNLMDYSLLVGIHD-----CIyfmAIIDILTHYGAKKRAAHAAKT 273
                         250       260
                  ....*....|....*....|....*....
gi 767917152 2065 tgILGGQGKMPTVVSPELYRTRFCEAMDK 2093
Cdd:cd17305   274 --VKHGAGAEISTVKPEQYAKRFLEFISK 300
PIPKc_PIP5K_yeast_like cd17303
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in yeast ...
1871-2093 2.73e-24

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: 105.84  E-value: 2.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1871 GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQqkrpTALAKILGVYRIgyknsQNNTEKKLDLLVMEN 1950
Cdd:cd17303    95 GKSGSFFYFSRDYRFIIKTIHHSEHKFLRKILPDYYNHVKENPN----TLLSQFYGLHRV-----KMPRGRKIHFVVMNN 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1951 LF-YGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLKmvRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYS 2029
Cdd:cd17303   166 LFpPHRDIHQTFDLKGSTVGRETPEDKLAKGPRATLKDLNWLR--RKRKLALGPEKRKQFLTQLKRDVEFLASLNIMDYS 243
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767917152 2030 LLVG-------------RDDTSNEL-VVGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMDK 2093
Cdd:cd17303   244 LLVGihdldggfqatdeNNEPGDEIyYLGIIDILTPYNAKKKLEHFFKS---LRHDRHTISAVPPKEYARRFLKFIED 318
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
368-448 1.04e-23

DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first discovered. The function of this domain is still not clear, but it is believed to be important for the membrane association of the signaling proteins in which it is present. New studies show that the DEP domain of Sst2, a yeast RGS protein is necessary and sufficient for receptor interaction.


Pssm-ID: 239836  Cd Length: 81  Bit Score: 96.64  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  368 DLWKKICHHSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALY 447
Cdd:cd04371     1 DLVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAITREEAVELGQALLKHGLIHHVSDDKHTFRDSYALY 80

                  .
gi 767917152  448 R 448
Cdd:cd04371    81 R 81
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
165-224 1.18e-22

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: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 93.21  E-value: 1.18e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152   165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPG-KFMGYTGDLRACTYC 224
Cdd:pfam01363    2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLlPELGSNKPVRVCDAC 62
PIPKc_PIP5KI cd17301
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in type I ...
1841-2091 8.39e-22

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: 98.47  E-value: 8.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1841 FHKMREvILDSSEEDFIRSLSHSsPWQ--ARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFnyiTNAVQQKRp 1918
Cdd:cd17301    65 FRYFRE-LFGIKPDDYLLSLCNE-PLRelSNPGASGSLFYLTHDDEFIIKTVQHKEAEFLQKLLPGYY---MNLNQNPR- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1919 TALAKILGVYriGYKNSQnnteKKLDLLVMENLF-YGRKMAQVFDLKGS-LRNRNVKTDTGKESCDVVLLDENllkmvRD 1996
Cdd:cd17301   139 TLLPKFYGLY--CYQSGG----KNIRFVVMNNLLpSNIKMHEKYDLKGStYKRKASKKERQKKSPTLKDLDFM-----ED 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1997 NP--LYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVG---------RDDTSNELV--VGIIDYIRTFTWDKKLEMVVK 2063
Cdd:cd17301   208 HPegILLEPDTYDALLKTIQRDCRVLESFKIMDYSLLLGvhnlggipaRNSKGERLLlfIGIIDILQSYRLKKKLEHTWK 287
                         250       260
                  ....*....|....*....|....*...
gi 767917152 2064 StgILGGqGKMPTVVSPELYRTRFCEAM 2091
Cdd:cd17301   288 S--VVHD-GDTVSVHRPSFYAERFQNFM 312
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
165-224 2.17e-21

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: 89.41  E-value: 2.17e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152    165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:smart00064    3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDC 62
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
377-449 6.53e-21

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: 88.49  E-value: 6.53e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917152    377 SSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSH-HDQLFRDEYALYRP 449
Cdd:smart00049    2 ETGLKLRDRKYFLKTYPNCFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGpNKHTFKDSKALYRF 75
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
165-224 7.06e-20

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: 85.12  E-value: 7.06e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15727     3 PWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNEC 62
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
166-224 1.01e-19

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: 84.70  E-value: 1.01e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15731     5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHC 63
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
645-862 1.63e-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: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  645 RDIIVSLVCQVVQTVRPDVKNQDD-DMDirqFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE 723
Cdd:cd03343   163 KDKLADLVVDAVLQVAEKRDGKYVvDLD---NIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  724 YLYRE-ETKFTCIDPIVL-----QEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRM 797
Cdd:cd03343   240 VKKTEiDAKIRITSPDQLqafleQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARA 319
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917152  798 TQGDLVMSMDQLlTKPHLGTCHKFymqifqlpnEQTKT----LMFFEGCPQHLGCTIKLRGGSDY---ELAR 862
Cdd:cd03343   320 TGAKIVTNIDDL-TPEDLGEAELV---------EERKVgddkMVFVEGCKNPKAVTILLRGGTEHvvdELER 381
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
646-864 4.77e-19

