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Conserved domains on  [gi|1907084854|ref|XP_036013024|]
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polycystin-1-like protein 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
1493-1611 1.49e-45

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.


The actual alignment was detected with superfamily member cd01752:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 160.90  E-value: 1.49e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1493 QLYAVVIDTGFRSPVRFTSKVFIVLCGENGCSETKELCCPEKPLFGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCW 1572
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907084854 1573 FISHVMVKELCSGQAWFFSAQCWLAVSKLGGHVLREFFC 1611
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
167-622 1.16e-22

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: 107.48  E-value: 1.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  167 QRGTVVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSVYTN-GTVFAANTNITFVAITEETIPLEFAWYFG- 244
Cdd:TIGR00864 1912 QPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCcAAGIATGEEKNFTANVQRGKPVAFAWTFDl 1991
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  245 ----ENPPVMTTSRSIRRRLSVPQWYRVKVKATSRIGSVvSEPHLIRVQKRIMANRLVS-TASALVNANVSFECRLNFGT 319
Cdd:TIGR00864 1992 hhlhGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE-NITLQLEAQDALMDAALQAgPQDCFTNKMAQFEAATSPKP 2070
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  320 D-VAYLWNFGD-----DTIElgsSSSSHVYSREGEFTVEVLAFNNVSSTTLRKQLFIVREPCQPPPVKNMGPAKVQIWRS 393
Cdd:TIGR00864 2071 NfMACHWDFGDgsagqDTDE---PRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRS 2147
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  394 QPLRLgvtfEAAILCN--ISQGLSYTWSFVSA-------------------EMTTVTLPTAVNTRRQTIMLPSYTLECGN 452
Cdd:TIGR00864 2148 QPNLL----EAHVDLKdcLRYGAEYLWEILRAascdndghfargalngatrSFPVIPLPAEVDVQRLQLSLPKLALAAGH 2223
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  453 YTAIAKVQIKGSMVYSNYCVGVEVRARAPVSVISEGTHIFISTATStfIILRGAQSYDPD-NPG--AALRYHWTCTAASS 529
Cdd:TIGR00864 2224 YCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNlDDDdqSLLHFHWACQASSK 2301
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  530 PRWPCfdNSTSYQVDTQAPAISFPAKWLsECCDQFLVTLTVSSRGQNSSqalmflSTRPDLAFRFVHISWVNFRDIS--- 606
Cdd:TIGR00864 2302 GEAGC--CALNFGLGGKGPTLGIPGEEL-AAGIEYTFKLSIGKAGMKEE------ATNQTVLIQSGHIPIVSLECVScka 2372
                          490       500
                   ....*....|....*....|.
gi 1907084854  607 -----VNWNEEVSLRAVCEDC 622
Cdd:TIGR00864 2373 qalyeVSQNSYVYLEGRCLNC 2393
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
2023-2198 1.71e-17

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: 83.24  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 2023 SLGDLSSTEDWWDWTLSTLLDELYPERTsaraWGAQPG-ALGGQCHLIGPPVVKLLKISAGTaCTPPRPFSELVEDVLPM 2101
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKT----PSGLPGsFIAYESLLLGVPRLRQLRVRNSS-CLVHDKFVREINECHAG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 2102 HSNDL-DLENQNVSPGGP---------------ETCGVKKESYMHS---------LGKTRHEAHAALTALRASKWIDHST 2156
Cdd:pfam20519   76 YSPPSeDRKLYSALPYKPvhygskywfiytppgLLMGYDHWGHLASypsggyvvlLPSSREESLKRLAYLQDNNWLDRGT 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907084854 2157 RAMSVHFTLYNPPTQLFTSVILGTECLPSGGLVPSFLVESFR 2198
Cdd:pfam20519  156 RAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVK 197
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
835-976 3.21e-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: 68.30  E-value: 3.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  835 GYTTSGIMGPAVTIKPFSLSSGKTYVLQASVASKHVLL-GKAQLYLTVNQAPQDMSCQVRPHHGMEAYTIFSVFCmSGKP 913
Cdd:pfam02010  261 SQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVsGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTC-QGWT 339
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907084854  914 DFH----YEF---RYRIGNTSSHTLYRG-QDTQHYFLLPAGDSSDNYKVIVSTEITDGHGSKVQ-PCTVAVT 976
Cdd:pfam02010  340 DDDlpltYQFgdiSFREASEEWFLLYEGsSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATSvSLTITVT 411
GPS super family cl02559
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
1387-1425 3.33e-03

