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Conserved domains on  [gi|568983387|ref|XP_006517325|]
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short transient receptor potential channel 7 isoform X1 [Mus musculus]

Protein Classification

transient-receptor-potential channel protein( domain architecture ID 11489825)

transient-receptor-potential ion channel protein conducts cations such as calcium into cells; belongs to the Transient Receptor Family (TC. 1.A.4)

SCOP:  4000366
TCDB:  1.A.4

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
126-866 0e+00

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


:

Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 825.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  126 RGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQ-LAVGNEHLEVTELLLKKENLAR 204
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFvAAIENENLELTELLLNLSCRGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  205 VGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLspleqelrdddFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLL 284
Cdd:TIGR00870  81 VGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-----------ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  285 KGARIErphdYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDP--VLTALELSNELARLANIETEFKNDY 362
Cdd:TIGR00870 150 RGASVP----ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEY 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  363 RKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVN--LQVWSDHHRPSLSRIKLAIKYEVKK-------------------- 420
Cdd:TIGR00870 226 EELSCQMYNFALSLLDKLRDSKELEVILNHQGLtpLKLAAKEGRIVLFRLKLAIKYKQKKfvawpngqqllslywleeld 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  421 -----------------------------------LGQTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPnetf 465
Cdd:TIGR00870 306 gwrrkqsvlelivvfviglkfpelsdmyliaplsrLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRTDL---- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  466 tdypkqifRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAql 545
Cdd:TIGR00870 382 --------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQA-- 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  546 yvdqyvqdvtlhnvslppevayFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVK-DIF 624
Cdd:TIGR00870 452 ----------------------FLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDIL 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  625 KFMVIFIMVFVAFMIGMFNLYSYYRGAKYN--------------PAFTTVEESFKTLFWSIFGLSEVisvvLKYDHKFIE 690
Cdd:TIGR00870 510 RFLFIYAVVLFGFACGLNQLYQYYDELKLNecsnpharscekqgNAYSTLFETSQELFWAIIGLGDL----LANEHKFTE 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  691 NIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIK 770
Cdd:TIGR00870 586 FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIE 665
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  771 MCLIELCQSKAKRCENDLEMGMLNSKFRKTRyqagmrnsenltanstfsKPTRYQKIMKRLIKRYVLKAQVDRENDEVNE 850
Cdd:TIGR00870 666 KHDGKKRQRWCRRVEEVNWTTWERKAETLIE------------------DGLHYQRVMKRLIKRYVLAEQRPRDDEGTTE 727
                         810
                  ....*....|....*.
gi 568983387  851 GELKEIKQDISSLRYE 866
Cdd:TIGR00870 728 EETKELKQDISSLRFE 743
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
126-866 0e+00

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 825.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  126 RGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQ-LAVGNEHLEVTELLLKKENLAR 204
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFvAAIENENLELTELLLNLSCRGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  205 VGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLspleqelrdddFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLL 284
Cdd:TIGR00870  81 VGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-----------ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  285 KGARIErphdYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDP--VLTALELSNELARLANIETEFKNDY 362
Cdd:TIGR00870 150 RGASVP----ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEY 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  363 RKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVN--LQVWSDHHRPSLSRIKLAIKYEVKK-------------------- 420
Cdd:TIGR00870 226 EELSCQMYNFALSLLDKLRDSKELEVILNHQGLtpLKLAAKEGRIVLFRLKLAIKYKQKKfvawpngqqllslywleeld 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  421 -----------------------------------LGQTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPnetf 465
Cdd:TIGR00870 306 gwrrkqsvlelivvfviglkfpelsdmyliaplsrLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRTDL---- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  466 tdypkqifRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAql 545
Cdd:TIGR00870 382 --------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQA-- 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  546 yvdqyvqdvtlhnvslppevayFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVK-DIF 624
Cdd:TIGR00870 452 ----------------------FLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDIL 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  625 KFMVIFIMVFVAFMIGMFNLYSYYRGAKYN--------------PAFTTVEESFKTLFWSIFGLSEVisvvLKYDHKFIE 690
Cdd:TIGR00870 510 RFLFIYAVVLFGFACGLNQLYQYYDELKLNecsnpharscekqgNAYSTLFETSQELFWAIIGLGDL----LANEHKFTE 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  691 NIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIK 770
Cdd:TIGR00870 586 FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIE 665
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  771 MCLIELCQSKAKRCENDLEMGMLNSKFRKTRyqagmrnsenltanstfsKPTRYQKIMKRLIKRYVLKAQVDRENDEVNE 850
Cdd:TIGR00870 666 KHDGKKRQRWCRRVEEVNWTTWERKAETLIE------------------DGLHYQRVMKRLIKRYVLAEQRPRDDEGTTE 727
                         810
                  ....*....|....*.
gi 568983387  851 GELKEIKQDISSLRYE 866
Cdd:TIGR00870 728 EETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
297-355 6.30e-28

