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Conserved domains on  [gi|19923084|ref|NP_612152|]
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polycystin-1-like protein 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1796-1914 1.47e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238850  Cd Length: 120  Bit Score: 195.19  E-value: 1.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1796 QLYAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGW 1875
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19923084 1876 FISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVERELTC 1914
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
460-833 7.05e-29

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 127.89  E-value: 7.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    460 ADSQVNQKSTVVIHHFPSIPSYNVSFISQTQVGDSQAWHSMTVWYKMQSVSVYTN-GTVFATDTDITFTAVTKETIPLEF 538
Cdd:TIGR00864 1906 AAPEVLQPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCcAAGIATGEEKNFTANVQRGKPVAF 1985
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    539 EWYFG-----EDPPVRTTSRSIKKRLSIPQWYRVMVKASNRMSSVvSEPHVIRVQKKIVANRLTS-PSSALVNASVAFEC 612
Cdd:TIGR00864 1986 AWTFDlhhlhGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE-NITLQLEAQDALMDAALQAgPQDCFTNKMAQFEA 2064
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    613 WINFGTD-VAYLWDFGDGTVS--LGSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEPCQPPLVKNMGPGKVQI 689
Cdd:TIGR00864 2065 ATSPKPNfMACHWDFGDGSAGqdTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAI 2144
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    690 WRSQPVRLgvtfEAAV---FCdISQGLSYTWNLM-----DSEGLPVS--------------LPAAVDTHRQTLILPSHTL 747
Cdd:TIGR00864 2145 RRSQPNLL----EAHVdlkDC-LRYGAEYLWEILraascDNDGHFARgalngatrsfpvipLPAEVDVQRLQLSLPKLAL 2219
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    748 EYGNYTALAKVQIEGSVVYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSspIVLRGTQSFDPD-DPG--ATLRYHWEC- 823
Cdd:TIGR00864 2220 AAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNlDDDdqSLLHFHWACq 2297
                          410
                   ....*....|
gi 19923084    824 ATAGSPAHPC 833
Cdd:TIGR00864 2298 ASSKGEAGCC 2307
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
2336-2511 1.56e-18

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


The actual alignment was detected with superfamily member pfam20519:

Pssm-ID: 466668  Cd Length: 199  Bit Score: 86.32  E-value: 1.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   2336 DWWDWSLTTLLDGLYPGGTPSarvpGAQPGALGGKCYLIGSSVIRQLKVFPRHlCKPPRPFSalieDSIPTCSPEVG--- 2412
Cdd:pfam20519   10 DIWDWLSSVLLPALHSNKTPS----GLPGSFIAYESLLLGVPRLRQLRVRNSS-CLVHDKFV----REINECHAGYSpps 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   2413 --------------GPENPYLIDPENQNV--------TLNGPGGCGTredcVLSLGRTRTEAHTALSRLRASMWIDRSTR 2470
Cdd:pfam20519   81 edrklysalpykpvHYGSKYWFIYTPPGLlmgydhwgHLASYPSGGY----VVLLPSSREESLKRLAYLQDNNWLDRGTR 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 19923084   2471 AVSVHFTLYNPPTQLFTSVSLRVEILPTGSLVPSSLVESFS 2511
Cdd:pfam20519  157 AVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVK 197
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
1140-1284 1.06e-11

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


The actual alignment was detected with superfamily member pfam02010:

Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 69.84  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   1140 VFQGYSSSGITEQTVTIKPYSLSSGETYVLQVSVASKHGLL-GKAQLYLTVNPAPRDMACQVQPHHGLEAHTVFSVFCmS 1218
Cdd:pfam02010  258 QLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVsGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTC-Q 336
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923084   1219 GKPDFHYEFSYQIGNTSKHT-------LYHGRDTQYY-FVLPAGEHLDNYKVMVSTEITDGKGSKVQ-PCTVVVT 1284
Cdd:pfam02010  337 GWTDDDLPLTYQFGDISFREaseewflLYEGSSQISIsTFLPPGLPANDYQVTVVVVVYDSLGAATSvSLTITVT 411
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
739-931 2.99e-11

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


The actual alignment was detected with superfamily member pfam02010:

Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 68.68  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    739 TLILPSHTLEYGNYTALAKVQIEGSV-VYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSspIVLRGTQSFDPD-DPGAT 816
Cdd:pfam02010   42 QLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIITVTVQPSPLVAVIDGGSSRVVGYNQD--LTLDGSESYDPDvDPGSS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    817 --LRYHWECATAGSPAHPCF--------DSSTAHQLDAAAPTVSFEAQWLSdSYDQFLVMLRVSSGGRNSSET----RVF 882
Cdd:pfam02010  120 sgLTYLWSCRRSSSGDNPLLnndpvcfsDQNEGTLLQSTSSSLTIPASTLQ-ANVTYTFKLTVSKGSRNSASTtqtiLVV 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19923084    883 LSPYPDsafrfVHISWVSFKDTFVNWNDELSLQA-MCEDC-SEIPNLSYSW 931
Cdd:pfam02010  199 DGNPPI-----IILSCISNCNRKNNPVDRLVLLAsTCLNCsSDLSDVTYRW 244
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1796-1914 1.47e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 195.19  E-value: 1.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1796 QLYAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGW 1875
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19923084 1876 FISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVERELTC 1914
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
460-833 7.05e-29

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 127.89  E-value: 7.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    460 ADSQVNQKSTVVIHHFPSIPSYNVSFISQTQVGDSQAWHSMTVWYKMQSVSVYTN-GTVFATDTDITFTAVTKETIPLEF 538
Cdd:TIGR00864 1906 AAPEVLQPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCcAAGIATGEEKNFTANVQRGKPVAF 1985
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    539 EWYFG-----EDPPVRTTSRSIKKRLSIPQWYRVMVKASNRMSSVvSEPHVIRVQKKIVANRLTS-PSSALVNASVAFEC 612
Cdd:TIGR00864 1986 AWTFDlhhlhGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE-NITLQLEAQDALMDAALQAgPQDCFTNKMAQFEA 2064
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    613 WINFGTD-VAYLWDFGDGTVS--LGSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEPCQPPLVKNMGPGKVQI 689
Cdd:TIGR00864 2065 ATSPKPNfMACHWDFGDGSAGqdTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAI 2144
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    690 WRSQPVRLgvtfEAAV---FCdISQGLSYTWNLM-----DSEGLPVS--------------LPAAVDTHRQTLILPSHTL 747
Cdd:TIGR00864 2145 RRSQPNLL----EAHVdlkDC-LRYGAEYLWEILraascDNDGHFARgalngatrsfpvipLPAEVDVQRLQLSLPKLAL 2219
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    748 EYGNYTALAKVQIEGSVVYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSspIVLRGTQSFDPD-DPG--ATLRYHWEC- 823
Cdd:TIGR00864 2220 AAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNlDDDdqSLLHFHWACq 2297
                          410
                   ....*....|
gi 19923084    824 ATAGSPAHPC 833
Cdd:TIGR00864 2298 ASSKGEAGCC 2307
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
2336-2511 1.56e-18

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 86.32  E-value: 1.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   2336 DWWDWSLTTLLDGLYPGGTPSarvpGAQPGALGGKCYLIGSSVIRQLKVFPRHlCKPPRPFSalieDSIPTCSPEVG--- 2412
Cdd:pfam20519   10 DIWDWLSSVLLPALHSNKTPS----GLPGSFIAYESLLLGVPRLRQLRVRNSS-CLVHDKFV----REINECHAGYSpps 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   2413 --------------GPENPYLIDPENQNV--------TLNGPGGCGTredcVLSLGRTRTEAHTALSRLRASMWIDRSTR 2470
Cdd:pfam20519   81 edrklysalpykpvHYGSKYWFIYTPPGLlmgydhwgHLASYPSGGY----VVLLPSSREESLKRLAYLQDNNWLDRGTR 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 19923084   2471 AVSVHFTLYNPPTQLFTSVSLRVEILPTGSLVPSSLVESFS 2511
Cdd:pfam20519  157 AVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVK 197
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
1798-1904 4.06e-14

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 70.92  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   1798 YAVVIDTGFRAPARLTSKVYIVLCGDNGlsETKELSCP-EKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGWF 1876
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVG--ESAQLEITlDNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78
                           90       100
                   ....*....|....*....|....*....
gi 19923084   1877 ISHVMV-KELHTGQGWFFPAQCWLSAGRH 1904
Cdd:pfam01477   79 LKSITVeVPGETGGKYTFPCNSWVYGSKK 107
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
1140-1284 1.06e-11

