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Conserved domains on  [gi|2130994378|ref|XP_044916770|]
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ankyrin repeat domain-containing protein 16 isoform X1 [Felis catus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11430360)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-307 2.99e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  41 TLLHCAARHGHRDVLAYLVESWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLE 120
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 121 VIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLT--VCPDAWkteSKIGRTPLHTAAMHGCLEAVKVLLQRGqY 198
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagADVNAQ---DNDGNTPLHLAAANGNLEIVKLLLEAG-A 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 199 QPDCRDRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGhLT 278
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDG-LT 254

                         250       260
                  ....*....|....*....|....*....
gi 2130994378 279 ALHYAAKEGHVSTVQMLLALGADINCKDA 307
Cdd:COG0666   255 ALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-359 5.41e-08

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 280 LHYAAKEGHVSTVQMLLALGADINCKDARNRSehgilglmmpetfsasfpreALHLACAGQHAACVELLLRSGLRDSRDD 359
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--------------------ALHLAAKNGHLEIVKLLLEHADVNLKDN 60
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-307 2.99e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  41 TLLHCAARHGHRDVLAYLVESWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLE 120
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 121 VIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLT--VCPDAWkteSKIGRTPLHTAAMHGCLEAVKVLLQRGqY 198
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagADVNAQ---DNDGNTPLHLAAANGNLEIVKLLLEAG-A 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 199 QPDCRDRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGhLT 278
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDG-LT 254

                         250       260
                  ....*....|....*....|....*....
gi 2130994378 279 ALHYAAKEGHVSTVQMLLALGADINCKDA 307
Cdd:COG0666   255 ALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 77-319 5.59e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  77 LHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQ 156
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 157 YLLTVCPDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRGQyQPDCRDRCGSTPFMDALQCGHIDVARLLLeKHQASASA 236
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLI-DHKACLDI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 237 QDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGHLTALHYAAKEGHVSTVQMLLALGADINCKDARNRSEHGIL 316
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLL-DSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242


                  ...
gi 2130994378 317 GLM 319
Cdd:PHA02875  243 DMI 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-306 3.29e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 3.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 177 LHTAAMHGCLEAVKVLLQRGqYQPDCRDRCGSTPFMDALQCGHIDVARLLLEKhqasasaqdslgaqaihraaltgqnea 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--------------------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2130994378 257 irflvcelgtdVDVRAASGHLTALHYAAKEGHVSTVQMLLALGADINCKD 306
Cdd:pfam12796  53 -----------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-359 5.41e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 280 LHYAAKEGHVSTVQMLLALGADINCKDARNRSehgilglmmpetfsasfpreALHLACAGQHAACVELLLRSGLRDSRDD 359
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--------------------ALHLAAKNGHLEIVKLLLEHADVNLKDN 60
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-296 1.02e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 108 TPLMMACTRRNLEVIQDLVE-HGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPD----AWKTESKIGRTPLHTAAM 182
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnePMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 183 HGCLEAVKVLLQRG-------------QYQPDCRDRCGSTPFMDALQCGHIDVARLLLEKHqASASAQDSLGAQAIHraA 249
Cdd:cd22192    99 NQNLNLVRELIARGadvvspratgtffRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLH--I 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 250 LTGQNEAIRflVCE-----LGTDVDVRAAS--------GhLTALHYAAKEGHVSTVQMLL 296
Cdd:cd22192   176 LVLQPNKTF--ACQmydliLSYDKEDDLQPldlvpnnqG-LTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 123-297 1.65e-06

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: 50.08  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 123 QDLVEHGANPLLKnkdgwnsvhvASREGDPVILQYlltvcpDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRG---QYQ 199
Cdd:TIGR00870  94 VDAVEAILLHLLA----------AFRKSGPLELAN------DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGasvPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 200 PDCRDrCGSTPFMDAL----------QC-GHIDVARLLLEkHQASASAQDSLGAQAIHRAAL----TGQNEAIRFLVCEL 264
Cdd:TIGR00870 158 ACGDF-FVKSQGVDSFyhgesplnaaAClGSPSIVALLSE-DPADILTADSLGNTLLHLLVMenefKAEYEELSCQMYNF 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2130994378 265 GTDVDVRAAS----------GHLTALHYAAKEGHVSTVQMLLA 297
Cdd:TIGR00870 236 ALSLLDKLRDskelevilnhQGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 278-304 3.12e-05

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: 40.65  E-value: 3.12e-05
                           10        20
                   ....*....|....*....|....*..
gi 2130994378  278 TALHYAAKEGHVSTVQMLLALGADINC 304
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 265-372 6.77e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 265 GTDVDVRAASGHlTALHYAAKEGHVSTVQMLLALGADINCKDARNR--------SEHGILGLMMPETFSASFPREALHLA 336
Cdd:PLN03192  548 KLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNtalwnaisAKHHKIFRILYHFASISDPHAAGDLL 626

