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Conserved domains on  [gi|932085572|gb|ALG40992|]
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NF-kappa B [Aulactinia veratra]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHD-n super family cl08275
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
73-298 1.11e-101

N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel).


The actual alignment was detected with superfamily member cd07883:

Pssm-ID: 447596  Cd Length: 197  Bit Score: 314.42  E-value: 1.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASgE 152
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCE-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRYTKMQELQNATmtalgatnndpstffgisGLNSHPTgilgten 232
Cdd:cd07883   80 GICTVQVGPKD-MTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNP------------------GDLVHVD------- 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kpFDKNFALTVADDEAKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07883  134 --AEGGGDRQLTDEEQAEIRQKAKQQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
306-408 5.46e-55

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


:

Pssm-ID: 465045  Cd Length: 102  Bit Score: 185.07  E-value: 5.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  306 KICRMDKNSGCVTGGDEVYLLCDRVQKEDIEVRFYEYDpeQGKQVWEDLGTFAPSDVHRQFAIVFKTPPYWNVAVEKPVK 385
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEED--DGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVT 78
                          90       100
                  ....*....|....*....|...
gi 932085572  386 VLCELRRKSDKETSEPMEFTYTP 408
Cdd:pfam16179  79 VNIQLRRPSDKATSEPQPFTYLP 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
495-788 7.46e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 7.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 495 EEMLRELKKEFALSILEHMSSAIRDYASTGDARYLLAIQRQVTAVQNDDGDTALHLAVINCQFNAIESLvsvmkDLPGSL 574
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL-----LAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 575 LDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKLrkeseefpEIHWQNY 654
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA--------DVNAQDN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 655 NGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLAAGL 734
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL-LEAGADVNAKDNDGKTALDLAAEN 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 932085572 735 GLEGLTALLVAAGADTMETNSEDETPYSLATTAEVKKILSDEDEVPAAADDIKI 788
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
 
Name Accession Description Interval E-value
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
73-298 1.11e-101

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light polypeptide gene enhancer in B-cells (NF-kappa B); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 and B2 families of transcription factors, also referred to as class I members of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. Family members include NF-kappa B1 and NF-kappa B2. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form), while NF-kappa B2 is called p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). p105 and p100 may also act as I-kappa Bs due to their C-terminal ankyrin repeats.


Pssm-ID: 143643  Cd Length: 197  Bit Score: 314.42  E-value: 1.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASgE 152
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCE-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRYTKMQELQNATmtalgatnndpstffgisGLNSHPTgilgten 232
Cdd:cd07883   80 GICTVQVGPKD-MTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNP------------------GDLVHVD------- 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kpFDKNFALTVADDEAKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07883  134 --AEGGGDRQLTDEEQAEIRQKAKQQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
75-297 2.15e-65

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 216.40  E-value: 2.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572   75 LEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNaSGEGI 154
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKD-CKDGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  155 VTVQIGPEqGMSASFPNLGIQHVTRKAVSKTLLSRYtkmqelqnatmtalgATNNDPstffgisglnshptgilgtenkp 234
Cdd:pfam00554  80 CEVELGPE-DMVASFQNLGIQCVKKKDVEEALKERI---------------ELNIDP----------------------- 120
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 932085572  235 fdknfaltvaddeaKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDS 297
Cdd:pfam00554 121 --------------FNVGFEALRQIKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
306-408 5.46e-55

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 185.07  E-value: 5.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  306 KICRMDKNSGCVTGGDEVYLLCDRVQKEDIEVRFYEYDpeQGKQVWEDLGTFAPSDVHRQFAIVFKTPPYWNVAVEKPVK 385
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEED--DGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVT 78
                          90       100
                  ....*....|....*....|...
gi 932085572  386 VLCELRRKSDKETSEPMEFTYTP 408
Cdd:pfam16179  79 VNIQLRRPSDKATSEPQPFTYLP 101
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
305-408 8.50e-54

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 181.75  E-value: 8.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 305 LKICRMDKNSGCVTGGDEVYLLCDRVQKEDIEVRFYEYDPEQGkqVWEDLGTFAPSDVHRQFAIVFKTPPYWNVAVEKPV 384
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEET--VWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPV 78
                         90       100
                 ....*....|....*....|....
gi 932085572 385 KVLCELRRKSDKETSEPMEFTYTP 408
Cdd:cd01177   79 KVKIQLKRPSDGERSESVPFTYVP 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
495-788 7.46e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 7.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 495 EEMLRELKKEFALSILEHMSSAIRDYASTGDARYLLAIQRQVTAVQNDDGDTALHLAVINCQFNAIESLvsvmkDLPGSL 574
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL-----LAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 575 LDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKLrkeseefpEIHWQNY 654
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA--------DVNAQDN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 655 NGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLAAGL 734
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL-LEAGADVNAKDNDGKTALDLAAEN 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 932085572 735 GLEGLTALLVAAGADTMETNSEDETPYSLATTAEVKKILSDEDEVPAAADDIKI 788
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
586-686 1.25e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  586 LHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKLRKEseefpeihwqNYNGFTPLHLAVI 665
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----------KDNGRTALHYAAR 70
                          90       100
                  ....*....|....*....|.
gi 932085572  666 KGNREIVKLLLSVGANVEAKD 686
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
544-764 1.52e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 544 GDTALHLAVincQFNAIESLVSVMKDLpGSLLDMYNYLRQTPLH--LAVLTKQPLATECLLRANASATTCDRHGNTPVHI 621
Cdd:PHA03095  83 GFTPLHLYL---YNATTLDVIKLLIKA-GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 622 -----ACaqgDIGCLKVLLNKKlrkeseefPEIHWQNYNGFTPLH--LAVIKGNREIVKLLLSVGANVEAKDgTCGRTPL 694
Cdd:PHA03095 159 llksrNA---NVELLRLLIDAG--------ADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 695 H-LAVENSNLAIAGFLILEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLA 764
Cdd:PHA03095 227 HsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
IPT smart00429
ig-like, plexins, transcription factors;
305-407 3.36e-12

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 63.21  E-value: 3.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572   305 LKICRMDKNSGCVTGGDEVyLLCDRVQKEDIEVRFYEydpeqgkQVWEDLGTFAPSdvhRQFAIVFKTPPYWNVAVEKPV 384
Cdd:smart00429   2 PVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-------GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPV 70
                           90       100
                   ....*....|....*....|...
gi 932085572   385 kvlCELRRKSDKETSEPMEFTYT 407
Cdd:smart00429  71 ---RTVGLRNGGVPSSPQPFTYV 90
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
544-745 1.16e-08