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 69.84  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   1140 VFQGYSSSGITEQTVTIKPYSLSSGETYVLQVSVASKHGLL-GKAQLYLTVNPAPRDMACQVQPHHGLEAHTVFSVFCmS 1218
Cdd:pfam02010  258 QLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVsGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTC-Q 336
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923084   1219 GKPDFHYEFSYQIGNTSKHT-------LYHGRDTQYY-FVLPAGEHLDNYKVMVSTEITDGKGSKVQ-PCTVVVT 1284
Cdd:pfam02010  337 GWTDDDLPLTYQFGDISFREaseewflLYEGSSQISIsTFLPPGLPANDYQVTVVVVVYDSLGAATSvSLTITVT 411
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
739-931 2.99e-11

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 68.68  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    739 TLILPSHTLEYGNYTALAKVQIEGSV-VYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSspIVLRGTQSFDPD-DPGAT 816
Cdd:pfam02010   42 QLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIITVTVQPSPLVAVIDGGSSRVVGYNQD--LTLDGSESYDPDvDPGSS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    817 --LRYHWECATAGSPAHPCF--------DSSTAHQLDAAAPTVSFEAQWLSdSYDQFLVMLRVSSGGRNSSET----RVF 882
Cdd:pfam02010  120 sgLTYLWSCRRSSSGDNPLLnndpvcfsDQNEGTLLQSTSSSLTIPASTLQ-ANVTYTFKLTVSKGSRNSASTtqtiLVV 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19923084    883 LSPYPDsafrfVHISWVSFKDTFVNWNDELSLQA-MCEDC-SEIPNLSYSW 931
Cdd:pfam02010  199 DGNPPI-----IILSCISNCNRKNNPVDRLVLLAsTCLNCsSDLSDVTYRW 244
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
597-663 6.54e-11

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 60.09  E-value: 6.54e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923084    597 TSPSSALVNASVAFECWINFGTDVAYLWDFGDGTV-SLGSSSSSHVYSREGEFTVEVLAFNNVSASTL 663
Cdd:pfam00801    3 ASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
592-662 5.24e-10

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 57.85  E-value: 5.24e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923084     592 VANRLTSPSSALVNASVAFECWI-NFGTDVAYLWDFGDGTVSLGsSSSSHVYSREGEFTVEVLAFNNVSAST 662
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTATSsDDGSIVSYTWDFGDGTSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSAS 71
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
599-670 1.13e-08

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 54.42  E-value: 1.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923084  599 PSSALVNASVAFECWI-NFGTDVAYLWDFGDGTVSL-GSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIV 670
Cdd:cd00146    8 PPVAELGASVTFSASDsSGGSIVSYKWDFGDGEVSSsGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
598-673 1.09e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 50.44  E-value: 1.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923084  598 SPSSALVNASVAFEcWINFGTDVAYLWDFGDGTVSLGsSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEP 673
Cdd:COG3291    4 TPTSGCAPLTVQFT-DTSSGNATSYEWDFGDGTTSTE-ANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1798-1900 1.82e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 45.71  E-value: 1.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    1798 YAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDsrGPSPGWFI 1877
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNE--HRHPEWFL 80
                            90       100
                    ....*....|....*....|...
gi 19923084    1878 SHVMVKELHTGQGWFFPAQCWLS 1900
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVY 103
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1796-1914 1.47e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 195.19  E-value: 1.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1796 QLYAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGW 1875
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19923084 1876 FISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVERELTC 1914
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
460-833 7.05e-29