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2130994378 337 CAGQHAACVEL---LLRSGLR-DSRDDTGALAQQLACGTD 372
Cdd:PLN03192  627 CTAAKRNDLTAmkeLLKQGLNvDSEDHQGATALQVAMAED 666
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-307 2.99e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  41 TLLHCAARHGHRDVLAYLVESWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLE 120
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 121 VIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLT--VCPDAWkteSKIGRTPLHTAAMHGCLEAVKVLLQRGqY 198
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagADVNAQ---DNDGNTPLHLAAANGNLEIVKLLLEAG-A 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 199 QPDCRDRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGhLT 278
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDG-LT 254

                         250       260
                  ....*....|....*....|....*....
gi 2130994378 279 ALHYAAKEGHVSTVQMLLALGADINCKDA 307
Cdd:COG0666   255 ALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-238 8.29e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 8.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  11 YRLAQEGRLCALREELRGAGRASCPGPAGDTLLHCAARHGHRDVLAYLVESwDMDIEAANRDYKRPLHEAASMGHRDCVR 90
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  91 YLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPDAwKTES 170
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-NAKD 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130994378 171 KIGRTPLHTAAMHGCLEAVKVLLQRGQyQPDCRDRCGSTPFMDALQCGHIDVARLLLEKHQASASAQD 238
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-309 3.13e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 3.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  63 DMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNS 142
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 143 VHVASREGDPVILQYLLTvCPDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRGqYQPDCRDRCGSTPFMDALQCGHIDV 222
Cdd:COG0666    91 LHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 223 ARLLLEKHqASASAQDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGHlTALHYAAKEGHVSTVQMLLALGADI 302
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADL 245


                  ....*..
gi 2130994378 303 NCKDARN 309
Cdd:COG0666   246 NAKDKDG 252
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-359 5.34e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 5.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  92 LLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLTVcPDAWKTESK 171
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA-GADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 172 IGRTPLHTAAMHGCLEAVKVLLQRGqYQPDCRDRCGSTPFMDALQCGHIDVARLLLEKHqASASAQDSLGAQAIHRAALT 251
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 252 GQNEAIRFLVcELGTDVDVRAASGHlTALHYAAKEGHVSTVQMLLALGADINCKDARNRSehgilglmmpetfsasfpre 331
Cdd:COG0666   164 GNLEIVKLLL-EAGADVNARDNDGE-TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT-------------------- 221

                         250       260
                  ....*....|....*....|....*...
gi 2130994378 332 ALHLACAGQHAACVELLLRSGLRDSRDD 359
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKD 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-369 7.02e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.42  E-value: 7.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 122 IQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRGQYqPD 201
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-IN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 202 CRDRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGHlTALH 281
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGN-TPLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 282 YAAKEGHVSTVQMLLALGADINCKDARNRSehgilglmmpetfsasfpreALHLACAGQHAACVELLLRSG-LRDSRDDT 360
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGET--------------------PLHLAAENGHLEIVKLLLEAGaDVNAKDND 218


                  ....*....
gi 2130994378 361 GALAQQLAC 369
Cdd:COG0666   219 GKTALDLAA 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 77-319 5.59e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  77 LHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQ 156
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 157 YLLTVCPDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRGQyQPDCRDRCGSTPFMDALQCGHIDVARLLLeKHQASASA 236
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLI-DHKACLDI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 237 QDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGHLTALHYAAKEGHVSTVQMLLALGADINCKDARNRSEHGIL 316
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLL-DSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242


                  ...
gi 2130994378 317 GLM 319
Cdd:PHA02875  243 DMI 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-306 3.29e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 3.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 177 LHTAAMHGCLEAVKVLLQRGqYQPDCRDRCGSTPFMDALQCGHIDVARLLLEKhqasasaqdslgaqaihraaltgqnea 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--------------------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2130994378 257 irflvcelgtdVDVRAASGHLTALHYAAKEGHVSTVQMLLALGADINCKD 306
Cdd:pfam12796  53 -----------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-136 2.51e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  43 LHCAARHGHRDVLAYLVESWDmDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKkaDWTPLMMACTRRNLEVI 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 2130994378 123 QDLVEHGANPLLKN 136
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-196 7.24e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 110 LMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPdawKTESKIGRTPLHTAAMHGCLEAV 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNGRTALHYAARSGHLEIV 77


                  ....*..
gi 2130994378 190 KVLLQRG 196
Cdd:pfam12796  78 KLLLEKG 84
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 141-304 4.43e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 141 NSVHVASReGDPVILQYLLTVCPDAWKTESKiGRTPLHTAAMHGCLEAVKVLLQRGqyqpdC----RDRCGSTPFMDALQ 216
Cdd:PLN03192  528 NLLTVAST-GNAALLEELLKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHA-----CnvhiRDANGNTALWNAIS 600

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 217 CGHIDVARLLlekHQASASAQDSLGAQAIHRAALTGQNEAIRFLVcELGTDVDVRAASGhLTALHYAAKEGHVSTVQMLL 296
Cdd:PLN03192  601 AKHHKIFRIL---YHFASISDPHAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQG-ATALQVAMAEDHVDMVRLLI 675


                  ....*...
gi 2130994378 297 ALGADINC 304
Cdd:PLN03192  676 MNGADVDK 683
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-311 5.90e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  76 PLHEAASMGHRDC---VRYLLGRGAAVDCLKKADWTPLMM-ACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHV--ASRE 149
Cdd:PHA03095   50 PLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 150 GDPVILQYLLTVCPDAWKTEsKIGRTPLH-----TAAmhgCLEAVKVLLQRGQYQPDcRDRCGSTPFMDALQCGHID--V 222
Cdd:PHA03095  130 INPKVIRLLLRKGADVNALD-LYGMTPLAvllksRNA---NVELLRLLIDAGADVYA-VDDRFRSLLHHHLQSFKPRarI 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 223 ARLLLEkHQASASAQDSLGAQAIHRAALTGQNEA--IRFLVcELGTDVDVRAASGHlTALHYAAKEGHVSTVQMLLALGA 300
Cdd:PHA03095  205 VRELIR-AGCDPAATDMLGNTPLHSMATGSSCKRslVLPLL-IAGISINARNRYGQ-TPLHYAAVFNNPRACRRLIALGA 281

                         250
                  ....*....|.
gi 2130994378 301 DINCKDARNRS 311
Cdd:PHA03095  282 DINAVSSDGNT 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-97 8.83e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 8.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  14 AQEGRLCALREELRGAGRASCPGPAGDTLLHCAARHGHRDVLAYLVESWDMDIEAANRDykrPLHEAASMGHRDCVRYLL 93
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT---ALHYAARSGHLEIVKLLL 81


                  ....
gi 2130994378  94 GRGA 97
Cdd:pfam12796  82 EKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-229 1.35e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  72 DYKRPLHEAASMGHRDCVRYLLGRGA-AVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREG 150
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 151 DPVILQYLLT--VCPDawkTESKIGRTPLHTAAMHGCLEAVKVLLQRGQyQPDCRDRCGSTPFM-DALQCGHIDVARLLL 227
Cdd:PHA02875  147 DIKGIELLIDhkACLD---IEDCCGCTPLIIAMAKGDIAICKMLLDSGA-NIDYFGKNGCVAALcYAIENNKIDIVRLFI 222


                  ..
gi 2130994378 228 EK 229
Cdd:PHA02875  223 KR 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 76-303 4.70e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 4.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  76 PLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHG-----ANPLLKNKDGWNS-------- 142
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSInkcsvFYTLVAIKDAFNNrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 143 --------------VHVASREGDPVI----LQYLLTVCPDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRGQyQPDCRD 204
Cdd:PHA02878  120 iltnrykniqtidlVYIDKKSKDDIIeaeiTKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPD 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 205 RCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRAALTGQNEAIRFLVCELGTDVDVRAASGHLTALHYAA 284
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI 277

                         250
                  ....*....|....*....
gi 2130994378 285 KEGHVstVQMLLALGADIN 303
Cdd:PHA02878  278 KSERK--LKLLLEYGADIN 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-302 1.03e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  64 MDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANpllKNKDGWNSV 143
Cdd:PHA02876  169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN---INKNDLSLL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 144 HVASREG-DPVILQYlltvcpDAWKTESKIG---RTPLHTAAMHGCLEA-VKVLLQRGqYQPDCRDRCGSTPFMDALQCG 218
Cdd:PHA02876  246 KAIRNEDlETSLLLY------DAGFSVNSIDdckNTPLHHASQAPSLSRlVPKLLERG-ADVNAKNIKGETPLYLMAKNG 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 219 H-IDVARLLLEKhQASASAQDSLGAQAIHRAALTGQNEAIRFLVCELGTDVDVRAASGHlTALHYAAKEGHVSTVQMLLA 297
Cdd:PHA02876  319 YdTENIRTLIML-GADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDK-TPIHYAAVRNNVVIINTLLD 396


                  ....*
gi 2130994378 298 LGADI 302
Cdd:PHA02876  397 YGADI 401
Ank_2 pfam12796
Ankyrin repeats (3 copies);
245-352 2.59e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 245 IHRAALTGQNEAIRFLVcELGTDVDVRAASGhLTALHYAAKEGHVSTVQMLLAlGADINCKDARNRsehgilglmmpetf 324
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRT-------------- 63