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: 58.94  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  544 GDTALHLAVINCQfNAIESLVSVMKDLPGslldmynylRQTPLHLAvltkqplatecllraNASATTCDRHGNTPVHIAC 623
Cdd:TIGR00870  82 GDTLLHAISLEYV-DAVEAILLHLLAAFR---------KSGPLELA---------------NDQYTSEFTPGITALHLAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  624 AQGDIGCLKVLLNKK----LRKESEEFPEIHWQN--YNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDgTCGRTPLHLA 697
Cdd:TIGR00870 137 HRQNYEIVKLLLERGasvpARACGDFFVKSQGVDsfYHGESPLNAAACLGSPSIVALLSEDPADILTAD-SLGNTLLHLL 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 932085572  698 V-------ENSNLAIA---GFLILEAKCDvDSY------NLDDNTPLHLAAGLGLEGLTALLVA 745
Cdd:TIGR00870 216 VmenefkaEYEELSCQmynFALSLLDKLR-DSKelevilNHQGLTPLKLAAKEGRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
544-677 3.71e-08

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: 56.94  E-value: 3.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 544 GDTALHLAVINCQFNAIESLVSVMKDL-------------PGSLLdmynYLRQTPLHLAVLTKQPLATECLLRANASATT 610
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgPKNLI----YYGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 611 CDRHGNTPVHIACAQG--DIGC--LKVLLNkkLRKESEEFPEIHWQNYNGFTPLHLAVIKGNREIVKLLLS 677
Cdd:cd22192  165 QDSLGNTVLHILVLQPnkTFACqmYDLILS--YDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
655-684 5.35e-07

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 46.43  E-value: 5.35e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 932085572   655 NGFTPLHLAVIKGNREIVKLLLSVGANVEA 684
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
73-298 1.11e-101

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light polypeptide gene enhancer in B-cells (NF-kappa B); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 and B2 families of transcription factors, also referred to as class I members of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. Family members include NF-kappa B1 and NF-kappa B2. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form), while NF-kappa B2 is called p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). p105 and p100 may also act as I-kappa Bs due to their C-terminal ankyrin repeats.


Pssm-ID: 143643  Cd Length: 197  Bit Score: 314.42  E-value: 1.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASgE 152
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCE-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRYTKMQELQNATmtalgatnndpstffgisGLNSHPTgilgten 232
Cdd:cd07883   80 GICTVQVGPKD-MTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNP------------------GDLVHVD------- 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kpFDKNFALTVADDEAKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07883  134 --AEGGGDRQLTDEEQAEIRQKAKQQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
75-297 2.15e-65

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 216.40  E-value: 2.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572   75 LEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNaSGEGI 154
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKD-CKDGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  155 VTVQIGPEqGMSASFPNLGIQHVTRKAVSKTLLSRYtkmqelqnatmtalgATNNDPstffgisglnshptgilgtenkp 234
Cdd:pfam00554  80 CEVELGPE-DMVASFQNLGIQCVKKKDVEEALKERI---------------ELNIDP----------------------- 120
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 932085572  235 fdknfaltvaddeaKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDS 297
Cdd:pfam00554 121 --------------FNVGFEALRQIKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
73-298 7.46e-64

N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel).


Pssm-ID: 143640  Cd Length: 174  Bit Score: 212.23  E-value: 7.46e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASGE 152
Cdd:cd07827    1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKTDCRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQGMSASFPNLGIQHVTRKAVSKTLLSRytkmqelqnatmtalGATNNDPstffgiSGLNSHPTGilgten 232
Cdd:cd07827   81 GVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQR---------------IQLGIDP------FMVHKGPEG------ 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kpfdknfaltvaddeakkirkmvddQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07827  134 -------------------------NASDIDLNRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
73-298 6.28e-57

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways.


Pssm-ID: 143651  Cd Length: 202  Bit Score: 194.34  E-value: 6.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASgE 152
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCE-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRytkmqelqnatMTALGATNNDPstffgisGLNSHPTgiLGTEN 232
Cdd:cd07935   80 GICTVTAGPKD-MVVGFANLGILHVTKKKVFETLEAR-----------MTEACKKGYNP-------GLLVHPE--LAYLQ 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 KPFDKNFALTvaDDEAKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07935  139 AEGGGDRQLT--EREKEIIRQAAVQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
73-298 6.07e-56

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B2 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B2 is commonly referred to as p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B2 is involved in the alternative NF-kappa B signaling pathway which is activated by few agonists and plays an important role in secondary lymphoid organogenesis, maturation of B-cells, and adaptive humoral immunity. p100 may also act as an I-kappa B due to its C-terminal ankyrin repeats.


Pssm-ID: 143650  Cd Length: 185  Bit Score: 190.88  E-value: 6.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASGE 152
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRyTKMQELQNATMTALgatnndpstffgisglnshptgilgten 232
Cdd:cd07934   81 GNCSVDVGPKD-MTAQFSNLGILHVTKKNMMEILKEK-LKRQKLRNTGPYKL---------------------------- 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kpfdknfaltvADDEAKKIRKMVDDQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07934  131 -----------TEAEERELEQEAKELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
306-408 5.46e-55

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 185.07  E-value: 5.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  306 KICRMDKNSGCVTGGDEVYLLCDRVQKEDIEVRFYEYDpeQGKQVWEDLGTFAPSDVHRQFAIVFKTPPYWNVAVEKPVK 385
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEED--DGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVT 78
                          90       100
                  ....*....|....*....|...
gi 932085572  386 VLCELRRKSDKETSEPMEFTYTP 408
Cdd:pfam16179  79 VNIQLRRPSDKATSEPQPFTYLP 101
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
305-408 8.50e-54

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 181.75  E-value: 8.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 305 LKICRMDKNSGCVTGGDEVYLLCDRVQKEDIEVRFYEYDPEQGkqVWEDLGTFAPSDVHRQFAIVFKTPPYWNVAVEKPV 384
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEET--VWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPV 78
                         90       100
                 ....*....|....*....|....
gi 932085572 385 KVLCELRRKSDKETSEPMEFTYTP 408
Cdd:cd01177   79 KVKIQLKRPSDGERSESVPFTYVP 102
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
73-298 9.96e-48

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Dorsal and Dif (Dorsal-related immunity factor), and similar proteins. Dorsal and Dif are Rel-like transcription factors, which play roles in mediating innate immunity in Drosophila. They are activated via the Toll pathway. Cytoplasmic Dorsal/Dif are inactivated via forming a complex with Cactus, the Drosophila homologue of mammalian I-kappa B proteins. In response to signals, Cactus is degraded and Dorsal/Dif can be transported into the nucleus, where they act as transcription factors. Dorsal is also an essential gene in establishing the proper dorsal/ventral polarity in the developing embryo.


Pssm-ID: 143647  Cd Length: 173  Bit Score: 167.66  E-value: 9.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASGE 152
Cdd:cd07887    1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEGCKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRYTKmqelqnatmtalgatNNDpstffgisglnshptgilgten 232
Cdd:cd07887   81 GVCTKKINPTE-MRIVFQKLGIQCVKKKDVEESLKLREEI---------------NVD---------------------- 122
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kPFDKNFaltvadDEAKKIrkmvddqaKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07887  123 -PFRTGF------DHKDQI--------NSIDLNVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
73-298 2.12e-46

N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the c-Rel family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). c-Rel plays an important role in B cell proliferation and survival.