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


The actual alignment was detected with superfamily member smart00303:

Pssm-ID: 470616  Cd Length: 49  Bit Score: 37.75  E-value: 3.33e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1907084854  1387 QCVFWDKT--EWRSEGPYPQPGSSPEkVNCSYHHLAPVSVL 1425
Cdd:smart00303    4 ICVFWDESsgEWSTRGCELLETNGTH-TTCSCNHLTTFAVL 43
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1493-1611 1.49e-45

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: 160.90  E-value: 1.49e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1493 QLYAVVIDTGFRSPVRFTSKVFIVLCGENGCSETKELCCPEKPLFGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCW 1572
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907084854 1573 FISHVMVKELCSGQAWFFSAQCWLAVSKLGGHVLREFFC 1611
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
167-622 1.16e-22

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: 107.48  E-value: 1.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  167 QRGTVVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSVYTN-GTVFAANTNITFVAITEETIPLEFAWYFG- 244
Cdd:TIGR00864 1912 QPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCcAAGIATGEEKNFTANVQRGKPVAFAWTFDl 1991
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  245 ----ENPPVMTTSRSIRRRLSVPQWYRVKVKATSRIGSVvSEPHLIRVQKRIMANRLVS-TASALVNANVSFECRLNFGT 319
Cdd:TIGR00864 1992 hhlhGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE-NITLQLEAQDALMDAALQAgPQDCFTNKMAQFEAATSPKP 2070
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  320 D-VAYLWNFGD-----DTIElgsSSSSHVYSREGEFTVEVLAFNNVSSTTLRKQLFIVREPCQPPPVKNMGPAKVQIWRS 393
Cdd:TIGR00864 2071 NfMACHWDFGDgsagqDTDE---PRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRS 2147
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  394 QPLRLgvtfEAAILCN--ISQGLSYTWSFVSA-------------------EMTTVTLPTAVNTRRQTIMLPSYTLECGN 452
Cdd:TIGR00864 2148 QPNLL----EAHVDLKdcLRYGAEYLWEILRAascdndghfargalngatrSFPVIPLPAEVDVQRLQLSLPKLALAAGH 2223
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  453 YTAIAKVQIKGSMVYSNYCVGVEVRARAPVSVISEGTHIFISTATStfIILRGAQSYDPD-NPG--AALRYHWTCTAASS 529
Cdd:TIGR00864 2224 YCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNlDDDdqSLLHFHWACQASSK 2301
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  530 PRWPCfdNSTSYQVDTQAPAISFPAKWLsECCDQFLVTLTVSSRGQNSSqalmflSTRPDLAFRFVHISWVNFRDIS--- 606
Cdd:TIGR00864 2302 GEAGC--CALNFGLGGKGPTLGIPGEEL-AAGIEYTFKLSIGKAGMKEE------ATNQTVLIQSGHIPIVSLECVScka 2372
                          490       500
                   ....*....|....*....|.
gi 1907084854  607 -----VNWNEEVSLRAVCEDC 622
Cdd:TIGR00864 2373 qalyeVSQNSYVYLEGRCLNC 2393
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
2023-2198 1.71e-17

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: 83.24  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 2023 SLGDLSSTEDWWDWTLSTLLDELYPERTsaraWGAQPG-ALGGQCHLIGPPVVKLLKISAGTaCTPPRPFSELVEDVLPM 2101
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKT----PSGLPGsFIAYESLLLGVPRLRQLRVRNSS-CLVHDKFVREINECHAG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 2102 HSNDL-DLENQNVSPGGP---------------ETCGVKKESYMHS---------LGKTRHEAHAALTALRASKWIDHST 2156
Cdd:pfam20519   76 YSPPSeDRKLYSALPYKPvhygskywfiytppgLLMGYDHWGHLASypsggyvvlLPSSREESLKRLAYLQDNNWLDRGT 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907084854 2157 RAMSVHFTLYNPPTQLFTSVILGTECLPSGGLVPSFLVESFR 2198
Cdd:pfam20519  156 RAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVK 197
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
1495-1610 6.06e-12