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


Pssm-ID: 223535 [Multi-domain]  Cd Length: 524  Bit Score: 93.05  E-value: 4.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  646 DIIVSLVCQVVQTVRPDVKNQDDdmdirqfVHIKKIPGGKKFDSVVVNGFVCTK-NIAHKKMSSC-IKNPKILLLKCSIE 723
Cdd:COG0459   157 EEIGELVVEAVEKVGKEQSDLDG-------IIIVKESGGSETELEVVEGMVFDKgYLSPYFMPDKrLENPKILLLDKKLE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  724 YLyREE--TKFTCIDPIVLQ------EREFLKNYVQRIVDVRPTLVLV-EKTVSRIAQDMLLEHGITLVINVKSQ-VLER 793
Cdd:COG0459   230 IK-KPElpLEIVISSGKPLLiiaedeEGEALATLVVNILRGGANVVVVkAPGIDDLAKAYLEDIAILTGRRVKKEdLGER 308
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  794 ISRMTQGDLVMSMDQlLTKPHLGT--CHKFYMQIFqlpNEQTKTlmFFEGCPQHLG--CTIKLRGGSDYELARVK 864
Cdd:COG0459   309 LAKLGGAKIVSVLKD-LTTIVLGEgaAGLVEETKT---GDYDME--KLQERKAKAGgvATILVRGATEVELDEKE 377
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
1814-2033 1.04e-18

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 92.97  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1814 QLINPHvelQFSDANAKFYCRLYyageFHKMREVI-LDSSE-------EDFIRSLShsSPwqargGKSGAAFYATEDDRF 1885
Cdd:PLN03185  394 QLTPSH---QSEDFKWKDYCPMV----FRNLREMFkIDAADymmsicgNDALRELS--SP-----GKSGSVFFLSQDDRF 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1886 ILKQMPRLEVQSFLDFAPHYFNYitnaVQQKRPTALAKILGVYRIGYKNSQnntekKLDLLVMENLFYGR-KMAQVFDLK 1964
Cdd:PLN03185  460 MIKTLRKSEVKVLLRMLPDYHHH----VKTYENTLITKFFGLHRIKPSSGQ-----KFRFVVMGNMFCTElRIHRRFDLK 530
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152 1965 GSLRNRnvktdtgkeSCDVVLLDEN--LLKMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVG 2033
Cdd:PLN03185  531 GSSLGR---------SADKVEIDENttLKDLDLNYSFYLEPSWRDALLRQIEIDSKFLEAQRIMDYSLLLG 592
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
165-224 2.08e-18

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: 80.86  E-value: 2.08e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTgDLRACTYC 224
Cdd:cd15729     6 VWVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEYLDNK-EARVCVPC 64
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
379-448 5.55e-18

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: 425776 [Multi-domain]  Cd Length: 70  Bit Score: 79.92  E-value: 5.55e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152   379 GMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVS-HHDqlFRDEYALYR 448
Cdd:pfam00610    1 GVKLKDRRKHLKTYPNCFTGSEAVDWLMDNLSIITREEAVELGQLLLDQGLIHHVGdKHG--FKDSYYFYR 69
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
174-224 1.16e-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: 78.34  E-value: 1.16e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767917152  174 ECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd00065     1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSC 51
PIPKc_PIP5K2B cd17310
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1830-2091 5.18e-17

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: 84.33  E-value: 5.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1830 KFYCRLYyageFHKMREViLDSSEEDFIRSLSHSSPWQARG-GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNY 1908
Cdd:cd17310    67 KEYCPMV----FRNLRER-FGIDDQDYQNSVTRSAPINSDSqGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQF 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1909 ItnaVQQKRPTALAKILGVYRIGYKNSQNNtekkldLLVMENLFYGR-KMAQVFDLKGSLRNRNVktdTGKESC-DVVLL 1986
Cdd:cd17310   142 I---VECHGNTLLPQFLGMYRLTVDGVETY------MVVTRNVFSHRlTVHRKYDLKGSTVSREA---SDKEKAkDLPTF 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1987 DENLLkMVRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSneLVVGIIDYIRTFTWDKKLEMVVKStg 2066
Cdd:cd17310   210 KDNDF-LNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVV--YFMAIIDILTPYDAKKKAAHAAKT-- 284
                         250       260
                  ....*....|....*....|....*
gi 767917152 2067 ILGGQGKMPTVVSPELYRTRFCEAM 2091
Cdd:cd17310   285 VKHGAGAEISTVNPEQYSKRFNEFM 309
PIPKc_PIP5K2A cd17309
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1830-2087 5.26e-16