Pssm-ID: 143649  Cd Length: 172  Bit Score: 163.89  E-value: 2.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASgE 152
Cdd:cd07933    1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCR-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQgMSASFPNLGIQHVTRKAVSKTLLSRYTKmqelqnatmtalgatnndpstffGISGLNSHPTGILGTEn 232
Cdd:cd07933   80 GYYEAEFGPER-RVLAFQNLGIQCVRRREVKEAIMLRISR-----------------------GINPFNVPEEQLLQIE- 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 kpfdknfaltvaddeakkirkmvddqakNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07933  135 ----------------------------EYDLNVVRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
305-408 8.12e-41

IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated Tcells (NFAT), and recombination signal J-kappa binding protein (RBP-Jkappa). The IPT domains in these proteins are involved in DNA binding. Most NF-kappaB/Rel proteins form homo- and heterodimers, while NFAT proteins are largely monomeric (with TonEBP being an exception). While the majority of sequence-specific DNA binding elements are found in the N-terminal domain, several are found in the IPT domain in loops adjacent to, and including, the linker region.


Pssm-ID: 238336  Cd Length: 101  Bit Score: 145.12  E-value: 8.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 305 LKICRMDKNSGCVTGGDEVYLLCDRVQKEDIEVRFYEYDPeqGKQVWEDLGTFAPSDVHrQFAIVFKTPPYWNVAVEKPV 384
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGP--GETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPV 77
                         90       100
                 ....*....|....*....|....
gi 932085572 385 KVLCELRRKSDKETSEPMEFTYTP 408
Cdd:cd00602   78 QVPIQLVRPDDRKRSEPLTFTYTP 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
495-788 7.46e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 7.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 495 EEMLRELKKEFALSILEHMSSAIRDYASTGDARYLLAIQRQVTAVQNDDGDTALHLAVINCQFNAIESLvsvmkDLPGSL 574
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL-----LAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 575 LDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKLrkeseefpEIHWQNY 654
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA--------DVNAQDN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 655 NGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLAAGL 734
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL-LEAGADVNAKDNDGKTALDLAAEN 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 932085572 735 GLEGLTALLVAAGADTMETNSEDETPYSLATTAEVKKILSDEDEVPAAADDIKI 788
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
73-298 1.06e-38

N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD domain of the RelA family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelA (also called p65) forms heterodimers with NF-kappa B1 (p50) and B2 (p52). RelA also forms homodimers.


Pssm-ID: 143645  Cd Length: 169  Bit Score: 141.55  E-value: 1.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHSLTGKNASgE 152
Cdd:cd07885    1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCK-D 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 153 GIVTVQIGPEQGMSaSFPNLGIQHVTRKAVSKTLLSRytkmqelqnatmtalgatnndpstffgisglnshptgiLGTEN 232
Cdd:cd07885   80 GYYEAELSPDRCIH-SFQNLGIQCVKKRDLEQAVSQR--------------------------------------IQTNN 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 932085572 233 KPFDknfaltVADDEakkirkmvddQAKNMNLSAVRLCFQAYLPDENGNFTkPLKPCISNPVYDSK 298
Cdd:cd07885  121 NPFN------VPIEE----------QRADYDLNAVRLCFQVTVRDPSGRLL-PLPPVLSQPIYDNR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
557-802 8.95e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 8.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 557 FNAIESLVSVMKDLPGSLLDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLN 636
Cdd:COG0666   29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 637 KKLrkeseefpEIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGFLiLEAKCD 716
Cdd:COG0666  109 AGA--------DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLL-LEAGAD 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 717 VDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLATTAEVKKILSDEDEVPAAADDIKIPEVEIKNM 796
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                 ....*.
gi 932085572 797 AAEVNA 802
Cdd:COG0666  259 AAAAGA 264
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
498-759 2.15e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 498 LRELKKEFALSILEHMSSAIRDYASTGDARYLLAIQRQVTAVQNDDGDTALHLAVINCQFNAIESLVSvmkdlPGSLLDM 577
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-----AGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 578 YNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKlrkeseefPEIHWQNYNGF 657
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG--------ADVNARDNDGE 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 658 TPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAgFLILEAKCDVDSYNLDDNTPLHLAAGLGLE 737
Cdd:COG0666  188 TPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
                        250       260
                 ....*....|....*....|..
gi 932085572 738 GLTALLVAAGADTMETNSEDET 759
Cdd:COG0666  266 LIVKLLLLALLLLAAALLDLLT 287
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
73-298 5.24e-31

N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral oncogene homolog B (RelB) protein; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the RelB family of transcription factors, categorized as class II NF-kappa B family members. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelB, is unable to homodimerize but is a potent transactivator in a heterodimer with NF-kappa B1 (p50) or B2 (p52). It is involved in the regulation of genes that play roles in inflammatory processes and the immune response.


Pssm-ID: 143646  Cd Length: 172  Bit Score: 119.58  E-value: 5.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRGFRFRYPCEGPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRI--VVSLVTEDEPYMPHAHSLTGKNAS 150
Cdd:cd07886    1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVtvTVCLVWKDPPHRVHPHGLVGKDCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 151 gEGIVTVQIGPEQGMSASFPNLGIQHVTRKAVSKTLlsrYTKMQElqnatmtalgatNNDPstfFGISGLNSHptgilgt 230
Cdd:cd07886   81 -NGICQVTLNPHSSPRHSFSNLGIQCVRKREIEAAI---ETRLQL------------NIDP---FKAGSLKNH------- 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 932085572 231 enkpfdknfaltvaddeakkirkmvddqaKNMNLSAVRLCFQAYLPDENGnFTKPLKPCISNPVYDSK 298
Cdd:cd07886  135 -----------------------------EEVDMNVVRLCFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
73-298 2.90e-27

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator.