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: 64.37  E-value: 6.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1495 YAVVIDTGFRSPVRFTSKVFIVLCGENGCSETKELCCPEKPlFGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCWFI 1574
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD-FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFL 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907084854 1575 SHVMV-KELCSGQAWFFSAQCWLAVSKLGGHvLREFF 1610
Cdd:pfam01477   80 KSITVeVPGETGGKYTFPCNSWVYGSKKYKE-TRVFF 115
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
835-976 3.21e-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: 68.30  E-value: 3.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  835 GYTTSGIMGPAVTIKPFSLSSGKTYVLQASVASKHVLL-GKAQLYLTVNQAPQDMSCQVRPHHGMEAYTIFSVFCmSGKP 913
Cdd:pfam02010  261 SQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVsGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTC-QGWT 339
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907084854  914 DFH----YEF---RYRIGNTSSHTLYRG-QDTQHYFLLPAGDSSDNYKVIVSTEITDGHGSKVQ-PCTVAVT 976
Cdd:pfam02010  340 DDDlpltYQFgdiSFREASEEWFLLYEGsSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATSvSLTITVT 411
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
416-632 8.11e-10

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: 63.67  E-value: 8.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  416 YTWSF--VSAEMTTVTLPTAVNTRRQTIMLPSYTLECGNYTAIAKVQI-KGSMVYSNYCVGVEVRARAPVSVISEGTHIF 492
Cdd:pfam02010   16 YLWSVftVSSNLNLQTISSPKDLVLPQLTIPSGTLPYGTYVFTLTVSLsSTPSLAGTDIITVTVQPSPLVAVIDGGSSRV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  493 ISTATStfIILRGAQSYDPDNPG---AALRYHWTCTAASSPRWPCFdNSTSYQVDTQA---------PAISFPAKWLSEc 560
Cdd:pfam02010   96 VGYNQD--LTLDGSESYDPDVDPgssSGLTYLWSCRRSSSGDNPLL-NNDPVCFSDQNegtllqstsSSLTIPASTLQA- 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907084854  561 cDQ-FLVTLTVSSRGQNSSQALMFLSTRPDLAFRfVHISWVNFRDISVNWNEEVSLRAV-CEDCG-DVPDLTYSW 632
Cdd:pfam02010  172 -NVtYTFKLTVSKGSRNSASTTQTILVVDGNPPI-IILSCISNCNRKNNPVDRLVLLAStCLNCSsDLSDVTYRW 244
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
298-371 4.41e-08

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: 52.45  E-value: 4.41e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907084854   298 VSTASALVNANVSFECR-LNFGTDVAYLWNFGDDTIELGSSSSsHVYSREGEFTVEVLAFNNVSSTTLRKQLFIV 371
Cdd:smart00089    6 ASPTVGVAGESVTFTATsSDDGSIVSYTWDFGDGTSSTGPTVT-HTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
303-371 1.77e-07

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: 50.57  E-value: 1.77e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907084854  303 ALVNANVSFEC-RLNFGTDVAYLWNFGDDTIEL-GSSSSSHVYSREGEFTVEVLAFNNVSSTTLRKQLFIV 371
Cdd:cd00146     11 AELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSsGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1492-1596 1.49e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 43.01  E-value: 1.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  1492 YQLYAVVIDTGFRSpvrFTSKVFIVLCGENGCSETKELCCPEKPLFGRNSRHTFILSIPNQLGPLQKIRLWHDssGSSPC 1571
Cdd:smart00308    3 YKVTVTTGGLDFAG---TTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNE--HRHPE 77
                            90       100
                    ....*....|....*....|....*
gi 1907084854  1572 WFISHVMVKELCSGQAWFFSAQCWL 1596
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWV 102
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
1387-1425 3.33e-03