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 127.89  E-value: 7.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    460 ADSQVNQKSTVVIHHFPSIPSYNVSFISQTQVGDSQAWHSMTVWYKMQSVSVYTN-GTVFATDTDITFTAVTKETIPLEF 538
Cdd:TIGR00864 1906 AAPEVLQPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCcAAGIATGEEKNFTANVQRGKPVAF 1985
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    539 EWYFG-----EDPPVRTTSRSIKKRLSIPQWYRVMVKASNRMSSVvSEPHVIRVQKKIVANRLTS-PSSALVNASVAFEC 612
Cdd:TIGR00864 1986 AWTFDlhhlhGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE-NITLQLEAQDALMDAALQAgPQDCFTNKMAQFEA 2064
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    613 WINFGTD-VAYLWDFGDGTVS--LGSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEPCQPPLVKNMGPGKVQI 689
Cdd:TIGR00864 2065 ATSPKPNfMACHWDFGDGSAGqdTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAI 2144
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    690 WRSQPVRLgvtfEAAV---FCdISQGLSYTWNLM-----DSEGLPVS--------------LPAAVDTHRQTLILPSHTL 747
Cdd:TIGR00864 2145 RRSQPNLL----EAHVdlkDC-LRYGAEYLWEILraascDNDGHFARgalngatrsfpvipLPAEVDVQRLQLSLPKLAL 2219
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    748 EYGNYTALAKVQIEGSVVYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSspIVLRGTQSFDPD-DPG--ATLRYHWEC- 823
Cdd:TIGR00864 2220 AAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNlDDDdqSLLHFHWACq 2297
                          410
                   ....*....|
gi 19923084    824 ATAGSPAHPC 833
Cdd:TIGR00864 2298 ASSKGEAGCC 2307
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
1798-1914 1.01e-27

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 109.95  E-value: 1.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1798 YAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKEL-SCPEKPLFERNSRHTFILSAPAqLGLLRKIRLWHDSRGPSPGWF 1876
Cdd:cd01756    3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLkKSNNKNKFERGQTDKFTVEAVD-LGKLKKIRIGHDNSGLGAGWF 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 19923084 1877 ISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVERELTC 1914
Cdd:cd01756   82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
2336-2511 1.56e-18

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 86.32  E-value: 1.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   2336 DWWDWSLTTLLDGLYPGGTPSarvpGAQPGALGGKCYLIGSSVIRQLKVFPRHlCKPPRPFSalieDSIPTCSPEVG--- 2412
Cdd:pfam20519   10 DIWDWLSSVLLPALHSNKTPS----GLPGSFIAYESLLLGVPRLRQLRVRNSS-CLVHDKFV----REINECHAGYSpps 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   2413 --------------GPENPYLIDPENQNV--------TLNGPGGCGTredcVLSLGRTRTEAHTALSRLRASMWIDRSTR 2470
Cdd:pfam20519   81 edrklysalpykpvHYGSKYWFIYTPPGLlmgydhwgHLASYPSGGY----VVLLPSSREESLKRLAYLQDNNWLDRGTR 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 19923084   2471 AVSVHFTLYNPPTQLFTSVSLRVEILPTGSLVPSSLVESFS 2511
Cdd:pfam20519  157 AVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVK 197
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
1798-1908 8.31e-17

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 78.53  E-value: 8.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1798 YAVVIDTGFRAPARLTSKVYIVLCGDNGLSE-TKELSCPEKplFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGWF 1876
Cdd:cd00113    3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSdIPILDGPGS--FERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 19923084 1877 ISHVMVKELHTGQGWFFPAQCWLSAGRHDGRV 1908
Cdd:cd00113   81 CESITVQALGTKKVYTFPVNRWVLGGKWYTSV 112
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
1798-1904 4.06e-14

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 70.92  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   1798 YAVVIDTGFRAPARLTSKVYIVLCGDNGlsETKELSCP-EKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGWF 1876
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVG--ESAQLEITlDNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78
                           90       100
                   ....*....|....*....|....*....
gi 19923084   1877 ISHVMV-KELHTGQGWFFPAQCWLSAGRH 1904
Cdd:pfam01477   79 LKSITVeVPGETGGKYTFPCNSWVYGSKK 107
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
1140-1284 1.06e-11

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 69.84  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084   1140 VFQGYSSSGITEQTVTIKPYSLSSGETYVLQVSVASKHGLL-GKAQLYLTVNPAPRDMACQVQPHHGLEAHTVFSVFCmS 1218
Cdd:pfam02010  258 QLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVsGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTC-Q 336
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923084   1219 GKPDFHYEFSYQIGNTSKHT-------LYHGRDTQYY-FVLPAGEHLDNYKVMVSTEITDGKGSKVQ-PCTVVVT 1284
Cdd:pfam02010  337 GWTDDDLPLTYQFGDISFREaseewflLYEGSSQISIsTFLPPGLPANDYQVTVVVVVYDSLGAATSvSLTITVT 411
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
739-931 2.99e-11