                          90       100
                  ....*....|....*....|....*...
gi 2130994378 325 sasfpreALHLACAGQHAACVELLLRSG 352
Cdd:pfam12796  64 -------ALHYAARSGHLEIVKLLLEKG 84
PHA03095 PHA03095
ankyrin-like protein; Provisional
 172-311 2.79e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 172 IGRTPLHT---AAMHGCLEAVKVLLQRGQYQpDCRDRCGSTPFMDALQCGH-IDVARLLLeKHQASASAQDSLGAQAIHr 247
Cdd:PHA03095   46 YGKTPLHLylhYSSEKVKDIVRLLLEAGADV-NAPERCGFTPLHLYLYNATtLDVIKLLI-KAGADVNAKDKVGRTPLH- 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130994378 248 AALTGQN---EAIRFLVcELGTDVDVRAASGHlTALHYAAKEGHVS--TVQMLLALGADINCKDARNRS 311
Cdd:PHA03095  123 VYLSGFNinpKVIRLLL-RKGADVNALDLYGM-TPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRS 189
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-196 9.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  39 GDTLLHCAARHGHRDVLAYLVESWDMDIEAANRDYKRPLHEAASMG-HRDCVRYLLGRGAAVDCLKKADWTPLMMACTRR 117
Cdd:PHA02876  307 GETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 118 NLEVIQDLVEHGAN-PLLKNKDGwNSVHVASREGDPVILQYLLTVCPDAWKTESKIGRTPLHTAAMHGC-LEAVKVLLQR 195
Cdd:PHA02876  387 NVVIINTLLDYGADiEALSQKIG-TALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCkLDVIEMLLDN 465


                  .
gi 2130994378 196 G 196
Cdd:PHA02876  466 G 466
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 89-352 1.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  89 VRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKD-------GWNSVHVASRegDPVILQYLLTV 161
Cdd:PHA03100   18 IKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNnstplhyLSNIKYNLTD--VKEIVKLLLEY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 162 CPDAWKTESKiGRTPLHTAAMH--GCLEAVKVLLQRGQYQPDCRDRcGSTPFMDALQCGHID--VARLLLEkhqasasaq 237
Cdd:PHA03100   96 GANVNAPDNN-GITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD-GENLLHLYLESNKIDlkILKLLID--------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 238 dslgaqaiHRAALTGQNEAIRFLvcELGTDVDVRAASGHlTALHYAAKEGHVSTVQMLLALGADINckdARNRSEHgilg 317
Cdd:PHA03100  165 --------KGVDINAKNRVNYLL--SYGVPINIKDVYGF-TPLHYAVYNNNPEFVKYLLDLGANPN---LVNKYGD---- 226

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2130994378 318 lmmpetfsasfprEALHLACAGQHAACVELLLRSG 352
Cdd:PHA03100  227 -------------TPLHIAILNNNKEIFKLLLNNG 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-227 1.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2130994378 173 GRTPLHTAAMHGCLEAVKVLLQRGqYQPDCRDRCGSTPFMDALQCGHIDVARLLL 227
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-141 1.87e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  39 GDTLLHCAARHGHRDVLAYLVESwDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRN 118
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264

                          90       100
                  ....*....|....*....|...
gi 2130994378 119 LEVIQDLVEHGANPLLKNKDGWN 141
Cdd:COG0666   265 ALIVKLLLLALLLLAAALLDLLT 287
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-227 4.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  58 LVESWDMDIEAANRDY-KRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKN 136
Cdd:PHA02878  152 LLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 137 KDGWNSVHVA-SREGDPVILQYLLTVCPDAWKTESKIGRTPLHTAAMHGclEAVKVLLQRGQyQPDCRDRCGSTPF-MDA 214
Cdd:PHA02878  232 KCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGA-DINSLNSYKLTPLsSAV 308

                         170
                  ....*....|...
gi 2130994378 215 LQCGHIDVARLLL 227
Cdd:PHA02878  309 KQYLCINIGRILI 321
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-93 4.50e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 4.50e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2130994378  39 GDTLLHCAARHGHRDVLAYLVESWdMDIEAANRDYKRPLHEAASMGHRDCVRYLL 93
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-359 5.41e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 280 LHYAAKEGHVSTVQMLLALGADINCKDARNRSehgilglmmpetfsasfpreALHLACAGQHAACVELLLRSGLRDSRDD 359
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--------------------ALHLAAKNGHLEIVKLLLEHADVNLKDN 60
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 76-311 7.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 7.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  76 PLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGAN------PLLkNKDGWNSV------ 143
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCI-EKDMIKTIldcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 144 ------------HVASREGDPVILQYLLTVCPDAwKTESKIGRTPLHTAAMHGCLEAVKVLLQRGQYQpDCRDRCGSTPF 211
Cdd:PHA02874  117 vnikdaelktflHYAIKKGDLESIKMLFEYGADV-NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA-NVKDNNGESPL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 212 MDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRAALTGQNeAIRFLVCElgTDVDVRAASGHlTALHYAAK-EGHVS 290
Cdd:PHA02874  195 HNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN--ASINDQDIDGS-TPLHHAINpPCDID 269