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 37.75  E-value: 3.33e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1907084854  1387 QCVFWDKT--EWRSEGPYPQPGSSPEkVNCSYHHLAPVSVL 1425
Cdd:smart00303    4 ICVFWDESsgEWSTRGCELLETNGTH-TTCSCNHLTTFAVL 43
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
298-379 4.73e-03

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 41.96  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  298 VSTASALVNANVSFECrLNFGTDVAYLWNFGDDTIELGSSSSsHVYSREGEFTVEVLAFNNVSSTTLRKQLFIVREPCQP 377
Cdd:COG3291      3 ATPTSGCAPLTVQFTD-TSSGNATSYEWDFGDGTTSTEANPS-HTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAPNPG 80

                   ..
gi 1907084854  378 PP 379
Cdd:COG3291     81 VT 82
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1493-1611 1.49e-45

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: 160.90  E-value: 1.49e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1493 QLYAVVIDTGFRSPVRFTSKVFIVLCGENGCSETKELCCPEKPLFGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCW 1572
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907084854 1573 FISHVMVKELCSGQAWFFSAQCWLAVSKLGGHVLREFFC 1611
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
167-622 1.16e-22

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: 107.48  E-value: 1.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  167 QRGTVVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSVYTN-GTVFAANTNITFVAITEETIPLEFAWYFG- 244
Cdd:TIGR00864 1912 QPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCcAAGIATGEEKNFTANVQRGKPVAFAWTFDl 1991
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  245 ----ENPPVMTTSRSIRRRLSVPQWYRVKVKATSRIGSVvSEPHLIRVQKRIMANRLVS-TASALVNANVSFECRLNFGT 319
Cdd:TIGR00864 1992 hhlhGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAE-NITLQLEAQDALMDAALQAgPQDCFTNKMAQFEAATSPKP 2070
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  320 D-VAYLWNFGD-----DTIElgsSSSSHVYSREGEFTVEVLAFNNVSSTTLRKQLFIVREPCQPPPVKNMGPAKVQIWRS 393
Cdd:TIGR00864 2071 NfMACHWDFGDgsagqDTDE---PRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRS 2147
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  394 QPLRLgvtfEAAILCN--ISQGLSYTWSFVSA-------------------EMTTVTLPTAVNTRRQTIMLPSYTLECGN 452
Cdd:TIGR00864 2148 QPNLL----EAHVDLKdcLRYGAEYLWEILRAascdndghfargalngatrSFPVIPLPAEVDVQRLQLSLPKLALAAGH 2223
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  453 YTAIAKVQIKGSMVYSNYCVGVEVRARAPVSVISEGTHIFISTATStfIILRGAQSYDPD-NPG--AALRYHWTCTAASS 529
Cdd:TIGR00864 2224 YCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNlDDDdqSLLHFHWACQASSK 2301
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  530 PRWPCfdNSTSYQVDTQAPAISFPAKWLsECCDQFLVTLTVSSRGQNSSqalmflSTRPDLAFRFVHISWVNFRDIS--- 606
Cdd:TIGR00864 2302 GEAGC--CALNFGLGGKGPTLGIPGEEL-AAGIEYTFKLSIGKAGMKEE------ATNQTVLIQSGHIPIVSLECVScka 2372
                          490       500
                   ....*....|....*....|.
gi 1907084854  607 -----VNWNEEVSLRAVCEDC 622
Cdd:TIGR00864 2373 qalyeVSQNSYVYLEGRCLNC 2393
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
1495-1611 1.42e-22

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: 94.93  E-value: 1.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1495 YAVVIDTGFRSPVRFTSKVFIVLCGENGCSETKELCCPEKP-LFGRNSRHTFILSIPNqLGPLQKIRLWHDSSGSSPCWF 1573
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKnKFERGQTDKFTVEAVD-LGKLKKIRIGHDNSGLGAGWF 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907084854 1574 ISHVMVKELCSGQAWFFSAQCWLAVSKLGGHVLREFFC 1611
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
2023-2198 1.71e-17