Pssm-ID: 143644  Cd Length: 159  Bit Score: 108.67  E-value: 2.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRgFRFRYPCE-GPSHGGLPGQFSSPKNKSYPSVQLNNYHGLCRIVVSLVT-EDEPYMPHAHSLTGKNAS 150
Cdd:cd07884    1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQaDDNRRKPHVHKLVGKQGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 151 GE--GIVTVQIGPEQGMSASFPNLGIQHVTRKAVSKTLLsrytkmqelqnatmtalgatnndpstffgisglnshptgil 228
Cdd:cd07884   80 DDvcDPHDIEVSPEGDYVAMFQNMGIIHTAKKNIPEELY----------------------------------------- 118
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 229 gtenkpfdknfaltvaddeakkirkmvddQAKNMNLSAVRLCFQAYLPDENGNFTKPLKPCISNPVYDSK 298
Cdd:cd07884  119 -----------------------------KKKNMNLNQVVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
539-726 2.76e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 2.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 539 VQNDDGDTALHLAVINCQFNAIESLVSvmkdlPGSLLDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTP 618
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLLLE-----AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 619 VHIACAQGDIGCLKVLLNKKlrkeseefPEIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAV 698
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAG--------ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAA 260
                        170       180
                 ....*....|....*....|....*...
gi 932085572 699 ENSNLAIAGFLILEAKCDVDSYNLDDNT 726
Cdd:COG0666  261 AAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
586-686 1.25e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  586 LHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKLRKEseefpeihwqNYNGFTPLHLAVI 665
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----------KDNGRTALHYAAR 70
                          90       100
                  ....*....|....*....|.
gi 932085572  666 KGNREIVKLLLSVGANVEAKD 686
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
620-721 2.91e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  620 HIACAQGDIGCLKVLLnkklrkesEEFPEIHWQNYNGFTPLHLAVIKGNREIVKLLLSvgaNVEAKDGTCGRTPLHLAVE 699
Cdd:pfam12796   2 HLAAKNGNLELVKLLL--------ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAAR 70
                          90       100
                  ....*....|....*....|..
gi 932085572  700 NSNLAIAGFLiLEAKCDVDSYN 721
Cdd:pfam12796  71 SGHLEIVKLL-LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
660-754 1.27e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  660 LHLAVIKGNREIVKLLLSVGANVEAKDgTCGRTPLHLAVENSNLAIAGFLILEAKCDVDSYNlddNTPLHLAAGLGLEGL 739
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 932085572  740 TALLVAAGADTMETN 754
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
544-764 1.52e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 544 GDTALHLAVincQFNAIESLVSVMKDLpGSLLDMYNYLRQTPLH--LAVLTKQPLATECLLRANASATTCDRHGNTPVHI 621
Cdd:PHA03095  83 GFTPLHLYL---YNATTLDVIKLLIKA-GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 622 -----ACaqgDIGCLKVLLNKKlrkeseefPEIHWQNYNGFTPLH--LAVIKGNREIVKLLLSVGANVEAKDgTCGRTPL 694
Cdd:PHA03095 159 llksrNA---NVELLRLLIDAG--------ADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 695 H-LAVENSNLAIAGFLILEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLA 764
Cdd:PHA03095 227 HsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
585-773 9.10e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 9.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 585 PLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKK--------LRKESEEFpeiHWQNYNG 656
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSInkcsvfytLVAIKDAF---NNRNVEI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 657 FTPLHLAVIKGNR------------------EIVKLLLSVGANVEAKDGTCGRTPLHLAVENSNLAIAGFLILEAkCDVD 718
Cdd:PHA02878 117 FKIILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVN 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 932085572 719 SYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLATTA----EVKKIL 773
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYckdyDILKLL 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
584-766 4.17e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 584 TPLHLAVLTKQPLAT-ECLLRANASATTCDRHGNTPVHIaCAQG---DIGCLKVLLNKKLRKESeefpeihwQNYNGFTP 659
Cdd:PHA03095  85 TPLHLYLYNATTLDViKLLIKAGADVNAKDKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNA--------LDLYGMTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 660 LHlAVIKGNR---EIVKLLLSVGANVEAKDgTCGRTPLHLAVEN--SNLAIAGFLIlEAKCDVDSYNLDDNTPLHLAAGL 734
Cdd:PHA03095 156 LA-VLLKSRNanvELLRLLIDAGADVYAVD-DRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAATDMLGNTPLHSMATG 232
                        170       180       190
                 ....*....|....*....|....*....|....
gi 932085572 735 GL--EGLTALLVAAGADTMETNSEDETPYSLATT 766
Cdd:PHA03095 233 SSckRSLVLPLLIAGISINARNRYGQTPLHYAAV 266
IPT smart00429
ig-like, plexins, transcription factors;
305-407 3.36e-12

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 63.21  E-value: 3.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572   305 LKICRMDKNSGCVTGGDEVyLLCDRVQKEDIEVRFYEydpeqgkQVWEDLGTFAPSdvhRQFAIVFKTPPYWNVAVEKPV 384
Cdd:smart00429   2 PVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-------GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPV 70
                           90       100
                   ....*....|....*....|...
gi 932085572   385 kvlCELRRKSDKETSEPMEFTYT 407
Cdd:smart00429  71 ---RTVGLRNGGVPSSPQPFTYV 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
656-786 4.92e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 4.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 656 GFTPLHLAVIKGN---REIVKLLLSVGANVEAKDgTCGRTPLHLAVENSN-LAIAGFLIlEAKCDVDSYNLDDNTPLHL- 730
Cdd:PHA03095  47 GKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYNATtLDVIKLLI-KAGADVNAKDKVGRTPLHVy 124
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 932085572 731 AAGLGL-EGLTALLVAAGADTMETNSEDETPY-----SLATTAEVKKILSDEDEVPAAADDI 786
Cdd:PHA03095 125 LSGFNInPKVIRLLLRKGADVNALDLYGMTPLavllkSRNANVELLRLLIDAGADVYAVDDR 186
PHA03100 PHA03100
ankyrin repeat protein; Provisional
572-718 2.76e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 572 GSLLDMYNYLRQTPLHLAVLTK--QPLATECLLRANASATTCDRHGNTPVHIA--CAQGDIGCLKVLL------NKKLRK 641
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIdkgvdiNAKNRV 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 642 E---SEEFPeIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGfLILEAKCDVD 718
Cdd:PHA03100 176 NyllSYGVP-INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDTPLHIAILNNNKEIFK-LLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
584-731 3.59e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 584 TPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLnkklrkesEEFPEIHWQNYNGFTPLHLA 663
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL--------ENGASTDARDKCGNTPLHIS 241
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 932085572 664 VIK-GNREIVKLLLSVGANVEAKDGTCGRTPLHLAVENSNLAIagfLILEAKCDVDSYNLDDNTPLHLA 731
Cdd:PHA02878 242 VGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
572-788 5.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 5.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 572 GSLLDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQG-----DIGCLKVLLNKKLRKESeef 646
Cdd:PHA03100  25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNA--- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 647 peihwQNYNGFTPLHLAVIK--GNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENS--NLAIAGFLI------------ 710
Cdd:PHA03100 102 -----PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD-GENLLHLYLESNkiDLKILKLLIdkgvdinaknrv 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 711 ---LEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLATTAEVKKILSdedEVPAAADDIK 787
Cdd:PHA03100 176 nylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK---LLLNNGPSIK 252

                 .
gi 932085572 788 I 788
Cdd:PHA03100 253 T 253
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
305-408 7.42e-10