                         250       260
                  ....*....|....*....|.
gi 2130994378 291 TVQMLLALGADINCKDARNRS 311
Cdd:PHA02874  270 IIDILLYHKADISIKDNKGEN 290
Ank_4 pfam13637
Ankyrin repeats (many copies);
75-126 1.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2130994378  75 RPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLV 126
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-159 3.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 3.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2130994378 107 WTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLL 159
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
276-349 6.68e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 6.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130994378 276 HLTALHYAAKEGHVSTVQMLLALGADINCKDARNRSehgilglmmpetfsasfpreALHLACAGQHAACVELLL 349
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--------------------ALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-296 1.02e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 108 TPLMMACTRRNLEVIQDLVE-HGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPD----AWKTESKIGRTPLHTAAM 182
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnePMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 183 HGCLEAVKVLLQRG-------------QYQPDCRDRCGSTPFMDALQCGHIDVARLLLEKHqASASAQDSLGAQAIHraA 249
Cdd:cd22192    99 NQNLNLVRELIARGadvvspratgtffRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLH--I 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 250 LTGQNEAIRflVCE-----LGTDVDVRAAS--------GhLTALHYAAKEGHVSTVQMLL 296
Cdd:cd22192   176 LVLQPNKTF--ACQmydliLSYDKEDDLQPldlvpnnqG-LTPFKLAAKEGNIVMFQHLV 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-159 1.60e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  39 GDTLLHCAARHGHRDVLAYLVeSWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTR-R 117
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2130994378 118 NLEVIQDLVEHGANPLLKNK-DGWNSVHVASRegDPVILQYLL 159
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLL 287
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 123-297 1.65e-06

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: 50.08  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 123 QDLVEHGANPLLKnkdgwnsvhvASREGDPVILQYlltvcpDAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRG---QYQ 199
Cdd:TIGR00870  94 VDAVEAILLHLLA----------AFRKSGPLELAN------DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGasvPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 200 PDCRDrCGSTPFMDAL----------QC-GHIDVARLLLEkHQASASAQDSLGAQAIHRAAL----TGQNEAIRFLVCEL 264
Cdd:TIGR00870 158 ACGDF-FVKSQGVDSFyhgesplnaaAClGSPSIVALLSE-DPADILTADSLGNTLLHLLVMenefKAEYEELSCQMYNF 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2130994378 265 GTDVDVRAAS----------GHLTALHYAAKEGHVSTVQMLLA 297
Cdd:TIGR00870 236 ALSLLDKLRDskelevilnhQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
244-296 3.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 3.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2130994378 244 AIHRAALTGQNEAIRFLVcELGTDVDVRAASGhLTALHYAAKEGHVSTVQMLL 296
Cdd:pfam13637   4 ALHAAAASGHLELLRLLL-EKGADINAVDGNG-ETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-230 4.58e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  39 GDTLLHCAARHGHR-DVLAYLVESwDMDIEAANRDYKRPLHE-AASMG-HRDCVRYLLGRGAAVDCLKKADWTPL--MMA 113
Cdd:PHA03095   83 GFTPLHLYLYNATTlDVIKLLIKA-GADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLavLLK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 114 CTRRNLEVIQDLVEHGANPLLKNKDGwNS---VHVASREGDPVILQYLLTVCPDAWKTESkIGRTPLHTAAMHGCLEAVK 190
Cdd:PHA03095  162 SRNANVELLRLLIDAGADVYAVDDRF-RSllhHHLQSFKPRARIVRELIRAGCDPAATDM-LGNTPLHSMATGSSCKRSL 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130994378 191 V-----------------------------------LLQRGqYQPDCRDRCGSTPFMDALQCGHIDVARLLLEKH 230
Cdd:PHA03095  240 VlplliagisinarnrygqtplhyaavfnnpracrrLIALG-ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-320 4.59e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  54 VLAYLVESWDMDIEAA---NRDY--KRPLHEAASMGHRDCVRYLL--GRGAAVDCLKKADWTPLMMACTRRNL-EVIQDL 125
Cdd:PHA02876  214 VLECAVDSKNIDTIKAiidNRSNinKNDLSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 126 VEHGANPLLKNKDGWNSVHVASREG-DPVILQYLLTVCPDAWKTESkIGRTPLHTAA-MHGCLEAVKVLLQRGQyQPDCR 203
Cdd:PHA02876  294 LERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADR-LYITPLHQAStLDRNKDIVITLLELGA-NVNAR 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 204 DRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHrAALTGQNE--AIRFLVcELGTDVDVRAASGHlTALH 281
Cdd:PHA02876  372 DYCDKTPIHYAAVRNNVVIINTLLD-YGADIEALSQKIGTALH-FALCGTNPymSVKTLI-DRGANVNSKNKDLS-TPLH 447