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: 83.24  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 2023 SLGDLSSTEDWWDWTLSTLLDELYPERTsaraWGAQPG-ALGGQCHLIGPPVVKLLKISAGTaCTPPRPFSELVEDVLPM 2101
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKT----PSGLPGsFIAYESLLLGVPRLRQLRVRNSS-CLVHDKFVREINECHAG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 2102 HSNDL-DLENQNVSPGGP---------------ETCGVKKESYMHS---------LGKTRHEAHAALTALRASKWIDHST 2156
Cdd:pfam20519   76 YSPPSeDRKLYSALPYKPvhygskywfiytppgLLMGYDHWGHLASypsggyvvlLPSSREESLKRLAYLQDNNWLDRGT 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907084854 2157 RAMSVHFTLYNPPTQLFTSVILGTECLPSGGLVPSFLVESFR 2198
Cdd:pfam20519  156 RAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVK 197
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
1495-1610 3.21e-13

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: 68.13  E-value: 3.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1495 YAVVIDTGFRSPVRFTSKVFIVLCGENGcsETKELCCPEKPL-FGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCWF 1573
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENG--NSSDIPILDGPGsFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907084854 1574 ISHVMVKELCSGQAWFFSAQCWLAVSKLgGHVLREFF 1610
Cdd:cd00113     81 CESITVQALGTKKVYTFPVNRWVLGGKW-YTSVRSLK 116
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
1495-1610 6.06e-12

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: 64.37  E-value: 6.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1495 YAVVIDTGFRSPVRFTSKVFIVLCGENGCSETKELCCPEKPlFGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCWFI 1574
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD-FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFL 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907084854 1575 SHVMV-KELCSGQAWFFSAQCWLAVSKLGGHvLREFF 1610
Cdd:pfam01477   80 KSITVeVPGETGGKYTFPCNSWVYGSKKYKE-TRVFF 115
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
835-976 3.21e-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: 68.30  E-value: 3.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  835 GYTTSGIMGPAVTIKPFSLSSGKTYVLQASVASKHVLL-GKAQLYLTVNQAPQDMSCQVRPHHGMEAYTIFSVFCmSGKP 913
Cdd:pfam02010  261 SQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVsGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTC-QGWT 339
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907084854  914 DFH----YEF---RYRIGNTSSHTLYRG-QDTQHYFLLPAGDSSDNYKVIVSTEITDGHGSKVQ-PCTVAVT 976
Cdd:pfam02010  340 DDDlpltYQFgdiSFREASEEWFLLYEGsSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATSvSLTITVT 411
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
73-504 4.76e-10

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: 65.87  E-value: 4.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854   73 VASGTALCLLLDFGDncGAQMRLCTLAGATTVTGYHQYRKEGVYELKavvhdfhRAEELGPYYVD-------ISHGNVSV 145
Cdd:TIGR00864 1453 FGRARNASYLWDFGD--GGLLEGPEILHAFNSPGDFNIRLAAANEVG-------KNEATLNVAVKarvrgltINASLTNV 1523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  146 FMNSSsIHDSEALSFADSL-----------PQQRGTVVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSV-- 212
Cdd:TIGR00864 1524 PLNGS-VHFEAHLDAGDDVrfswilcdhctPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQIlg 1602
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  213 -----------YTNGTVFAANTNITFVAITEETIPLEFAW-----YFGENPPVMTTSRSIRRRLSVPQWYRVKVKATSRI 276
Cdd:TIGR00864 1603 etaegggggvqELDGCYFETNHTVQFHAGFKDGTNLSFSWnaildNEPDGPAFAGSGKGAKLNPLEAGPCDIFLQAANLL 1682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  277 GSVVSEPHLIRVQKRIMANRLVSTASALVNANVSFECRLNFGTDVAYLWNF-GDDTIELGSSSSSHVYSREGEFTVEVLA 355
Cdd:TIGR00864 1683 GQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLeEGDDLETSEPFMSHSFPSAGLHLVTMKA 1762
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  356 FNNVSSTTlRKQLFIVREPCQPPPVKNMGPAKVQIWrsqPLRLGVTFEAailcNISQGLSYTWSFVSAEMTTVTLPTAvn 435
Cdd:TIGR00864 1763 FNELGSAN-ASEEVDVQEPISGLKIRAADAGEQNFF---AADSSVCFQG----ELATGTNVSWCWAIDGGSSKMGKHA-- 1832
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907084854  436 trrqTIMLP-----SYTLECGNytAIAKVQIKGSMVYSNYCVGVEVRARAPVSVISEGTHIFISTATSTFIILR 504
Cdd:TIGR00864 1833 ----CMTFPdagtfAIRLNASN--AVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFR 1900
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
416-632 8.11e-10