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 106.90  E-value: 6.30e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983387  297 CKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIE 355
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVE 59
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-290 4.95e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.75  E-value: 4.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 146 FLDSAEYGNIPVVRKMLEesKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKK----ENLARVGD-ALLLAISKGYVRI 220
Cdd:COG0666   91 LHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgadvNAQDNDGNtPLHLAAANGNLEI 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 221 VEAILSHPAfaqgqrltlspleqelrddDFYAYDEDGTrfshdiTPIILAAHCQEYEIVHILLLKGARIE 290
Cdd:COG0666  169 VKLLLEAGA-------------------DVNARDNDGE------TPLHLAAENGHLEIVKLLLEAGADVN 213
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
587-727 8.99e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 53.02  E-value: 8.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  587 LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAF-MIG--MFNLYSyyrgakynPAFTTVEES 663
Cdd:PLN03223 1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYaFIGhvIFGNAS--------VHFSDMTDS 1365
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568983387  664 FKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDA 727
Cdd:PLN03223 1366 INSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFGEVKANA 1429
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
589-732 2.64e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 589 AIAVVLSFSRIAYILPANESFGPLQISLGRTV-KDIFKFMVIFIMVFVAFMIGMFNLYsYYRGAKYNPAFTtveeSFKTL 667
Cdd:cd22192  427 SLALVLGWCNVMYFARGFQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIF-QTEDPDSLGHFY----DFPMT 501
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568983387 668 FWSIFGLS-EVISVVLKYDHKfIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWK 732
Cdd:cd22192  502 LFSTFELFlGLIDGPANYTVD-LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
126-866 0e+00

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 825.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  126 RGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQ-LAVGNEHLEVTELLLKKENLAR 204
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFvAAIENENLELTELLLNLSCRGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  205 VGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLspleqelrdddFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLL 284
Cdd:TIGR00870  81 VGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-----------ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  285 KGARIErphdYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDP--VLTALELSNELARLANIETEFKNDY 362
Cdd:TIGR00870 150 RGASVP----ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEY 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  363 RKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVN--LQVWSDHHRPSLSRIKLAIKYEVKK-------------------- 420
Cdd:TIGR00870 226 EELSCQMYNFALSLLDKLRDSKELEVILNHQGLtpLKLAAKEGRIVLFRLKLAIKYKQKKfvawpngqqllslywleeld 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  421 -----------------------------------LGQTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPnetf 465
Cdd:TIGR00870 306 gwrrkqsvlelivvfviglkfpelsdmyliaplsrLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRTDL---- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  466 tdypkqifRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAql 545
Cdd:TIGR00870 382 --------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQA-- 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  546 yvdqyvqdvtlhnvslppevayFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVK-DIF 624
Cdd:TIGR00870 452 ----------------------FLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDIL 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  625 KFMVIFIMVFVAFMIGMFNLYSYYRGAKYN--------------PAFTTVEESFKTLFWSIFGLSEVisvvLKYDHKFIE 690
Cdd:TIGR00870 510 RFLFIYAVVLFGFACGLNQLYQYYDELKLNecsnpharscekqgNAYSTLFETSQELFWAIIGLGDL----LANEHKFTE 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  691 NIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIK 770
Cdd:TIGR00870 586 FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIE 665
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  771 MCLIELCQSKAKRCENDLEMGMLNSKFRKTRyqagmrnsenltanstfsKPTRYQKIMKRLIKRYVLKAQVDRENDEVNE 850
Cdd:TIGR00870 666 KHDGKKRQRWCRRVEEVNWTTWERKAETLIE------------------DGLHYQRVMKRLIKRYVLAEQRPRDDEGTTE 727
                         810
                  ....*....|....*.
gi 568983387  851 GELKEIKQDISSLRYE 866
Cdd:TIGR00870 728 EETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
297-355 6.30e-28