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2130994378 282 YAAKEG-HVSTVQMLLALGADINCKDARNR-------SEHGILGLMM 320
Cdd:PHA02876  448 YACKKNcKLDVIEMLLDNGADVNAINIQNQypllialEYHGIVNILL 494
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 21-160 4.62e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  21 ALREELRGAGRASCPGPA-GDTLLHCAARHGHRD-VLAYLVESWDMDIEAANRDykRPLHEAASMGHRDCVRYLLGRGAA 98
Cdd:PLN03192  539 ALLEELLKAKLDPDIGDSkGRTPLHIAASKGYEDcVLVLLKHACNVHIRDANGN--TALWNAISAKHHKIFRILYHFASI 616

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130994378  99 VDCLKKADWtpLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLT 160
Cdd:PLN03192  617 SDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 77-162 4.79e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  77 LHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQ 156
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                  ....*.
gi 2130994378 157 YLLTVC 162
Cdd:PTZ00322  166 LLSRHS 171
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-248 7.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  46 AARHGHRDVLAYLVESwDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGA-----AVDCLKK---------------- 104
Cdd:PHA02874   42 AIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilPIPCIEKdmiktildcgidvnik 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 105 --ADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPDAwKTESKIGRTPLHTAAM 182
Cdd:PHA02874  121 daELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA-NVKDNNGESPLHNAAE 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130994378 183 HGCLEAVKVLLQRGQY-QPDCRDrcGSTPFMDALQCGHIDVARLLlekHQASASAQDSLGAQAIHRA 248
Cdd:PHA02874  200 YGDYACIKLLIDHGNHiMNKCKN--GFTPLHNAIIHNRSAIELLI---NNASINDQDIDGSTPLHHA 261
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 173-311 1.01e-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: 47.45  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 173 GRTPLHTAAMHGCLEAVKVLLQRGQ----------YQPDCRDRC---GSTPFMDALQCGHIDVARLLLEKHQASASAQDS 239
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGAdvnahakgvfFNPKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 240 LGAQAIHraALT-------GQNEAIR------FLVCELGTDVDVRAASGhLTALHYAAKEGHVSTVQMLlaLGADINCKD 306
Cdd:cd22194   221 RGNTVLH--ALVtvaedskTQNDFVKrmydmiLLKSENKNLETIRNNEG-LTPLQLAAKMGKAEILKYI--LSREIKEKP 295


                  ....*
gi 2130994378 307 ARNRS 311
Cdd:cd22194   296 NRSLS 300
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 209-306 1.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 209 TPFMDALQCGHIDVARLLLeKHQASASAQDSLGAQAIHRAALTGQNEAIRFL----------------------VCELGT 266
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFI-KHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktILDCGI 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2130994378 267 DVDVRAASGHlTALHYAAKEGHVSTVQMLLALGADINCKD 306
Cdd:PHA02874  116 DVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIED 154
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 39-132 1.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  39 GDTLLHCAARHGHRDVLAYLVeSWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRN 118
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90
                  ....*....|....
gi 2130994378 119 LEVIQDLVEHGANP 132
Cdd:PHA02875  181 IAICKMLLDSGANI 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 278-304 3.12e-05