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: 63.67  E-value: 8.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  416 YTWSF--VSAEMTTVTLPTAVNTRRQTIMLPSYTLECGNYTAIAKVQI-KGSMVYSNYCVGVEVRARAPVSVISEGTHIF 492
Cdd:pfam02010   16 YLWSVftVSSNLNLQTISSPKDLVLPQLTIPSGTLPYGTYVFTLTVSLsSTPSLAGTDIITVTVQPSPLVAVIDGGSSRV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  493 ISTATStfIILRGAQSYDPDNPG---AALRYHWTCTAASSPRWPCFdNSTSYQVDTQA---------PAISFPAKWLSEc 560
Cdd:pfam02010   96 VGYNQD--LTLDGSESYDPDVDPgssSGLTYLWSCRRSSSGDNPLL-NNDPVCFSDQNegtllqstsSSLTIPASTLQA- 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907084854  561 cDQ-FLVTLTVSSRGQNSSQALMFLSTRPDLAFRfVHISWVNFRDISVNWNEEVSLRAV-CEDCG-DVPDLTYSW 632
Cdd:pfam02010  172 -NVtYTFKLTVSKGSRNSASTTQTILVVDGNPPI-IILSCISNCNRKNNPVDRLVLLAStCLNCSsDLSDVTYRW 244
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
300-364 1.14e-09

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: 56.63  E-value: 1.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907084854  300 TASALV---NANVSFECRLNFGTDVAYLWNFGDDTIE-LGSSSSSHVYSREGEFTVEVLAFNNVSSTTL 364
Cdd:pfam00801    2 SASGTVvaaGQPVTFTATLADGSNVTYTWDFGDSPGTsGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
298-371 4.41e-08

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: 52.45  E-value: 4.41e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907084854   298 VSTASALVNANVSFECR-LNFGTDVAYLWNFGDDTIELGSSSSsHVYSREGEFTVEVLAFNNVSSTTLRKQLFIV 371
Cdd:smart00089    6 ASPTVGVAGESVTFTATsSDDGSIVSYTWDFGDGTSSTGPTVT-HTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
303-371 1.77e-07

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: 50.57  E-value: 1.77e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907084854  303 ALVNANVSFEC-RLNFGTDVAYLWNFGDDTIEL-GSSSSSHVYSREGEFTVEVLAFNNVSSTTLRKQLFIV 371
Cdd:cd00146     11 AELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSsGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
159-360 1.80e-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: 57.40  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  159 SFADSLPQQ--RGT-VVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSVYTNGTVFAANTNITFVAITEETI 235
Cdd:TIGR00864 1290 SFGDGSPNEthHGCpGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQFQACAEPEF 1369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  236 PLEFAWYFG--ENPPVMTTSRSIRRRLSVPQWYRVKVKATSRIgSVVSEPHLIRVQKRIMANRLVSTASALVNANVS--- 310
Cdd:TIGR00864 1370 NYRYEWDFGgeEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNI-SAANDSALIEVLEPVGATSFKHNGSHGNNLELGqpy 1448
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907084854  311 FECRLNFGTDVAYLWNFGDDTIeLGSSSSSHVYSREGEFTVEVLAFNNVS 360
Cdd:TIGR00864 1449 LFSAFGRARNASYLWDFGDGGL-LEGPEILHAFNSPGDFNIRLAAANEVG 1497
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
168-533 4.04e-06