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 106.90  E-value: 6.30e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983387  297 CKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIE 355
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVE 59
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
481-728 1.62e-18

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 85.78  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  481 SWTEMLIMKWVLGMIWSECKEIWEEgPREYVLHLWNLLDFGMLSIFVASFTARFMAFlkaseaqlyvdqyvqdvtlhnvs 560
Cdd:pfam00520   2 RYFELFILLLILLNTIFLALETYFQ-PEEPLTTVLEILDYVFTGIFTLEMLLKIIAA----------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  561 lPPEVAYFtyaRDKWW--------PSDPQIISEGLYAIAV--VLSFSRIAYILPANESFGPLQI---SLGRTVKDIFKFM 627
Cdd:pfam00520  58 -GFKKRYF---RSPWNildfvvvlPSLISLVLSSVGSLSGlrVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  628 VIFIMVFVAFMIGMFNLYSYYRGAKYNPA-----FTTVEESFKTLFWSIF--GLSEVISVVLKYDHKFIeniGYVLYGVY 700
Cdd:pfam00520 134 LLLLLFLFIFAIIGYQLFGGKLKTWENPDngrtnFDNFPNAFLWLFQTMTteGWGDIMYDTIDGKGEFW---AYIYFVSF 210
                         250       260
                  ....*....|....*....|....*...
gi 568983387  701 NVTMVVVLLNMLIAMINNSYQEIEEDAD 728
Cdd:pfam00520 211 IILGGFLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-290 4.95e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.75  E-value: 4.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 146 FLDSAEYGNIPVVRKMLEesKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKK----ENLARVGD-ALLLAISKGYVRI 220
Cdd:COG0666   91 LHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgadvNAQDNDGNtPLHLAAANGNLEI 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 221 VEAILSHPAfaqgqrltlspleqelrddDFYAYDEDGTrfshdiTPIILAAHCQEYEIVHILLLKGARIE 290
Cdd:COG0666  169 VKLLLEAGA-------------------DVNARDNDGE------TPLHLAAENGHLEIVKLLLEAGADVN 213
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
478-723 9.53e-12

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 65.76  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  478 TQFSWTEMLIMKWVLGMI----WSECKEIWEEGPReYVLHLWNLLDFGMLSIFVASFTARFM-AFLKASEAQLYVDQYVQ 552
Cdd:pfam08016   4 TNRSLFILLCEIVFVVFFlyfvVEEILKIRKHRPS-YLRSVWNLLDLAIVILSVVLIVLNIYrDFLADRLIKSVEASPVT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  553 DVTLHNVSlppevayftyardKWwpsdpQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIM 632
Cdd:pfam08016  83 FIDFDRVA-------------QL-----DNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  633 VFVAFMIGMFNLYSyyrgaKYNPAFTTVEESFKTLF---WSIFGLSEvisvvLKYDHKFIeniGYVLYGVYNVTMVVVLL 709
Cdd:pfam08016 145 FFFAYAQFGYLLFG-----TQAPNFSNFVKSILTLFrtiLGDFGYNE-----IFSGNRVL---GPLLFLTFVFLVIFILL 211
                         250
                  ....*....|....
gi 568983387  710 NMLIAMINNSYQEI 723
Cdd:pfam08016 212 NLFLAIINDSYVEV 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
150-229 1.35e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  150 AEYGNIPVVRKMLEESKtlNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGD---ALLLAISKGYVRIVEAILS 226
Cdd:pfam12796   5 AKNGNLELVKLLLENGA--DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgrtALHYAARSGHLEIVKLLLE 82