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: 40.65  E-value: 3.12e-05
                           10        20
                   ....*....|....*....|....*..
gi 2130994378  278 TALHYAAKEGHVSTVQMLLALGADINC 304
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 80-227 4.01e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  80 AASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDG----WNSVHVASREGDPVIL 155
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGntalWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130994378 156 QYlltvcpdAWKTESKIGRTPLHTAAMHGCLEAVKVLLQRGqYQPDCRDRCGSTPFMDALQCGHIDVARLLL 227
Cdd:PLN03192  612 HF-------ASISDPHAAGDLLCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 278-306 4.80e-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. 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: 39.97  E-value: 4.80e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2130994378 278 TALHYAA-KEGHVSTVQMLLALGADINCKD 306
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-248 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2130994378 192 LLQRGQYQPDCRDRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSLGAQAIHRA 248
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-165 2.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  39 GDTLLHCAA--RHGHRDVLAYLvESWDMDIEAANRDYKRPLHEAASMGHRDC------------------VRYLLGRGAA 98
Cdd:PHA03100  106 GITPLLYAIskKSNSYSIVEYL-LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVP 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130994378  99 VDCLKKADWTPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLTVCPDA 165
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_5 pfam13857
Ankyrin repeats (many copies);
108-146 2.97e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2130994378 108 TPLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVA 146
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 168-278 3.86e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 168 TESKIGRTPLHTAAMHGC-LEA------VKVLLQRGQyQPDCRDRCGSTPFMDALQCGHIDVARLLLEkHQASASAQDSL 240
Cdd:PTZ00322   70 TEEVIDPVVAHMLTVELCqLAAsgdavgARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKD 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2130994378 241 GAQAIHRAALTGQNEAIRFLV--CELGTDVDVRAASGHLT 278
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSrhSQCHFELGANAKPDSFT 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 31-101 4.42e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130994378  31 RASCPGPAGDtLLHCAARHGHRDVLAYLVESwDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDC 101
Cdd:PLN03192  615 SISDPHAAGD-LLCTAAKRNDLTAMKELLKQ-GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 173-196 4.47e-04

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: 37.24  E-value: 4.47e-04
                          10        20
                  ....*....|....*....|....
gi 2130994378 173 GRTPLHTAAMHGCLEAVKVLLQRG 196
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENG 25
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 265-372 6.77e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 265 GTDVDVRAASGHlTALHYAAKEGHVSTVQMLLALGADINCKDARNR--------SEHGILGLMMPETFSASFPREALHLA 336
Cdd:PLN03192  548 KLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNtalwnaisAKHHKIFRILYHFASISDPHAAGDLL 626

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2130994378 337 CAGQHAACVEL---LLRSGLR-DSRDDTGALAQQLACGTD 372
Cdd:PLN03192  627 CTAAKRNDLTAmkeLLKQGLNvDSEDHQGATALQVAMAED 666
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-128 9.56e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 9.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  71 RDY--KRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRRNLEVIQDLVEH 128
Cdd:PTZ00322  111 RDYdgRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-137 1.04e-03

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: 36.11  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2130994378 107 WTPLMMACTRR-NLEVIQDLVEHGANPLLKNK 137
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 173-196 1.19e-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: 36.03  E-value: 1.19e-03
                           10        20
                   ....*....|....*....|....
gi 2130994378  173 GRTPLHTAAMHGCLEAVKVLLQRG 196
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKG 25
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 278-304 1.21e-03

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: 36.08  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....*..
gi 2130994378 278 TALHYAAKEGHVSTVQMLLALGADINC 304
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-196 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  37 PAGDTLLHCAARHGHRDVLAYLVESWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTR 116
Cdd:PHA02875   66 PDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 117 RNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGDPVILQYLLtvcpDAWKTESKIGRTP----LHTAAMHGCLEAVKVL 192
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL----DSGANIDYFGKNGcvaaLCYAIENNKIDIVRLF 221


                  ....
gi 2130994378 193 LQRG 196
Cdd:PHA02875  222 IKRG 225
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 173-296 1.85e-03

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: 40.25  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 173 GRTPLHTAAMHGCLEAVKVLLQRG------------QYQPDCRDRCGSTPFMDALQCGHIDVARLLLEK-HQ-ASASAQD 238
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGadvsaratgrffRKSPGNLFYFGELPLSLAACTNQEEIVRLLLENgAQpAALEAQD 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130994378 239 SLGAQAIHRAALTGQNEAIRF-LVCELGTDVDVRAASGH-------------LTALHYAAKEGHVSTVQMLL 296
Cdd:cd21882   153 SLGNTVLHALVLQADNTPENSaFVCQMYNLLLSYGAHLDptqqleeipnhqgLTPLKLAAVEGKIVMFQHIL 224
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 76-101 1.93e-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: 35.26  E-value: 1.93e-03
                           10        20
                   ....*....|....*....|....*.
gi 2130994378   76 PLHEAASMGHRDCVRYLLGRGAAVDC 101
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 173-311 1.99e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 173 GRTPLHTAAMHGCLEAVKVLLQRGQ----------YQPDCRDRC---GSTPFMDALQCGHIDVARLLLEKHQ--ASASAQ 237
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGAdvhahakgrfFQPKYQGEGfyfGELPLSLAACTNQPDIVQYLLENEHqpADIEAQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 238 DSLGAQAIHRAALTGQN------------EAIRFLVCELGTDVDVRAASGH--LTALHYAAKEGHVSTVQMLLALgaDIN 303
Cdd:cd22193   156 DSRGNTVLHALVTVADNtkentkfvtrmyDMILIRGAKLCPTVELEEIRNNdgLTPLQLAAKMGKIEILKYILQR--EIK 233