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 56.32  E-value: 7.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 305 LKICRMDKNSGCVTGGDEVYLLCDRVQKE-DIEVRFYEYdpeqgkqvwedlGTFAPSDVHrQFAIVFKTPPYwnvAVEKP 383
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFGGG------------VPCSVLSVS-STAIVCTTPPY---ANPGP 64
                         90       100
                 ....*....|....*....|....*
gi 932085572 384 VKVLCELRRKSDKETSEPMEFTYTP 408
Cdd:cd00102   65 GPVEVTVDRGNGGITSSPLTFTYVP 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
539-710 8.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 539 VQNDDGDTALHLAVINCQFNAIESLVsvmkDLPGSLLDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTP 618
Cdd:PHA02875  63 VKYPDIESELHDAVEEGDVKAVEELL----DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 619 VHIACAQGDIGCLKVLLNKKLRKESEEfpeihwqnYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTCGRTPLHLAV 698
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIED--------CCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI 210
                        170
                 ....*....|..
gi 932085572 699 ENSNLAIAGFLI 710
Cdd:PHA02875 211 ENNKIDIVRLFI 222
PHA02874 PHA02874
ankyrin repeat protein; Provisional
583-731 9.00e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 9.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 583 QTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLnkklrkesEEFPEIHWQNYNGFTPLHL 662
Cdd:PHA02874 125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL--------EKGAYANVKDNNGESPLHN 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 663 AVIKGNREIVKLLLSVGANVEAKdgtCGR--TPLHLAVENSNLAIAgFLILEAKCDVDsyNLDDNTPLHLA 731
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNK---CKNgfTPLHNAIIHNRSAIE-LLINNASINDQ--DIDGSTPLHHA 261
PHA02875 PHA02875
ankyrin repeat protein; Provisional
654-764 1.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 654 YNGFTPLHLAVIKGNREIVKLLLSVGA--NVEAKDGtcgRTPLHLAVENSNLAIAGFLILEAKCDVDSYNLDDNTPLHLA 731
Cdd:PHA02875  33 YDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI---ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLA 109
                         90       100       110
                 ....*....|....*....|....*....|...
gi 932085572 732 AGLGLEGLTALLVAAGADTMETNSEDETPYSLA 764
Cdd:PHA02875 110 TILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
529-681 1.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 529 LLAIQRQVTAVQNDDGDTALHLAVINCQFNAIESLVSVMKDLpgsllDMYNYLRQTPLHLAVLTKQPLATECLLRANASA 608
Cdd:PHA02875  87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADP-----DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 932085572 609 TTCDRHGNTPVHIACAQGDIGCLKVLLNKKlrkeseefPEIHWQNYNGFTPLHLAVIKGNR-EIVKLLLSVGAN 681
Cdd:PHA02875 162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSG--------ANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
615-676 2.08e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.08e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 932085572  615 GNTPVHIACAQGDIGCLKVLLNKKLrkeseefpEIHWQNYNGFTPLHLAVIKGNREIVKLLL 676
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA--------DINAVDGNGETALHFAASNGNVEVLKLLL 54
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
307-408 2.60e-09

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


Pssm-ID: 238583  Cd Length: 101  Bit Score: 55.18  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 307 ICRMDKNSGCVTGGDEVYLLCDRVQKeDIEVRFYEYDPEqGKQVWEDLGTFAPSDVHrQFAIVFKTPPYWNVAVEKPVKV 386
Cdd:cd01178    4 IEKKSLNSCSVNGGEELFLTGKNFLK-DSKVVFQEKGQD-GEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQV 80
                         90       100
                 ....*....|....*....|....*
gi 932085572 387 ---LCELRRKSdketSEPMEFTYTP 408
Cdd:cd01178   81 qfyVVNGKRKR----SQPQTFTYTP 101
Ank_4 pfam13637
Ankyrin repeats (many copies);
658-710 2.79e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 2.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 932085572  658 TPLHLAVIKGNREIVKLLLSVGANVEAKDGtCGRTPLHLAVENSNLAIAGFLI 710
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
544-745 1.16e-08

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: 58.94  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  544 GDTALHLAVINCQfNAIESLVSVMKDLPGslldmynylRQTPLHLAvltkqplatecllraNASATTCDRHGNTPVHIAC 623
Cdd:TIGR00870  82 GDTLLHAISLEYV-DAVEAILLHLLAAFR---------KSGPLELA---------------NDQYTSEFTPGITALHLAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  624 AQGDIGCLKVLLNKK----LRKESEEFPEIHWQN--YNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDgTCGRTPLHLA 697
Cdd:TIGR00870 137 HRQNYEIVKLLLERGasvpARACGDFFVKSQGVDsfYHGESPLNAAACLGSPSIVALLSEDPADILTAD-SLGNTLLHLL 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 932085572  698 V-------ENSNLAIA---GFLILEAKCDvDSY------NLDDNTPLHLAAGLGLEGLTALLVA 745
Cdd:TIGR00870 216 VmenefkaEYEELSCQmynFALSLLDKLR-DSKelevilNHQGLTPLKLAAKEGRIVLFRLKLA 278
PHA02876 PHA02876
ankyrin repeat protein; Provisional
541-764 1.59e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 541 NDDGDTALHLAVincQFNAIESLVSVMKDlPGSLLDMYNYLRQTPLHLavLTKQPLATE---CLLRANASATTCDRHGNT 617
Cdd:PHA02876 270 DDCKNTPLHHAS---QAPSLSRLVPKLLE-RGADVNAKNIKGETPLYL--MAKNGYDTEnirTLIMLGADVNAADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 618 PVHIACAQGDIGCLKVLLnkklrkeSEEFPEIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTCGrTPLHLA 697
Cdd:PHA02876 344 PLHQASTLDRNKDIVITL-------LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFA 415
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 932085572 698 VENSNLAIAGFLILEAKCDVDSYNLDDNTPLHLAAGLGLE-GLTALLVAAGADTMETNSEDETPYSLA 764
Cdd:PHA02876 416 LCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02736 PHA02736
Viral ankyrin protein; Provisional
606-731 3.06e-08

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 53.73  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 606 ASATTCDRHGNTPVHIACAQGDIGCL---KVLLNKKLRKESEEFpeihwqNYNGFTPLHLAVIKGN---REIVKLLLSVG 679
Cdd:PHA02736   8 IFASEPDIEGENILHYLCRNGGVTDLlafKNAISDENRYLVLEY------NRHGKQCVHIVSNPDKadpQEKLKLLMEWG 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 932085572 680 ANVEAKDGTCGRTPLHLAVENSNLAIAGFLILEAKCDVDSYNLDDNTPLHLA 731
Cdd:PHA02736  82 ADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVA 133
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
655-686 3.28e-08

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 49.98  E-value: 3.28e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 932085572  655 NGFTPLHLAVIK-GNREIVKLLLSVGANVEAKD 686
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
544-677 3.71e-08