                  ...
gi 568983387  227 HPA 229
Cdd:pfam12796  83 KGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-289 1.39e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 150 AEYGNIPVVRKMLEesKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKK----ENLARVGD-ALLLAISKGYVRIVEAI 224
Cdd:COG0666  128 AYNGNLEIVKLLLE--AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgadvNARDNDGEtPLHLAAENGHLEIVKLL 205
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983387 225 LSHPAfaqgqrltlspleqelrddDFYAYDEDGtrfshdITPIILAAHCQEYEIVHILLLKGARI 289
Cdd:COG0666  206 LEAGA-------------------DVNAKDNDG------KTALDLAAENGNLEIVKLLLEAGADL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-291 2.84e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  181 LQLAVGNEHLEVTELLLKKENLARVGD-----ALLLAISKGYVRIVEAILSHPafaqgqrltlspleqelrdddfyayde 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDkngrtALHLAAKNGHLEIVKLLLEHA--------------------------- 53
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568983387  256 DGTRFSHDITPIILAAHCQEYEIVHILLLKGARIER 291
Cdd:pfam12796  54 DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-295 4.70e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  94 LRILLSMLGSNTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCV 173
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 174 DYMGQNALQLAVGNEHLEVTELLLKK-ENLARVGD----ALLLAISKGYVRIVEAILSHPAfaqgqrltlspleqelrdd 248
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAgADVNARDKdgetPLHLAAYNGNLEIVKLLLEAGA------------------- 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568983387 249 DFYAYDEDGTrfshdiTPIILAAHCQEYEIVHILLLKGARIERPHDY 295
Cdd:COG0666  145 DVNAQDNDGN------TPLHLAAANGNLEIVKLLLEAGADVNARDND 185
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
587-727 8.99e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 53.02  E-value: 8.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387  587 LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAF-MIG--MFNLYSyyrgakynPAFTTVEES 663
Cdd:PLN03223 1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYaFIGhvIFGNAS--------VHFSDMTDS 1365
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568983387  664 FKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDA 727
Cdd:PLN03223 1366 INSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFGEVKANA 1429
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
589-732 2.64e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 589 AIAVVLSFSRIAYILPANESFGPLQISLGRTV-KDIFKFMVIFIMVFVAFMIGMFNLYsYYRGAKYNPAFTtveeSFKTL 667
Cdd:cd22192  427 SLALVLGWCNVMYFARGFQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIF-QTEDPDSLGHFY----DFPMT 501
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568983387 668 FWSIFGLS-EVISVVLKYDHKfIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWK 732
Cdd:cd22192  502 LFSTFELFlGLIDGPANYTVD-LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-197 2.93e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568983387  150 AEYGNIPVVRKMLEesKTLNFNCVDYMGQNALQLAVGNEHLEVTELLL 197
Cdd:pfam13637   9 AASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
591-736 4.11e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 591 AVVLSFSRIAYILPANESFGPLQISLGRTV-KDIFKFMVIFIMVFVAFMIGmfnLYSYYRGAKYN--PAFTTVEESFKTL 667
Cdd:cd21882  414 SLVLGWCNVLYYTRGFQMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASA---FVILFQTEDPNklGEFRDYPDALLEL 490
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983387 668 FWSIFGLSEvISVVLKYDHKFIENIgyvLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARA 736
Cdd:cd21882  491 FKFTIGMGD-LPFNENVDFPFVYLI---LLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQKA 555
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
621-759 3.71e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983387 621 KDIFKFMVIFIMVFVAFMIGmfnLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISvvlkyDHKFIENIGY-----V 695
Cdd:cd22193  450 RDLLRFLFVYLLFLFGFAVA---LVSLIEKCSSDKKDCSSYGSFSDAVLELFKLTIGMG-----DLEFQENSTYpavflI 521
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983387 696 LYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWL-----------SYFDEGRTLPAPFNLVPSP 759
Cdd:cd22193  522 LLLTYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQRAITILefeksfpecmrKAFRSGRLLKVGLCKDGTP 596
 
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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