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Conserved domains on  [gi|149242827]
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Chain T, Caspase-2

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-167 4.75e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 4.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVE 97
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  98 VLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQK 167
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-167 4.75e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 4.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVE 97
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  98 VLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQK 167
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-165 1.74e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 130.17  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLHLAA--KTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH--LEIVEVLLKHGAD 105
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149242827 106 VNAK----------------DYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:PHA03100 169 INAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-143 1.19e-30

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 106.74  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   51 LHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHgADVNAKDYeGFTPLHLAAYDGHLEIVE 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 149242827  131 VLLKYGADVNAQD 143
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 18-162 1.14e-19

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: 85.06  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEV-RILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGAD-VN---AWDNY-GATPLHLAADNG 91
Cdd:cd22192   21 LLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmTSDLYqGETALHIAVVNQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  92 HLEIVEVLLKHGADVN--------------AKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNG 157
Cdd:cd22192  101 NLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQP 180


                 ....*
gi 149242827 158 NEDLA 162
Cdd:cd22192  181 NKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 12-141 1.84e-12

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: 64.33  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   12 SDLGKKLLEAARAGQDDEVRILMANGA--DVNATDWLGHTPLHLAAKTG-HLEIVEVLLKYGADVNAwdnyGATPLHLAA 88
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAIS 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827   89 DNGHlEIVEVLLKHGAD----------VNAKD----YEGFTPLHLAAYDGHLEIVEVLLKYGADVNA 141
Cdd:TIGR00870  91 LEYV-DAVEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 79-108 2.07e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 2.07e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 149242827    79 YGATPLHLAADNGHLEIVEVLLKHGADVNA 108
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-167 4.75e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 4.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVE 97
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  98 VLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQK 167
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-165 1.99e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVE 97
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149242827  98 VLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:COG0666  138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-169 6.63e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 6.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVE 97
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149242827  98 VLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN 169
Cdd:COG0666  204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-165 1.74e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 130.17  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLHLAA--KTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH--LEIVEVLLKHGAD 105
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149242827 106 VNAK----------------DYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:PHA03100 169 INAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
 28-162 1.30e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.21  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHLAAKTGH---LEIVEVLLKYGADVNAWDNYGATPLHLAADNGH-LEIVEVLLKHG 103
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149242827 104 ADVNAKDYEGFTPLH--LAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLA 162
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVE 168
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-143 1.19e-30

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 106.74  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   51 LHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHgADVNAKDYeGFTPLHLAAYDGHLEIVE 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 149242827  131 VLLKYGADVNAQD 143
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-165 1.38e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.96  E-value: 1.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  13 DLGKKLLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH 92
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149242827  93 LEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 28-152 5.86e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 107.80  E-value: 5.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHL---AAKTghLEIVEVLLKYGADVNAWDNYGATPLH--LAADNGHLEIVEVLLKH 102
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLylyNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149242827 103 GADVNAKDYEGFTPLH--LAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDI 152
Cdd:PHA03095 142 GADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHH 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
18-110 5.61e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 97.11  E-value: 5.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYgADVNAWDNyGATPLHLAADNGHLEIVE 97
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 149242827   98 VLLKHGADVNAKD 110
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-150 9.25e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 9.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVE 97
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149242827  98 VLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAF 150
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-145 2.47e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.82  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLHLAAKTGH--LEIVEVLLKYGADVNAW----------------DNYGATPLHLAADNG 91
Cdd:PHA03100 124 VEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNN 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 149242827  92 HLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKF 145
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-168 7.15e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 7.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  31 RILMaNGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH-----LEIVEVLLKHGAD 105
Cdd:PHA03100  20 YIIM-EDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGAN 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149242827 106 VNAKDYEGFTPLHLAAYD--GHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLaEILQKL 168
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-KILKLL 162
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-148 7.65e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 93.79  E-value: 7.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  13 DLGKKLLEAARAGQD-DEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADN- 90
Cdd:PHA02878 166 HKGNTALHYATENKDqRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYc 245

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149242827  91 GHLEIVEVLLKHGADVNAKDY-EGFTPLHLAAYDGhlEIVEVLLKYGADVNAQDKFGKT 148
Cdd:PHA02878 246 KDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLT 302
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-169 2.86e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 2.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPLHLAADNGH---LEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGH-LEIVEVLLKY 135
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 149242827 136 GADVNAQDKFGKTAFDI--SIDNGNEDLAEILQKLN 169
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKG 142
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-154 6.88e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.79  E-value: 6.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  26 QDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGAD 105
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 149242827 106 VNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISI 154
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-149 2.39e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.31  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLH--LAAKTGHLEIVEVLLKYGADVNAWDNYGATPLH--LAADNGHLEIVEVLLKHGAD 105
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGAD 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149242827 106 VNAKDYEGFTPLHLaaydgHLE-------IVEVLLKYGADVNAQDKFGKTA 149
Cdd:PHA03095 180 VYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTP 225
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-154 2.61e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 89.55  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDW-LGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNA 108
Cdd:PHA02878 150 TKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 149242827 109 KDYEGFTPLHLA-AYDGHLEIVEVLLKYGADVNAQDKF-GKTAFDISI 154
Cdd:PHA02878 230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSI 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 14-102 7.11e-21