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: 56.94  E-value: 3.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 544 GDTALHLAVINCQFNAIESLVSVMKDL-------------PGSLLdmynYLRQTPLHLAVLTKQPLATECLLRANASATT 610
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgPKNLI----YYGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 611 CDRHGNTPVHIACAQG--DIGC--LKVLLNkkLRKESEEFPEIHWQNYNGFTPLHLAVIKGNREIVKLLLS 677
Cdd:cd22192  165 QDSLGNTVLHILVLQPnkTFACqmYDLILS--YDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
599-758 7.13e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 7.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 599 ECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKLrkeseefpEIHWQNYNGFTPLHLAVIKGNREIVKLLLSV 678
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC--------NVHIRDANGNTALWNAISAKHHKIFRILYHF 613
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 679 GAnveAKDGTCGRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDE 758
Cdd:PLN03192 614 AS---ISDPHAAGDLLCTAAKRNDLTAMKEL-LKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA03095 PHA03095
ankyrin-like protein; Provisional
527-709 9.86e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 9.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 527 RYLLAIQRQVTAVqNDDGDTALHLAVI--NCQFNAIESLVSVMKDLPGSllDMYnylRQTPLHLAVLTKQPLAT--ECLL 602
Cdd:PHA03095 136 RLLLRKGADVNAL-DLYGMTPLAVLLKsrNANVELLRLLIDAGADVYAV--DDR---FRSLLHHHLQSFKPRARivRELI 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 603 RANASATTCDRHGNTPVHIACAQGDigCLKVLLNKKLRKESEefpeIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANV 682
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSS--CKRSLVLPLLIAGIS----INARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283
                        170       180
                 ....*....|....*....|....*...
gi 932085572 683 EAKDgTCGRTPLHLAVENSNL-AIAGFL 709
Cdd:PHA03095 284 NAVS-SDGNTPLSLMVRNNNGrAVRAAL 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
544-735 2.56e-07

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: 54.25  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 544 GDTALHLAVINcqfNAIESLVSVMKDLPGsLLDMYN----YLRQTPLHLAVLTKQPLATECLLR-----ANASAT-TCDR 613
Cdd:cd22192   51 GETALHVAALY---DNLEAAVVLMEAAPE-LVNEPMtsdlYQGETALHIAVVNQNLNLVRELIArgadvVSPRATgTFFR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 614 HGntpvhiacaqgdIGCLKvllnkklrkeseefpeihwqnYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDgTCGRTP 693
Cdd:cd22192  127 PG------------PKNLI---------------------YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD-SLGNTV 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 932085572 694 LHLAV--ENSNLAIAGF-LILEAKCDVDSYNLD--DN----TPLHLAAGLG 735
Cdd:cd22192  173 LHILVlqPNKTFACQMYdLILSYDKEDDLQPLDlvPNnqglTPFKLAAKEG 223
PHA02875 PHA02875
ankyrin repeat protein; Provisional
615-775 2.71e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 615 GNTPVHIACAQGDIGCLKVLLNKKlrkeseEFPEIhwqNYNGF-TPLHLAVIKGNREIVKLLLSVGA---NVEAKDGTcg 690
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHG------AIPDV---KYPDIeSELHDAVEEGDVKAVEELLDLGKfadDVFYKDGM-- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 691 rTPLHLAVENSNLAIAGfLILEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLATT---A 767
Cdd:PHA02875 104 -TPLHLATILKKLDIMK-LLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAkgdI 181

                 ....*...
gi 932085572 768 EVKKILSD 775
Cdd:PHA02875 182 AICKMLLD 189
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
73-174 4.74e-07

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143648  Cd Length: 161  Bit Score: 50.35  E-value: 4.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  73 PYLEILEQPKSRgFRFRYPCEGpSHGGLPGqfssPKNKSYPSVQLNNYHGLCRIVVSLVTEDEPYMPHAHS----LTGKN 148
Cdd:cd07927    1 YELRIEVQPEPH-HRARYETEG-SRGAVKA----PSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYqvhrITGKT 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 932085572 149 AS--------GEGIVTVQIGPEQGMSASFPNLGI 174
Cdd:cd07927   75 TTpckekiigNTKVLEIPLEPKNNMTATIDCAGI 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
655-684 5.35e-07

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 46.43  E-value: 5.35e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 932085572   655 NGFTPLHLAVIKGNREIVKLLLSVGANVEA 684
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
648-697 6.29e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 6.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 932085572  648 EIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGtCGRTPLHLA 697
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
602-729 1.09e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs 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: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 52.45  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 602 LRANASATTC------DRHGNTP----VHIACAQGDiGCLKVLLNKklrkeseEFPEihwQNYNGFTPLHLAVIKGNREI 671
Cdd:cd22194   88 LTASDTGKTClmkallNINENTKeivrILLAFAEEN-GILDRFINA-------EYTE---EAYEGQTALNIAIERRQGDI 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 672 VKLLLSVGANVEAK------------DG-TCGRTPLHLAVENSNLAIAGFLILEAKCDVDSYNLDDNTPLH 729
Cdd:cd22194  157 VKLLIAKGADVNAHakgvffnpkykhEGfYFGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLH 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
632-765 3.69e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 632 KVLLNKKLRKESEEFPEIHWQNYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHL-----AVENSNLAIA 706
Cdd:PHA03100  11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKN-NSTPLHYlsnikYNLTDVKEIV 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085572 707 GfLILEAKCDVDSYNLDDNTPLHLAAGLGLEGLT--ALLVAAGADTMETNSEDETPYSLAT 765
Cdd:PHA03100  90 K-LLLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYL 149
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
653-727 5.30e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 5.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 932085572 653 NYNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGFLILEAKCDvdsYNLDDNTP 727
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD-GKTPLELAEENGFREVVQLLSRHSQCH---FELGANAK 182
PHA02874 PHA02874
ankyrin repeat protein; Provisional
539-699 5.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 539 VQNDDGDTALHLAVINCQFNAIESLVSV-----MKDLPGslldmyNYlrqtPLHLAVLTKQPLATECLLRANASATTCDR 613
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYgadvnIEDDNG------CY----PIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 614 HGNTPVHIACAQGDIGCLKVLL---NKKLRKESEEFPEIHW--------------------QNYNGFTPLHLAV-IKGNR 669
Cdd:PHA02874 189 NGESPLHNAAEYGDYACIKLLIdhgNHIMNKCKNGFTPLHNaiihnrsaiellinnasindQDIDGSTPLHHAInPPCDI 268
                        170       180       190
                 ....*....|....*....|....*....|
gi 932085572 670 EIVKLLLSVGANVEAKDGTcGRTPLHLAVE 699
Cdd:PHA02874 269 DIIDILLYHKADISIKDNK-GENPIDTAFK 297
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
601-677 5.53e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 5.53e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 932085572 601 LLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLnkklrkeseEF-PEIHWQNYNGFTPLHLAVIKGNREIVKLLLS 677
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL---------EFgADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
596-771 5.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 596 LATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKlrkeseefPEIHWQNYNGFTPLHLAVIKGNREIVKLL 675
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG--------ADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 676 LSVGANVEAKD----------------------------GTCGRTPLHLAVENSNLAIAGFLILEAKCDVDSYNLDDNTP 727
Cdd:PHA02876 231 IDNRSNINKNDlsllkairnedletslllydagfsvnsiDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 932085572 728 LHLAA--GLGLEGLTAlLVAAGADTMETNSEDETPYSLATTAEVKK 771
Cdd:PHA02876 311 LYLMAknGYDTENIRT-LIMLGADVNAADRLYITPLHQASTLDRNK 355
PHA03095 PHA03095
ankyrin-like protein; Provisional
502-638 5.94e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 502 KKEFALSILEHMSSAIRDYASTgdARYLLAIQRQVTAVqNDDGDTALHLAVINCQFNAieslvSVMKDL--PGSLLDMYN 579
Cdd:PHA03095 183 VDDRFRSLLHHHLQSFKPRARI--VRELIRAGCDPAAT-DMLGNTPLHSMATGSSCKR-----SLVLPLliAGISINARN 254
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 932085572 580 YLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKK 638
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
PHA02874 PHA02874
ankyrin repeat protein; Provisional
658-760 6.65e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 6.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 658 TPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSNLAIAGFLILE-AKCDVDSYNLddNTPLHLAAGLGL 736
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKgAYANVKDNNG--ESPLHNAAEYGD 202
                         90       100
                 ....*....|....*....|....
gi 932085572 737 EGLTALLVAAGADTMETNSEDETP 760
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTP 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
670-760 1.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 670 EIVKLLLSVGANVEaKDGTCGRTPLHLAVENSN---LAIAGFLiLEAKCDVDSYNLDDNTPLHLAAGLG-LEGLTALLVA 745
Cdd:PHA03095  28 EEVRRLLAAGADVN-FRGEYGKTPLHLYLHYSSekvKDIVRLL-LEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIK 105
                         90
                 ....*....|....*
gi 932085572 746 AGADTMETNSEDETP 760
Cdd:PHA03095 106 AGADVNAKDKVGRTP 120
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
696-774 1.56e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 696 LAVENSNLAIAG-----FLILEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLAT---TA 767
Cdd:PTZ00322  82 LTVELCQLAASGdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEengFR 161