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: 81.18  E-value: 5.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1830 KFYCRLYyageFHKMRE-VILDssEEDFIRSLSHSSPWQARG-GKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFN 1907
Cdd:cd17309    65 KEYCPMV----FRNLRErFGID--DQDFQNSLTRSAPLANDSqARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQ 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1908 YItnaVQQKRPTALAKILGVYRIGYKNSQnntekkLDLLVMENLFYGR-KMAQVFDLKGSLRNRNVkTDTGKESCDVVLL 1986
Cdd:cd17309   139 YI---VECHGNTLLPQFLGMYRLTVDGVE------TYMIVTRNVFSHRlSVYRKYDLKGSTVAREA-SDKEKAKELPTLK 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1987 DENLLKmvRDNPLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVGRDDTSneLVVGIIDYIRTFTWDKKLEMVVKStg 2066
Cdd:cd17309   209 DNDFIN--DGQKIYIDENNKKMFLEKLKKDVEFLAQLKLMDYSLLVGIHDVV--YFMAIIDILTHYDAKKKAAHAAKT-- 282
                         250       260
                  ....*....|....*....|.
gi 767917152 2067 ILGGQGKMPTVVSPELYRTRF 2087
Cdd:cd17309   283 VKHGAGAEISTVNPEQYSKRF 303
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
166-227 6.66e-16

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 [Multi-domain]  Cd Length: 61  Bit Score: 73.53  E-value: 6.66e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRcCNQEIPGKfmgytgdLRACTYCRKI 227
Cdd:cd15716     4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNK-CSQFLPLH-------IRCCHHCKDL 57
PIPKc_PIP5K2C cd17311
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in Phosphatidylinositol ...
1853-2089 8.21e-16

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: 80.30  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1853 EEDFIRSLSHSSPwQARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYItnaVQQKRPTALAKILGVYRIGY 1932
Cdd:cd17311    74 DQDYQVSLTRSPP-YSESEGSDGRFLLSYDRTLVIKEISSEDVADMHSILSHYHQYI---VKCHGNTLLPQFLGMYRLSV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1933 KNSQNNtekkldLLVMENLFYGR-KMAQVFDLKGSLRNRNVkTDTGKESCDVVLLDENLLKmvRDNPLYIRSHSKAVLRT 2011
Cdd:cd17311   150 DNEDSY------MLVMRNMFSHRlPVHRKYDLKGSLVSREA-SDKEKVKELPTLKDMDFLN--KNQKVYVGEEQKRIFLE 220
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767917152 2012 SIHSDSHFLSSHLIIDYSLLVGRDDTSneLVVGIIDYIRTFTWDKKLEMVVKStgILGGQGKMPTVVSPELYRTRFCE 2089
Cdd:cd17311   221 KLKRDVEFLVQLKIMDYSLLLGIHDVV--YFMGLIDILTQYDAKKKAAHAAKT--VKHGAGAEISTVHPEQYAKRFLD 294
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
166-224 1.07e-15

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: 73.10  E-value: 1.07e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  166 WMPDSqckECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP-GKFMGYTGDLRACTYC 224
Cdd:cd15760     2 WKPDS---RCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPlPHLGPLGVPQRVCDRC 58
PIPKc_PIP5K1B cd17307
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1831-2092 1.25e-15

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: 80.42  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1831 FYCRLYYAGEFHKMREvILDSSEEDFIRSLSH------SSPwqargGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPH 1904
Cdd:cd17307    55 FRFKTYAPLAFRYFRE-LFGIKPDDYLYSICSeplielSNP-----GASGSLFYVTSDDEFIIKTVQHKEAEFLQKLLPG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1905 YFnyiTNAVQQKRpTALAKILGVYRIGYKNSQnntekkLDLLVMENLF-YGRKMAQVFDLKGSLRNRNVKTDTGKESCDv 1983
Cdd:cd17307   129 YY---MNLNQNPR-TLLPKFYGLYCMQSGGIN------IRIVVMNNVLpRSVKMHYKYDLKGSTYKRRASRKEREKSCP- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1984 VLLDENLLKMVRDNpLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVG-----------RDDTSNELVVGIIDYIRTF 2052
Cdd:cd17307   198 TYKDLDFLQDMHDG-LYFDPETYNALMKTLQRDCRVLESFKIMDYSLLLGihvlggipaknHKGEKLLLFMGIIDILQSY 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767917152 2053 TWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAMD 2092
Cdd:cd17307   277 RLMKKLEHSWKA---LVYDGDTVSVHRPSFYADRFLKFMN 313
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
165-224 3.70e-15

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: 71.59  E-value: 3.70e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15734     1 YWVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPC 60
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
166-225 4.15e-14

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 [Multi-domain]  Cd Length: 83  Bit Score: 69.46  E-value: 4.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCS----RCCN-----------QEIPGKFMGYTGD-------LRACTY 223
Cdd:cd15737     2 WEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTevpldllssalPDLPFVFKEPQSDipddtksVRVCRD 81