                  ....*...
gi 2130994378 304 CKDARNRS 311
Cdd:cd22193   234 EPELRHLS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
58-113 2.52e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 2.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130994378  58 LVESWDMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMA 113
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-132 2.78e-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: 34.87  E-value: 2.78e-03
                           10        20
                   ....*....|....*....|....*..
gi 2130994378  106 DWTPLMMACTRRNLEVIQDLVEHGANP 132
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
278-311 2.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 2.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2130994378 278 TALHYAAKEGHVSTVQMLLALGADINCKDARNRS 311
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLT 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-211 3.32e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 3.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2130994378 168 TESKIGRTPLHTAAMHGCLEAVKVLLQRGQyQPDCRDRCGSTPF 211
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTAL 53
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 41-195 4.08e-03

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: 39.36  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  41 TLLHCAARHGHRDVLaylveswdMDIEAANRDYK--RPLHEAASMGHRDCVRYLLGRGAAVDCLKKADW----------- 107
Cdd:cd22194   115 ILLAFAEENGILDRF--------INAEYTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfy 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 108 ---TPLMMACTRRNLEVIQDLVEHGANPL-LKNKDGWNSVH----VA---SREGDPVILQY--LLTVCPDA--WKTESKI 172
Cdd:cd22194   187 fgeTPLALAACTNQPEIVQLLMEKESTDItSQDSRGNTVLHalvtVAedsKTQNDFVKRMYdmILLKSENKnlETIRNNE 266

                         170       180
                  ....*....|....*....|...
gi 2130994378 173 GRTPLHTAAMHGCLEAVKVLLQR 195
Cdd:cd22194   267 GLTPLQLAAKMGKAEILKYILSR 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 13-94 4.34e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  13 LAQEGRLCALREELRGAGRASCPGPAGDTLLHCAARHGHRDVLAYLVEsWDMDIEAANRDYKRPLHEAASMGHRDCVRYL 92
Cdd:PTZ00322   89 LAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ..
gi 2130994378  93 LG 94
Cdd:PTZ00322  168 SR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 36-195 6.41e-03

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: 38.46  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  36 GPAGDTLLHCAARHGHRDVLAYLVESwdmDIEAANRD-----YK--RPLHEAASMGHRDCVRYLLGRGAAV--------- 99
Cdd:cd22192    48 GALGETALHVAALYDNLEAAVVLMEA---APELVNEPmtsdlYQgeTALHIAVVNQNLNLVRELIARGADVvspratgtf 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 100 -----DCLKKADWTPLMMACTRRNLEVIQDLVEHGANplLKNKDGW-NSV-H--VASREGDPVILQYLLTVCPDAWKTE- 169
Cdd:cd22192   125 frpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgNTVlHilVLQPNKTFACQMYDLILSYDKEDDLq 202

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2130994378 170 ------SKIGRTPLHTAAMHGCLEAVKVLLQR 195
Cdd:cd22192   203 pldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 33-151 8.40e-03

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: 38.14  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  33 SCPGPAGDTLLHCAARHGHRDVLAYLV---------ESWDMDIEAANRDYKR---PLHEAAsmgHRD---CVRYLLGRGA 97
Cdd:TIGR00870  76 SCRGAVGDTLLHAISLEYVDAVEAILLhllaafrksGPLELANDQYTSEFTPgitALHLAA---HRQnyeIVKLLLERGA 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130994378  98 AV-------DCLKKADWT-------PLMMACTRRNLEVIQDLVEHGANPLLKNKDGWNSVHVASREGD 151
Cdd:TIGR00870 153 SVparacgdFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENE 220
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 36-203 9.11e-03

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: 37.94  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378  36 GPAGDTLLHCAA---RHGHRDVLAYLVE---SWDMDIEAANRDY-------KRPLHEAASMGHRDCVRYLLGRGAAV--- 99
Cdd:cd21882    23 GATGKTCLHKAAlnlNDGVNEAIMLLLEaapDSGNPKELVNAPCtdefyqgQTALHIAIENRNLNLVRLLVENGADVsar 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130994378 100 ---DCLKKADWT-------PLMMACTRRNLEVIQDLVEHGANP------------------LLKNKDGWNSVHVASREGd 151
Cdd:cd21882   103 atgRFFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPaaleaqdslgntvlhalvLQADNTPENSAFVCQMYN- 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2130994378 152 pVILQYLLTVCPDAWKTE--SKIGRTPLHTAAMHGCLEAVKVLLQR---GQYQPDCR 203
Cdd:cd21882   182 -LLLSYGAHLDPTQQLEEipNHQGLTPLKLAAVEGKIVMFQHILQRefsGPYQPLSR 237
 
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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