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: 52.78  E-value: 4.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  168 RGTVVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSVYTNGTVFAANTNITFVAITEETIPLEFAWYFGE-- 245
Cdd:TIGR00864 1472 EGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDhc 1551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  246 -----NPPVMTTSRSIRRrlsvpqwYRVKVKATSRIGSVVSEPHLIRVQKRIMANRLVSTASAL-------------VNA 307
Cdd:TIGR00864 1552 tpifgGNTIFYTFRSVGT-------FNIIVTAENDVGAAQASIFLFVLQEIEGLQILGETAEGGgggvqeldgcyfeTNH 1624
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  308 NVSFECRLNFGTDVAYLW-----NFGDDTIELGSSSSSHVY-SREGEFTVEVLAFNNVSSTTLRKQLFIVRepcqppPVK 381
Cdd:TIGR00864 1625 TVQFHAGFKDGTNLSFSWnaildNEPDGPAFAGSGKGAKLNpLEAGPCDIFLQAANLLGQATADCTIDFLE------PAG 1698
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  382 NMgpaKVQIwRSQPLRLGVTFEAAILCNISQGLSYTWSF-------VSAEMTTVTLPTAvnTRRQTIMLPSYTLECGNYT 454
Cdd:TIGR00864 1699 NL---MLAA-SDNPAAVNALINLSAELAEGSGLQYRWFLeegddleTSEPFMSHSFPSA--GLHLVTMKAFNELGSANAS 1772
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907084854  455 AIAKVQIKGSmvysnycvGVEVRARAPvsviseGTHIFISTATStfIILRGAQSydpdnPGAALRYHWTCTAASSPRWP 533
Cdd:TIGR00864 1773 EEVDVQEPIS--------GLKIRAADA------GEQNFFAADSS--VCFQGELA-----TGTNVSWCWAIDGGSSKMGK 1830
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
1512-1608 1.26e-05

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 46.53  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1512 KVFIVLCGENGCSETKELCCPEKPlFGRNSRHTFILSIPNQLGPLQKIRLWHDSSGSSPCWFISHVMVKELCSGQAWFfs 1591
Cdd:cd01753     20 YIYLTLVGTAGESEKQLLDRPGYD-FERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDAWFCNYITVTGPGGDEYHF-- 96
                           90
                   ....*....|....*..
gi 1907084854 1592 aQCWLAVSKLGGHVLRE 1608
Cdd:cd01753     97 -PCYRWIEGYGTLELRE 112
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
212-281 1.57e-05

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: 44.68  E-value: 1.57e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  212 VYTNGTVFAANTNITFVAITEETIPLEFAWYFGENPPVMTTSRSIRRRLSVPQWYRVKVKATSRIGSVVS 281
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
172-444 9.18e-05

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: 48.15  E-value: 9.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  172 VVHCFSSISSYNVSFISQTQVASGQAWCGVTVGYKMQSVSVYTNGTVFAANTNITFVAiteETIP----LEFAWYFGENP 247
Cdd:TIGR00864 1052 VMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEA---HPLPspggIHYEWDFGDGS 1128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  248 PVMTTSR-SIRRRLSVPQWYRVKVKATSRIGSVVSEPHlIRVQKRIMANRLVSTASALVNANVSFECRLNFGTDVAYLWN 326
Cdd:TIGR00864 1129 ALLQGRQpAAAHTFAKRGPFHVCLEVNNTISGAAACAD-MFAFEEIEGLSADMSLATELGAATTVRAALQSGDNITWTFD 1207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  327 FGDDTI-ELGSSSSSHVYSREGEFTVEVLAFNNVSS--TTLRKQLFIVR----EP--CQPppvknmgpakvqiwrSQPLr 397
Cdd:TIGR00864 1208 MGDGKSlSGPEATVEHKYAKAGNCTVNIGAANAAGHgaRIIHVEVFVFEvagiEPaaCIG---------------EHAD- 1271
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907084854  398 lgVTFEAAILCNISQGLsYTWSF--VSAEMTTVTLPTAVNTRRQTIMLP 444
Cdd:TIGR00864 1272 --ANFRARVSGNAAHYL-FDWSFgdGSPNETHHGCPGISHNFRGNGTFP 1317
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1492-1596 1.49e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 43.01  E-value: 1.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  1492 YQLYAVVIDTGFRSpvrFTSKVFIVLCGENGCSETKELCCPEKPLFGRNSRHTFILSIPNQLGPLQKIRLWHDssGSSPC 1571
Cdd:smart00308    3 YKVTVTTGGLDFAG---TTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNE--HRHPE 77
                            90       100
                    ....*....|....*....|....*
gi 1907084854  1572 WFISHVMVKELCSGQAWFFSAQCWL 1596
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWV 102
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
151-433 3.00e-04