                  ..
gi 767917152  224 CR 225
Cdd:cd15737    82 CK 83
PIPKc_PIP5K1C cd17308
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1831-2091 5.53e-14

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: 75.42  E-value: 5.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1831 FYCRLYYAGEFHKMREvILDSSEEDFIRSLSHSSPWQ-ARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFnyi 1909
Cdd:cd17308    56 FRFKTYAPVAFRYFRE-LFGIRPDDYLYSLCNEPLIElSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYY--- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1910 TNAVQQKRpTALAKILGVYRIgyknsqNNTEKKLDLLVMENLF-YGRKMAQVFDLKGSLRNRNVKTDTGKESC----DVV 1984
Cdd:cd17308   132 MNLNQNPR-TLLPKFYGLYCV------QSGGKNIRVVVMNNILpRVVKMHLKFDLKGSTYKRRASKKEREKSKptfkDLD 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1985 LLDENLLKMVRDNPLYirshsKAVLRTsIHSDSHFLSSHLIIDYSLLVGRDDTSN-----------ELVVGIIDYIRTFT 2053
Cdd:cd17308   205 FMQDMPEGLMLDADTF-----SALVKT-LQRDCLVLESFKIMDYSLLLGVHNIGGipavngkgerlLLYIGIIDILQSYR 278
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767917152 2054 WDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAM 2091
Cdd:cd17308   279 LIKKLEHTWKA---LVHDGDTVSVHRPSFYAERFFKFM 313
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
663-857 5.98e-14

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 [Multi-domain]  Cd Length: 522  Bit Score: 76.94  E-value: 5.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  663 VKNQDDDMDIrQFVHIKKIPGGKKFDSVVVNGfvctknIAHKKMSSC---------IKNPKILLLKCSIEyLYRE----E 729
Cdd:cd03340   179 VLSLDDDLDL-DMIGIKKVPGGSLEDSQLVNG------VAFKKTFSYagfeqqpkkFKNPKILLLNVELE-LKAEkdnaE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  730 TKFTciDP-----IVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTqGDLVM 804
Cdd:cd03340   251 VRVE--DPeeyqaIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQAT-GGSIQ 327
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767917152  805 SMDQLLTKPHLGTCHKFYMQifQLPNEQTKtlmFFEGCPQHLGCTIKLRGGSD 857
Cdd:cd03340   328 TTVSNITDDVLGTCGLFEER--QVGGERYN---IFTGCPKAKTCTIILRGGAE 375
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
166-208 6.41e-14

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: 67.84  E-value: 6.41e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP 208
Cdd:cd15733     1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLP 43
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
166-228 1.28e-13

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: 67.42  E-value: 1.28e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCC--NQEIPgkfmGYTGDLRACTYCRKIA 228
Cdd:cd15730     3 WADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSskTATTP----SSKKPVRVCDACFDDL 63
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
667-873 3.39e-13

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: 74.41  E-value: 3.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   667 DDDMDiRQFVHIKKIPGGKKFDSVVVNGFVCTKNIA---HKKMSSCIKNPKILLLKCSIEY-LYREETKFTCIDP----- 737
Cdd:TIGR02345  185 RDDLD-LKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILLLNVELELkAEKDNAEIRVEDVedyqa 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   738 IVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMDQLlTKPHLGT 817
Cdd:TIGR02345  264 IVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDL-EADVLGT 342
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767917152   818 CHKFYMQifQLPNEQTKtlmFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICV 873
Cdd:TIGR02345  343 CALFEER--QIGSERYN---YFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMI 393
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
165-224 3.80e-13

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: 65.69  E-value: 3.80e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15732     1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSC 60
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
174-224 2.62e-12

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: 63.56  E-value: 2.62e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767917152  174 ECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQE--IPgKFmGYTGDLRACTYC 224
Cdd:cd15720     7 ECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSstIP-KF-GIEKEVRVCDPC 57
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
166-204 3.81e-12

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 [Multi-domain]  Cd Length: 58  Bit Score: 62.96  E-value: 3.81e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCN 204
Cdd:cd15726     1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSN 39
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
166-229 5.43e-12

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: 62.78  E-value: 5.43e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIpgKFMGYTGDLRACTYCRKIAL 229
Cdd:cd15758     6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNEL--ALPSYPKPVRVCDSCHTLLL 67
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
554-874 5.54e-12