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 68.68  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    739 TLILPSHTLEYGNYTALAKVQIEGSV-VYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSspIVLRGTQSFDPD-DPGAT 816
Cdd:pfam02010   42 QLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIITVTVQPSPLVAVIDGGSSRVVGYNQD--LTLDGSESYDPDvDPGSS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    817 --LRYHWECATAGSPAHPCF--------DSSTAHQLDAAAPTVSFEAQWLSdSYDQFLVMLRVSSGGRNSSET----RVF 882
Cdd:pfam02010  120 sgLTYLWSCRRSSSGDNPLLnndpvcfsDQNEGTLLQSTSSSLTIPASTLQ-ANVTYTFKLTVSKGSRNSASTtqtiLVV 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19923084    883 LSPYPDsafrfVHISWVSFKDTFVNWNDELSLQA-MCEDC-SEIPNLSYSW 931
Cdd:pfam02010  199 DGNPPI-----IILSCISNCNRKNNPVDRLVLLAsTCLNCsSDLSDVTYRW 244
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
597-663 6.54e-11

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 60.09  E-value: 6.54e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923084    597 TSPSSALVNASVAFECWINFGTDVAYLWDFGDGTV-SLGSSSSSHVYSREGEFTVEVLAFNNVSASTL 663
Cdd:pfam00801    3 ASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
592-662 5.24e-10

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 57.85  E-value: 5.24e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923084     592 VANRLTSPSSALVNASVAFECWI-NFGTDVAYLWDFGDGTVSLGsSSSSHVYSREGEFTVEVLAFNNVSAST 662
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTATSsDDGSIVSYTWDFGDGTSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSAS 71
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
471-661 1.13e-09

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 64.72  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    471 VIHHFPSIPSYNVSFISQTQVGDSQAWHSMTVWYKMQSVSVYTNGTVFATDTDITFTAVTKETIPLEFEWYFG--EDPPV 548
Cdd:TIGR00864 1306 ISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGgeEAAPL 1385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    549 RTTSRSIKKRLSIPQWYRVMVKASNRMSSvVSEPHVIRVQKKIVANRLTSPSSALVNASVAFECW---INFGTDVAYLWD 625
Cdd:TIGR00864 1386 PAAGAEVTFIYNDPGCYLVTVAASNNISA-ANDSALIEVLEPVGATSFKHNGSHGNNLELGQPYLfsaFGRARNASYLWD 1464
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 19923084    626 FGDGTVsLGSSSSSHVYSREGEFTVEVLAFNNVSAS 661
Cdd:TIGR00864 1465 FGDGGL-LEGPEILHAFNSPGDFNIRLAAANEVGKN 1499
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
599-670 1.13e-08

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 54.42  E-value: 1.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923084  599 PSSALVNASVAFECWI-NFGTDVAYLWDFGDGTVSL-GSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIV 670
Cdd:cd00146    8 PPVAELGASVTFSASDsSGGSIVSYKWDFGDGEVSSsGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
500-676 7.26e-07

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 55.47  E-value: 7.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    500 MTVWYKMQSVSVYTNGTVFATDTDITFTAvtkETIP----LEFEWYFGEDPPVRTTSR-SIKKRLSIPQWYRVMVKASNR 574
Cdd:TIGR00864 1081 MSVRAILPRVAIGTEDGLLLAGKPADFEA---HPLPspggIHYEWDFGDGSALLQGRQpAAAHTFAKRGPFHVCLEVNNT 1157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    575 MSSVVSEPHViRVQKKIVANRLTSPSSALVNASVAFECWINFGTDVAYLWDFGDGTV-SLGSSSSSHVYSREGEFTVEVL 653
Cdd:TIGR00864 1158 ISGAAACADM-FAFEEIEGLSADMSLATELGAATTVRAALQSGDNITWTFDMGDGKSlSGPEATVEHKYAKAGNCTVNIG 1236
                          170       180       190
                   ....*....|....*....|....*....|....
gi 19923084    654 AFNNVS--ASTLRQQLFIV---------CEPCQP 676
Cdd:TIGR00864 1237 AANAAGhgARIIHVEVFVFevagiepaaCIGEHA 1270
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
1797-1919 2.91e-06