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: 46.61  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  151 SIHDSEALSFADslpqqrgTVVVHCFSSISSYNVSFISQTQVASGQAWCGVTVGY--KMQSVSVYTNGTVFAANTNITFV 228
Cdd:TIGR00864  929 TIDDKPFFTFQN-------TVFNVIYQHAAVFKLSLTAMNHVSNLTEDFNVTVDRlnPMQGLQVKGVPAVLPPGATLALT 1001
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  229 A--ITEETIPLEFAWYFGE--------NPPVMTT-------------SRSIRRRLSVPQWYRVKVKATSRIGSVVSEphl 285
Cdd:TIGR00864 1002 AgvLIDMAVEAAFLWSFGDgeqalfefKPPYNESfpcpdpspaqvllEHNVMHIYAAPGEYLATVLASNAFENISQQ--- 1078
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  286 IRVQKRIMANRL---VSTASALVNANVSFECR-LNFGTDVAYLWNFGDDTIEL--GSSSSSHVYSREGEFTVEVLAFNNV 359
Cdd:TIGR00864 1079 INMSVRAILPRVaigTEDGLLLAGKPADFEAHpLPSPGGIHYEWDFGDGSALLqgRQPAAAHTFAKRGPFHVCLEVNNTI 1158
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907084854  360 SSTTLRKQLFIVREPcqpppvknmgpAKVQIWRSQPLRLG--VTFEAAIlcniSQGLSYTWSFVSAEMTTVTLPTA 433
Cdd:TIGR00864 1159 SGAAACADMFAFEEI-----------EGLSADMSLATELGaaTTVRAAL----QSGDNITWTFDMGDGKSLSGPEA 1219
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
1494-1596 2.31e-03

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: 40.21  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854 1494 LYAVVIDTGF-RSPVRFTSKVFIVLCGENGcsETKELCCPEKPLfgrnsrhTFILSIPNqLGPLQKIRLWHDSSGSSPCW 1572
Cdd:cd01757      2 PYHVVIVPSKkLGGSMFTANPWICVSGELG--ETPPLQIPKNSL-------EMTFDCQN-LGKLTTVQIGHDNSGLLAKW 71
                           90       100
                   ....*....|....*....|....
gi 1907084854 1573 FISHVMVKELCSGQAWFFSAQCWL 1596
Cdd:cd01757     72 LVEYVMVRNEITGHTYKFPCGRWL 95
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
1387-1425 3.33e-03

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 37.75  E-value: 3.33e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1907084854  1387 QCVFWDKT--EWRSEGPYPQPGSSPEkVNCSYHHLAPVSVL 1425
Cdd:smart00303    4 ICVFWDESsgEWSTRGCELLETNGTH-TTCSCNHLTTFAVL 43
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
298-379 4.73e-03

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 41.96  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907084854  298 VSTASALVNANVSFECrLNFGTDVAYLWNFGDDTIELGSSSSsHVYSREGEFTVEVLAFNNVSSTTLRKQLFIVREPCQP 377
Cdd:COG3291      3 ATPTSGCAPLTVQFTD-TSSGNATSYEWDFGDGTTSTEANPS-HTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAPNPG 80

                   ..
gi 1907084854  378 PP 379
Cdd:COG3291     81 VT 82
 
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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