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: 70.79  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  554 DQKEYLIsDTGGQQLSISDAFIKE-SLFNRRVEEKSKELPFTPlgwhhNNLELLReengeKQAMERL----LSANHNHMM 628
Cdd:cd03339   109 EQAEKLL-DRGIHPIRIADGYEQAcKIAVEHLEEIADKIEFSP-----DNKEPLI-----QTAMTSLgskiVSRCHRQFA 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  629 allqqllhsdslssswrDIIVSLVCQVVQTVRPDVknqddDMDIrqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSS 708
Cdd:cd03339   178 -----------------EIAVDAVLSVADLERKDV-----NFEL---IKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPK 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  709 CIKNPKILLLKCSIEyLYREETKFTC-IDPI----VLQ--EREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGIT 781
Cdd:cd03339   233 EVKDAKIAILTCPFE-PPKPKTKHKLdITSVedykKLQeyEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLP 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  782 LVINVKSQVLERISRMTQGDLVMSMDQlLTKPHLGTCHKFYMQIFQLPNEQtktLMFFEGCPQHLGCTIKLRGGSDYELA 861
Cdd:cd03339   312 AVRWVGGVEIELIAIATGGRIVPRFED-LSPEKLGKAGLVREISFGTTKDK---MLVIEGCPNSKAVTIFIRGGNKMIIE 387
                         330
                  ....*....|...
gi 767917152  862 RVKEILIFMICVA 874
Cdd:cd03339   388 EAKRSLHDALCVV 400
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
165-224 6.07e-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: 62.40  E-value: 6.07e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  165 YWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15719     2 HWVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQAC 61
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
166-208 1.34e-11

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: 61.24  E-value: 1.34e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP 208
Cdd:cd15721     1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMP 43
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
384-483 1.74e-11

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange proteins directly activated by cAMP) proteins are GEFs (guanine-nucleotide-exchange factors) for the small GTPases, Rap1 and Rap2. They are directly regulated by cyclic AMP, a second messenger that plays a role in the control of diverse cellular processes, such as cell adhesion and insulin secretion. Epac-like proteins share a common domain architecture, containing RasGEF, DEP and CAP-effector (cAMP binding) domains. The DEP domain is involved in membrane localization.


Pssm-ID: 239884  Cd Length: 125  Bit Score: 63.13  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  384 DHRYWLRTHPNCIVGKELVNWLIRNGH-IATRAQAIAIGQAMVDGRWLDCVSHHDQlFRDEYALYRplqsteFSEtpspD 462
Cdd:cd04437    19 DRKYHLRTYRQCCVGTELVDWLLQQSPcVQSRSQAVGMWQVLLEEGVLLHVDQELH-FQDKYQFYR------FSD----D 87
                          90       100
                  ....*....|....*....|..
gi 767917152  463 SDSVNSVEGH-SEPSWFKDIKF 483
Cdd:cd04437    88 ECSPAPLEKReAEEELQEAVTL 109
PIPKc_PIP5K1A_like cd17306
Phosphatidylinositol phosphate kinase (PIPK) catalytic domain found in phosphatidylinositol ...
1831-2091 2.46e-11

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: 67.33  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1831 FYCRLYYAGEFHKMREvILDSSEEDFIRSLSHSSPWQ-ARGGKSGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFnyi 1909
Cdd:cd17306    58 FRFKTYAPVAFRYFRE-LFGIRPDDYLYSLCSEPLIElSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYY--- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1910 TNAVQQKRpTALAKILGVY--RIGYKNsqnntekkLDLLVMENLF-YGRKMAQVFDLKGSLRNRNVKTDTgKESCDVVLL 1986
Cdd:cd17306   134 MNLNQNPR-TLLPKFYGLYcvQAGGKN--------IRIVVMNNLLpRSVKMHLKYDLKGSTYKRRASQKE-REKPLPTYK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152 1987 DENLLKMVRDNpLYIRSHSKAVLRTSIHSDSHFLSSHLIIDYSLLVG-----------------------RDDTSNELV- 2042
Cdd:cd17306   204 DLDFLQDIPDG-LFLDSDMYNALCKTLQRDCLVLQSFKIMDYSLLVGihnidarrggtietddqmggipaRNSKGERLLl 282
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767917152 2043 -VGIIDYIRTFTWDKKLEMVVKStgiLGGQGKMPTVVSPELYRTRFCEAM 2091
Cdd:cd17306   283 yIGIIDILQSYRFVKKLEHSWKA---LVHDGDTVSVHRPGFYAERFQRFM 329
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
175-224 4.19e-11

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: 60.13  E-value: 4.19e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15728    10 CYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVC 59
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
676-873 7.71e-11

T-complex protein 1, alpha 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: 274081  Cd Length: 536  Bit Score: 67.05  E-value: 7.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   676 VHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIE-YLYREETKFTCIDP-----IVLQEREFLKNY 749
Cdd:TIGR02340  191 INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQkAKMALGVQIVVDDPekleqIRQREADITKER 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   750 VQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSM-----DQLLTKPHLGTCHKFYMQ 824
Cdd:TIGR02340  271 IKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLadlegEETFEASYLGFADEVVQE 350
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 767917152   825 ifQLPNEQtktLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICV 873
Cdd:TIGR02340  351 --RIADDE---CILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCV 394
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
175-224 3.84e-10

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: 57.15  E-value: 3.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15735     9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGC 58
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
383-448 4.95e-10

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown.