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 48.30  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1797 LYAVVIDTGF-RAPARLTSKVYIVLCGDngLSETKELSCPekplfernsRHTFILSAPAQ-LGLLRKIRLWHDSRGPSPG 1874
Cdd:cd01757    2 PYHVVIVPSKkLGGSMFTANPWICVSGE--LGETPPLQIP---------KNSLEMTFDCQnLGKLTTVQIGHDNSGLLAK 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 19923084 1875 WFISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVerELTCLQGGL 1919
Cdd:cd01757   71 WLVEYVMVRNEITGHTYKFPCGRWLGEGVDDGNG--EDGSLERVL 113
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
511-580 4.48e-06

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 46.61  E-value: 4.48e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    511 VYTNGTVFATDTDITFTAVTKETIPLEFEWYFGEDPPVRTTSRSIKKRLSIPQWYRVMVKASNRMSSVVS 580
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
598-673 1.09e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 50.44  E-value: 1.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923084  598 SPSSALVNASVAFEcWINFGTDVAYLWDFGDGTVSLGsSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEP 673
Cdd:COG3291    4 TPTSGCAPLTVQFT-DTSSGNATSYEWDFGDGTTSTE-ANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1798-1900 1.82e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 45.71  E-value: 1.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    1798 YAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDsrGPSPGWFI 1877
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNE--HRHPEWFL 80
                            90       100
                    ....*....|....*....|...
gi 19923084    1878 SHVMVKELHTGQGWFFPAQCWLS 1900
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVY 103
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
1797-1912 3.35e-04

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 42.91  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084 1797 LYAVVIDTGFRAPARLTSKVYIVLCGDNG-------LSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSR 1869
Cdd:cd01754    2 VYTIYVQTGSIWKAGTDSRISLQIYDADGpglrianLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19923084 1870 GPSPGWFISHVMVKElhTGQGwffpAQCwlsaGRHDGRVEREL 1912
Cdd:cd01754   82 GNHPGWYVNYVEVTQ--AGQH----APC----MQHLFAVEQWL 114
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
620-650 7.60e-04

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 40.72  E-value: 7.60e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 19923084    620 VAYLWDFGDGTVSLGsSSSSHVYSREGEFTV 650
Cdd:pfam18911   35 LSYRWDFGDGTTATG-ANVSHTYAAPGTYTV 64
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
420-800 2.05e-03

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 43.92  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    420 YNEFHGTEVELG-PYYVEigheAVSAFMNSSSVHEdevlvFADSQVnQKSTVVIHHFPSIPSYNVSFISQTQVGDSQAWH 498
Cdd:TIGR00864 1434 HNGSHGNNLELGqPYLFS----AFGRARNASYLWD-----FGDGGL-LEGPEILHAFNSPGDFNIRLAAANEVGKNEATL 1503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    499 SMTVWYKMQSVSVYTNGTVFATDTDITFTAVTKETIPLEFEWYFGE-------DPPVRTTSRSIKKrlsipqwYRVMVKA 571
Cdd:TIGR00864 1504 NVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDhctpifgGNTIFYTFRSVGT-------FNIIVTA 1576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    572 SNRMSSVVSEPHVIRVQK----KIVANRLTSPSSAL---------VNASVAFECWINFGTDVAYLW-----DFGDGTVSL 633
Cdd:TIGR00864 1577 ENDVGAAQASIFLFVLQEieglQILGETAEGGGGGVqeldgcyfeTNHTVQFHAGFKDGTNLSFSWnaildNEPDGPAFA 1656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    634 GSSSSSHVY-SREGEFTVEVLAFNNVSASTLRQQLFIVcEPCqpplvknmgpGKVQIWRS-QPVRLGVTFEAAVFCDISQ 711
Cdd:TIGR00864 1657 GSGKGAKLNpLEAGPCDIFLQAANLLGQATADCTIDFL-EPA----------GNLMLAASdNPAAVNALINLSAELAEGS 1725
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923084    712 GLSYTWNLMDSEGLPVSLPAAVDTHrQTLILPSHTLEYGN--YTALAKVQIEGSVVYSnycvGLEVRAQAPvsviseGTH 789
Cdd:TIGR00864 1726 GLQYRWFLEEGDDLETSEPFMSHSF-PSAGLHLVTMKAFNelGSANASEEVDVQEPIS----GLKIRAADA------GEQ 1794
                          410
                   ....*....|.
gi 19923084    790 LFFSRTTSSPI 800
Cdd:TIGR00864 1795 NFFAADSSVCF 1805
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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