                 ....*..
gi 932085572 768 EVKKILS 774
Cdd:PTZ00322 162 EVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
540-677 1.81e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs 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: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.60  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 540 QNDDGDTALHLAVINCQFNAIESLVSVMKDL----------PGSLLDMYnYLRQTPLHLAVLTKQPLATECLL-RANASA 608
Cdd:cd22194  137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVnahakgvffnPKYKHEGF-YFGETPLALAACTNQPEIVQLLMeKESTDI 215
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 932085572 609 TTCDRHGNTPVHIACAQGD-----IGCLKVLLNKKLRK-ESEEFPEIhwQNYNGFTPLHLAVIKGNREIVKLLLS 677
Cdd:cd22194  216 TSQDSRGNTVLHALVTVAEdsktqNDFVKRMYDMILLKsENKNLETI--RNNEGLTPLQLAAKMGKAEILKYILS 288
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
655-684 2.05e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 2.05e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 932085572  655 NGFTPLHLAVIKGNREIVKLLLSVGANVEA 684
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
584-750 2.08e-05

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: 48.09  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 584 TPLHLAVLTKQPLATECLLRaNASATTCDR--HGNTPVHIACAQGDIGCLKVLLnkklrkesEEFPE-----IHWQNYNG 656
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRgaLGETALHVAALYDNLEAAVVLM--------EAAPElvnepMTSDLYQG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 657 FTPLHLAVIKGNREIVKLLLSVGANVEAK--DGTCGRTPLHlavensNLAIAGflileakcdvdsynlddNTPLHLAAGL 734
Cdd:cd22192   90 ETALHIAVVNQNLNLVRELIARGADVVSPraTGTFFRPGPK------NLIYYG-----------------EHPLSFAACV 146
                        170
                 ....*....|....*.
gi 932085572 735 GLEGLTALLVAAGADT 750
Cdd:cd22192  147 GNEEIVRLLIEHGADI 162
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
513-710 2.20e-05

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: 48.15  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  513 MSSAIRDYASTGDARYLLAIQRQVTAVQNDDGDTALHLAvINCQfnaieslvsvmkdlpgslldmyNYLRQTPLHLAVLT 592
Cdd:TIGR00870   6 IVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKKLN-INCP----------------------DRLGRSALFVAAIE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572  593 KQPLA-TECLLRANASATTcdrhGNTPVHIAcAQGDIGCLKVLLN--KKLRKESEEFPEIHWQN----YNGFTPLHLAVI 665
Cdd:TIGR00870  63 NENLElTELLLNLSCRGAV----GDTLLHAI-SLEYVDAVEAILLhlLAAFRKSGPLELANDQYtsefTPGITALHLAAH 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 932085572  666 KGNREIVKLLLSVGANVEAKdGTC--------------GRTPLHLAVENSNLAIAGFLI 710
Cdd:TIGR00870 138 RQNYEIVKLLLERGASVPAR-ACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195
PHA02741 PHA02741
hypothetical protein; Provisional
653-731 2.40e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.80  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 653 NYNGFTPLHLAVIKGNR----EIVKLLLSVGANVEAKDGTCGRTPLHLAVENSNLAIAGFLILEAKCDVDSYNLDDNTPL 728
Cdd:PHA02741  57 DDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPF 136

                 ...
gi 932085572 729 HLA 731
Cdd:PHA02741 137 ELA 139
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
544-735 3.78e-05