Pssm-ID: 239889 [Multi-domain]  Cd Length: 82  Bit Score: 57.60  E-value: 4.95e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917152  383 QDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALYR 448
Cdd:cd04442    16 KDRRHHLRTYPNCFVGKELIDWLIEHKEASDRETAIKIMQKLLDHSIIHHVCDEHKEFKDAKLFYR 81
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
166-224 6.14e-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: 56.61  E-value: 6.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767917152  166 WMPDSQCKECYDCSE-KFTTFRRRHHCRLCGQIFCSRCCNQeipgKFM---GYTGDLRACTYC 224
Cdd:cd15717     2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSK----KFLlphQSSKPLRVCDTC 60
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
174-226 6.41e-10

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: 56.74  E-value: 6.41e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  174 ECYDCSEKFTTF-RRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGD------LRACTYCRK 226
Cdd:cd15723     1 NCTGCGASFSVLlKKRRSCNNCGNAFCSRCCSKKVPRSVMGATAPaaqretVFVCSGCND 60
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
166-227 6.48e-10

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: 56.73  E-value: 6.48e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767917152  166 WMPDSQCKECYDCSEKFTT-FRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDlRACTYCRKI 227
Cdd:cd15741     3 WVRDNEVTMCMRCKEPFNAlTRRRHHCRACGYVVCWKCSDYKATLEYDGNKLN-RVCKHCYVI 64
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
662-874 7.37e-10

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 [Multi-domain]  Cd Length: 532  Bit Score: 64.05  E-value: 7.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   662 DVKNQDDDMDIrqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEyLYREETKFTCI------ 735
Cdd:TIGR02343  193 DMERRDVDFDL---IKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFE-PPKPKTKHKLDissvee 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   736 -DPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMdQLLTKPH 814
Cdd:TIGR02343  269 yKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRF-QELSKDK 347
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   815 LGTCHKFYMQIFQLPNEQtktLMFFEGCPQHLGCTIKLRGGSDYELARVKEILIFMICVA 874
Cdd:TIGR02343  348 LGKAGLVREISFGTTKDR---MLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
166-208 7.59e-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 [Multi-domain]  Cd Length: 61  Bit Score: 56.57  E-value: 7.59e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767917152  166 WMPDSQCKECyDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP 208
Cdd:cd15738     3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRA 44
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
166-224 1.18e-09

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: 55.91  E-value: 1.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTgDLRACTYC 224
Cdd:cd15743     3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLKNK-SARVCDEC 60
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
646-864 1.63e-09

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 [Multi-domain]  Cd Length: 484  Bit Score: 62.66  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  646 DIIVSLVCQVVQTVRPDVKNQDDDMdirqfVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYl 725
Cdd:cd03342   162 DQLTEIVVDAVLAIYKPDEPIDLHM-----VEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEY- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  726 yrEETKFTCidpivlqerEFLKNyvqrivdvrptLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMS 805
Cdd:cd03342   236 --EKTEVNS---------GFFYS-----------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNS 293
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767917152  806 MDQLlTKPHLGTCHKFYMQIFqlpNEQTKTlmFFEGCPQHLGCTIKLRGGSDYELARVK 864
Cdd:cd03342   294 VDDL-SPECLGYAGLVYERTL---GEEKYT--FIEGVKNPKSCTILIKGPNDHTITQIK 346
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
166-227 2.58e-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: 55.04  E-value: 2.58e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  166 WMPDSQCKECYDCSE-KFTTFRRRHHCRLCGQIFCSRCCNQE--IPGKfmgYTGDLRACTYCRKI 227
Cdd:cd15755     2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKflLPSQ---SSKPVRVCDFCYDL 63
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
164-234 8.43e-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: 53.88  E-value: 8.43e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917152  164 QYWMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPgkFMGYTGDLRACTYCRKIALSYAHS 234
Cdd:cd15759     2 QVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELP--LPSSPKPVRVCDSCHAMLIQRCSS 70
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
175-224 1.51e-08

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: 52.50  E-value: 1.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15745     2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTC 51
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
166-202 1.97e-08

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: 52.52  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767917152  166 WMPDSQCKECYDCS-EKFTTFRRRHHCRLCGQIFCSRC 202
Cdd:cd15724     1 WVPDEAVSVCMVCQvERFSMFNRRHHCRRCGRVVCSSC 38
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
166-208 2.76e-08

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: 52.34  E-value: 2.76e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767917152  166 WMPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP 208
Cdd:cd15739     4 WQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVP 46
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
175-224 5.44e-08

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: 51.03  E-value: 5.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP----GKFMGYTGDLRACTYC 224
Cdd:cd15736     2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPlnlsAYDPRNGKWYRCCHSC 55
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
166-226 7.09e-08

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: 51.11  E-value: 7.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  166 WMPDSQCKECYDCSE-KFTTFRRRHHCRLCGQIFCSRCCNQeipgKFMGYT---GDLRACTYCRK 226
Cdd:cd15754     2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRQ----RFLIPRlspKPVRVCSLCYR 62
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
676-856 7.41e-08

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 57.35  E-value: 7.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  676 VHIKKIPGGKKFDSVVVNGFVCTKNIA---HKKMSscikNPKILLLKCSIEY----LYREETK---FTCIDPIVLQEREF 745
Cdd:PTZ00212  201 IQIIKKPGGTLRDSYLEDGFILEKKIGvgqPKRLE----NCKILVANTPMDTdkikIYGAKVKvdsMEKVAEIEAAEKEK 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  746 LKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSMDQLLtKPHLGTCHKfyMQI 825
Cdd:PTZ00212  277 MKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPE-KVKLGHCDL--IEE 353
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767917152  826 FQLPNEqtkTLMFFEGCPQHLGCTIKLRGGS 856
Cdd:PTZ00212  354 IMIGED---KLIRFSGCAKGEACTIVLRGAS 381
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
384-448 8.61e-08

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like proteins, also known as PGR22, contain an N-terminal permease domain, a central transmembrane region and a C-terminal DEP domain. They are orphan receptors of the class B G protein-coupled receptors. Their function is unknown.


Pssm-ID: 239890 [Multi-domain]  Cd Length: 83  Bit Score: 51.56  E-value: 8.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917152  384 DHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVS--HHdqlFRDEYALYR 448
Cdd:cd04443    19 DRRCGLRTYKGVFCGCDLVSWLIEVGLAQDRGEAVLYGRRLLQGGVLQHITneHH---FRDENLLYR 82
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
367-448 1.41e-07

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and by the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity.


Pssm-ID: 239886  Cd Length: 81  Bit Score: 50.64  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  367 KDLWKKICHHSSGMefQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQlFRDEYAL 446
Cdd:cd04439     2 EKLYKMMCKQGSLI--KDRRRKLSTFPKCFLGNEFVSWLLEIGEISKPEEGVNLGQALLENGIIHHVSDKHQ-FKNEQVL 78

                  ..
gi 767917152  447 YR 448
Cdd:cd04439    79 YR 80
DEP_DEPDC5-like cd04449
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in ...
376-448 5.35e-07

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in DEPDC5-like proteins. DEPDC5, in human also known as KIAA0645, is a DEP domain containing protein of unknown function.


Pssm-ID: 239896  Cd Length: 83  Bit Score: 49.20  E-value: 5.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917152  376 HSSGMEFQDHRYWLRTHPNCIVGKELVNWLIRN-GHIATRAQAIAIGQAMVDGRWLDCVSHHDQlFRDEYALYR 448
Cdd:cd04449    10 DPSGIGIFDRSWHKGLPSNCFIGSEAVSWLINNfEDVDTREEAVELGQELMNEGLIEHVSGRHP-FLDGFYFYY 82
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
663-865 9.46e-07

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 [Multi-domain]  Cd Length: 531  Bit Score: 53.97  E-value: 9.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   663 VKNQDDDMDIrQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMSSCIKNPKILLLKCSIEYLYREETKFTCI------D 736
Cdd:TIGR02347  179 IKKDGEDIDL-FMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYssaeqrE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152   737 PIVLQEREFLKNYVQRIVDVRPTL----------VLVEKTVSRIAQDMLLEHGITLVINVKSQVLERISRMTQGDLVMSM 806
Cdd:TIGR02347  258 KLVKAERKFVDDRVKKIIELKKKVcgkspdkgfvVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSV 337
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767917152   807 DQlLTKPHLGTCHKFYMQIFqlpNEQTKTlmFFEGCPQHLGCTIKLRGGSDYELARVKE 865
Cdd:TIGR02347  338 ED-LTPECLGWAGLVYETTI---GEEKYT--FIEECKNPKSCTILIKGPNDHTIAQIKD 390
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
180-224 1.75e-06

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: 47.32  E-value: 1.75e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767917152  180 EKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15718    25 EKKTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMGFEFPVRVCNEC 69
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
167-212 5.99e-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: 45.70  E-value: 5.99e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767917152  167 MPDSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFM 212
Cdd:cd15742     4 VPVSHVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYL 49
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
166-224 1.42e-05

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: 45.06  E-value: 1.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917152  166 WMPDSQCKEC-----YDCSEKFTTFR---RRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15756     3 WLESDSCQKCeqpffWNIKQMWDTKTlglRQHHCRKCGQAVCGKCSSKRSSYPIMGFEFQVRVCDSC 69
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
175-208 2.10e-05

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: 43.65  E-value: 2.10e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIP 208
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAV 35
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
175-225 5.57e-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: 42.35  E-value: 5.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMgytgdlraCTYCR 225
Cdd:cd15750     3 CESCGAKFSVFKRKRTCADCKRYFCSNCLSKEERGRRR--------CRRCR 45
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
169-202 6.61e-05

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: 42.30  E-value: 6.61e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767917152  169 DSQCKECYDCSEKFTTF-RRRHHCRLCGQIFCSRC 202
Cdd:cd15740     2 EKEKQTCKGCNESFNSItKRRHHCKQCGAVICGKC 36
DEP_2_P-Rex cd04440
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex ...
383-448 3.10e-04

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity.