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: 47.57  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 544 GDTALHLAVINCQFNAIESLVSVMKDLPGSlldmynylrqtplhlavLTKQPLatecllrANASATTCDRHGNTPVHIAC 623
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDS-----------------GNPKEL-------VNAPCTDEFYQGQTALHIAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 624 AQGDIGCLKVLLNK----KLRKESEEFPEiHWQN--YNGFTPLHLAVIKGNREIVKLLLSVGANVEAKDGT--CGRTPLH 695
Cdd:cd21882   82 ENRNLNLVRLLVENgadvSARATGRFFRK-SPGNlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdsLGNTVLH 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 932085572 696 LAV-------ENSNLAIA---GFLILEAK-CDVDSYNLDDN----TPLHLAAGLG 735
Cdd:cd21882  161 ALVlqadntpENSAFVCQmynLLLSYGAHlDPTQQLEEIPNhqglTPLKLAAVEG 215
PHA03100 PHA03100
ankyrin repeat protein; Provisional
539-688 4.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 539 VQNDDGDTALHLAVINCqFNAIEsLVSVMKDLpGSLLDMYNYLRQTPLHLAVltKQPLAT-------------------- 598
Cdd:PHA03100 101 APDNNGITPLLYAISKK-SNSYS-IVEYLLDN-GANVNIKNSDGENLLHLYL--ESNKIDlkilkllidkgvdinaknrv 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 599 ECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLLNKKlrkeseefPEIHWQNYNGFTPLHLAVIKGNREIVKLLLSV 678
Cdd:PHA03100 176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG--------ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
                        170
                 ....*....|
gi 932085572 679 GANVEAKDGT 688
Cdd:PHA03100 248 GPSIKTIIET 257
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
496-735 1.24e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs 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: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 45.90  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 496 EMLRELKKEfalsilehMSSAIRDYASTGDARYLLaiqRQVTAVqnDDGDTALHLAVINCQFNA---IESLVSVMKDlpG 572
Cdd:cd22194   59 EELGELLKE--------LKDLSRRRRKTDVPDFLM---HKLTAS--DTGKTCLMKALLNINENTkeiVRILLAFAEE--N 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 573 SLLDMY--------NYLRQTPLHLAVLTKQPLATECLLRANASattcdrhgntpVHiACAQGdigclkVLLNKKLRKESE 644
Cdd:cd22194  124 GILDRFinaeyteeAYEGQTALNIAIERRQGDIVKLLIAKGAD-----------VN-AHAKG------VFFNPKYKHEGF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 645 EFPEihwqnyngfTPLHLAVIKGNREIVKLLLSVGANVEAKDGTCGRTPLHLAV-------ENSNLAIAGFLILEAKCDV 717
Cdd:cd22194  186 YFGE---------TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVtvaedskTQNDFVKRMYDMILLKSEN 256
                        250       260
                 ....*....|....*....|..
gi 932085572 718 DSY----NLDDNTPLHLAAGLG 735
Cdd:cd22194  257 KNLetirNNEGLTPLQLAAKMG 278
PHA02743 PHA02743
Viral ankyrin protein; Provisional
663-748 2.82e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 42.50  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 663 AVIKgnreiVKLLLSVGANVEAKDGTCGRTPLHLAVENSNLAIAGFLILEAKCDVDSYNLDDNTPLHLAAGLGLEGLTAL 742
Cdd:PHA02743  72 AVMK-----IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRDRRMMEI 146

                 ....*.
gi 932085572 743 LVAAGA 748
Cdd:PHA02743 147 LRANGA 152
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
654-756 4.11e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.08  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 654 YNGFTPLHLAVIKGNREIVKLLLSVGANVEA---------KDGTC---GRTPLHLAVENSNLAIAGFLiLEAKCDVDSYN 721
Cdd:cd22197   92 YRGHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYL-LENPHQPASLQ 170
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 932085572 722 LDD---NTPLHlaaglglegltALLVAagADTMETNSE 756
Cdd:cd22197  171 AQDslgNTVLH-----------ALVMI--ADNSPENSA 195
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
654-729 4.13e-04

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: 44.02  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 654 YNGFTPLHLAVIKGNREIVKLLLSVGANVEA----------KDGTC---GRTPLHLAVENSNLAIAGFLILEAKCDVDSY 720
Cdd:cd22193   74 YEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffqpkYQGEGfyfGELPLSLAACTNQPDIVQYLLENEHQPADIE 153
                         90
                 ....*....|.
gi 932085572 721 NLDD--NTPLH 729
Cdd:cd22193  154 AQDSrgNTVLH 164
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
654-729 6.44e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 43.26  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 654 YNGFTPLHLAVIKGNREIVKLLLSVGANVEA------------KDG-TCGRTPLHLAVENSNLAIAGFLiLE---AKCDV 717
Cdd:cd22196   92 YKGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkkgGPGfYFGELPLSLAACTNQLDIVKFL-LEnphSPADI 170
                         90
                 ....*....|..
gi 932085572 718 DSYNLDDNTPLH 729
Cdd:cd22196  171 SARDSMGNTVLH 182
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
523-735 6.96e-04

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: 43.25  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 523 TGDARYLLAIQRQVTA---VQNDDGDTALHLAVINCQFNA---IESLVSVMKDlPGSLLDMYN-------YLRQTPLHLA 589
Cdd:cd22193    5 LGFLQDLCRRRKDLTDsefTESSTGKTCLMKALLNLNPGTndtIRILLDIAEK-TDNLKRFINaeytdeyYEGQTALHIA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 590 VLTKQPLATECLLRANASattcdrhgntpVHiACAQGDigclkvLLNKKlrKESEEFpeihwqnYNGFTPLHLAVIKGNR 669
Cdd:cd22193   84 IERRQGDIVALLVENGAD-----------VH-AHAKGR------FFQPK--YQGEGF-------YFGELPLSLAACTNQP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 670 EIVKLLLS---VGANVEAKDgTCGRTPLHLAV-------ENSNLAIA---GFLILEAKCDVDS-----YNLDDNTPLHLA 731
Cdd:cd22193  137 DIVQYLLEnehQPADIEAQD-SRGNTVLHALVtvadntkENTKFVTRmydMILIRGAKLCPTVeleeiRNNDGLTPLQLA 215

                 ....
gi 932085572 732 AGLG 735
Cdd:cd22193  216 AKMG 219
Ank_5 pfam13857
Ankyrin repeats (many copies);
715-764 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 932085572  715 CDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAGADTMETNSEDETPYSLA 764
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
614-638 1.22e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|....*
gi 932085572   614 HGNTPVHIACAQGDIGCLKVLLNKK 638
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKG 25
Ank_4 pfam13637
Ankyrin repeats (many copies);
690-732 1.91e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 932085572  690 GRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLAA 732
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLL-LEKGADINAVDGNGETALHFAA 42
PHA02874 PHA02874
ankyrin repeat protein; Provisional
668-760 2.57e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085572 668 NREIVKLLLSVGANVEAKDGTCgRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLAAGLGLEGLTALLVAAG 747
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKML-FEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
                         90
                 ....*....|...
gi 932085572 748 ADTMETNSEDETP 760
Cdd:PHA02874 181 AYANVKDNNGESP 193
PHA02878 PHA02878
ankyrin repeat protein; Provisional
650-717 2.80e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 2.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 932085572 650 HWQNYNG------FTPLHLAVIKGNREIVKLLLSVGANVEAKDGTcGRTPLHLAVENSN-LAIAGFLILEAKCDV 717
Cdd:PHA02878  25 HTENYSTsaslipFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHR-DLTPLHIICKEPNkLGMKEMIRSINKCSV 98
Ank_5 pfam13857
Ankyrin repeats (many copies);
680-731 3.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 932085572  680 ANVEAKDGtCGRTPLHLAVENSNLAIAGFLiLEAKCDVDSYNLDDNTPLHLA 731
Cdd:pfam13857   7 IDLNRLDG-EGYTPLHVAAKYGALEIVRVL-LAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
584-635 3.85e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 3.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 932085572  584 TPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIACAQGDIGCLKVLL 635
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
574-622 3.85e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 932085572  574 LLDMYNYLRQTPLHLAVLTKQPLATECLLRANASATTCDRHGNTPVHIA 622
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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