Pssm-ID: 239887  Cd Length: 93  Bit Score: 41.83  E-value: 3.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767917152  383 QDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLdcvsHH---DQLFRDEYALYR 448
Cdd:cd04440    25 KDRDYHLKTYKSVVPASKLVDWLLAQGDCRTREEAVILGVGLCNNGFM----HHvleKSEFKDEPLLFR 89
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
166-224 3.76e-04

FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); 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. WDFY2 contains WD40 motifs and a FYVE domain.


Pssm-ID: 277296 [Multi-domain]  Cd Length: 70  Bit Score: 40.82  E-value: 3.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917152  166 WMPDSQCKEC-----YDCSEKFTTFR---RRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYC 224
Cdd:cd15757     3 WLDSDSCQKCdqpffWNFKQMWDSKKiglRQHHCRKCGKAVCGKCSSKRSTIPLMGFEFEVRVCDSC 69
DEP_RGS7-like cd04450
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in RGS (regulator of G-protein ...
377-449 1.31e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in RGS (regulator of G-protein signaling) proteins of the subfamily R7. This subgroup contains RGS7, RGS6, RGS9 and RGS11. They share a common domain architecture, containing, beside the RGS domain, a DEP domain and a GGL (G-protein gamma subunit-like ) domain. RGS proteins are GTPase-activating (GAP) proteins of heterotrimeric G proteins by increasing the rate of GTP hydrolysis of the alpha subunit. The fungal homologs, like yeast Sst2, share a related common domain architecture, containing RGS and DEP domains. Sst2 has been identified as the principal regulator of mating pheromone signaling and recently the DEP domain of Sst2 has been shown to be necessary and sufficient to mediate receptor interaction.


Pssm-ID: 239897  Cd Length: 88  Bit Score: 39.58  E-value: 1.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767917152  377 SSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLDCVSHHDQLFRDEYALYRP 449
Cdd:cd04450    10 EVGVRMRTEKSFLTTVPYAFTGKAIVQWLMDCTDVVDPSEALEIAALFVKYGLITPVSDHRSLLKPDETLYRF 82
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
646-857 2.04e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, theta 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: 239457 [Multi-domain]  Cd Length: 472  Bit Score: 42.98  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  646 DIIVSLVCQVVQTVRPDvknqdddmDIRQF----VHIKKIPGGKKFDSVVVNGFVCTKNiAHKKMSScIKNPKILLLKCS 721
Cdd:cd03341   158 DFLSPLVAEACISVLPE--------NIGNFnvdnIRVVKILGGSLEDSKVVRGMVFKRE-PEGSVKR-VKKAKVAVFSCP 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917152  722 IEylyreetkfTCIDPIVlqereflknyvqrivdvrptlvlVEKTVSRIAQDMLLEHGItLVINVKSQV-LERISRMTQG 800
Cdd:cd03341   228 FD---------IGVNVIV-----------------------AGGSVGDLALHYCNKYGI-MVIKINSKFeLRRLCRTVGA 274
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917152  801 DLVMSMDqLLTKPHLGTCHKFYMQ--------IFQLPNEQTKTlmffegcpqhlgCTIKLRGGSD 857
Cdd:cd03341   275 TPLPRLG-APTPEEIGYCDSVYVEeigdtkvvVFRQNKEDSKI------------ATIVLRGATQ 326
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
172-224 3.46e-03

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 37.40  E-value: 3.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767917152  172 CKECYDcsEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTgDLRACTYC 224
Cdd:cd15744     2 CSLCQE--DFASLALPKHNCYNCGGTFCDACSSNELPLPSSIYE-PARVCDVC 51
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
175-204 4.05e-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: 38.02  E-value: 4.05e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRCCN 204
Cdd:cd15761    13 CSECGKTLNKKNGIVNCRKCGELFCNEHCR 42
FYVE_CARP1 cd15769
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ...
175-224 5.26e-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: 5.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767917152  175 CYDCSEKFTTFRRRHHCRLCGQIFCSRC-CNQEipgkfmgytgDLRACTYC 224
Cdd:cd15769     4 CKACGLAFSVFRKKHVCCDCKKDFCSVCsVLQE----------NLRRCSTC 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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