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 88.42  E-value: 7.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  14 LGKKLLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHL 93
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*....
gi 149242827  94 EIVEVLLKH 102
Cdd:PTZ00322 162 EVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-165 1.52e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   84 LHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYgADVNAQDKfGKTAFDISIDNGNEDLAE 163
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 149242827  164 IL 165
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-118 1.74e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 1.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVN 107
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                         90
                 ....*....|....*
gi 149242827 108 AKD----YEGFTPLH 118
Cdd:PHA03100 253 TIIetllYFKDKDLN 267
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 18-148 3.35e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.66  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHL-EIVEVLLKYGADVNAWDNYGATPLHLAADNGH-LEI 95
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 149242827  96 VEVLLKHGADVNAKDYEGFTPLHLAA-YDGHLEIVEVLLKYGADVNAQDKFGKT 148
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKT 377
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-167 5.33e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.43  E-value: 5.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  13 DLGKKLLEAARAGQDDEVRILMANGADVNATDWL-GHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNG 91
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827  92 HLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGK-TAFDISIDNGNEDLAEILQK 167
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 18-162 1.14e-19

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: 85.06  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEV-RILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGAD-VN---AWDNY-GATPLHLAADNG 91
Cdd:cd22192   21 LLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmTSDLYqGETALHIAVVNQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  92 HLEIVEVLLKHGADVN--------------AKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNG 157
Cdd:cd22192  101 NLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQP 180


                 ....*
gi 149242827 158 NEDLA 162
Cdd:cd22192  181 NKTFA 185
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-148 2.13e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.34  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  22 ARAGQDDE-VRILMANGADVNATDWLGHTPLHLAAKTG-HLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVL 99
Cdd:PHA02876 315 AKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 149242827 100 LKHGADVNAKDYEGFTPLHLAAYDGHLEI-VEVLLKYGADVNAQDKFGKT 148
Cdd:PHA02876 395 LDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLST 444
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-155 2.69e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  21 AARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLL 100
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149242827 101 KHGADVNAKDYEGFTPLHLAAYdgHLEIVEVLLKYGADVNAQDKFGKTAFDISID 155
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAIN 263
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 85-165 2.83e-19

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 83.79  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  85 HLAAdNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEI 164
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 .
gi 149242827 165 L 165
Cdd:PTZ00322 167 L 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-158 1.05e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.93  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVL-----------------------LKYGADVN 74
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGIDVN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  75 AWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISI 154
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198


                 ....
gi 149242827 155 DNGN 158
Cdd:PHA02874 199 EYGD 202
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-165 3.08e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.07  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  54 AAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPL-------H-------- 118
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrily 611

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149242827 119 ----------------LAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:PLN03192 612 hfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-148 4.48e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.49  E-value: 4.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  26 QDDEVRI---LMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVN---------------------------- 74
Cdd:PHA02876 154 QQDELLIaemLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecavdsknidtikaiidn 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  75 ----------------------------------AWDNYGATPLHLAADNGHL-EIVEVLLKHGADVNAKDYEGFTPLHL 119
Cdd:PHA02876 234 rsninkndlsllkairnedletslllydagfsvnSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313

                        170       180       190
                 ....*....|....*....|....*....|
gi 149242827 120 AAYDGH-LEIVEVLLKYGADVNAQDKFGKT 148
Cdd:PHA02876 314 MAKNGYdTENIRTLIMLGADVNAADRLYIT 343
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-161 5.07e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 5.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLH--LAAKTGHLEIVEVLLKYGADV---------------------------------- 73
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVyavddrfrsllhhhlqsfkprarivreliragcd 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  74 -NAWDNYGATPLHLAADNGHLE--IVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAF 150
Cdd:PHA03095 215 pAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                        170
                 ....*....|.
gi 149242827 151 DISIDNGNEDL 161
Cdd:PHA03095 295 SLMVRNNNGRA 305
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 52-135 8.16e-18

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 79.56  E-value: 8.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  52 HLAAkTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEV 131
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ....
gi 149242827 132 LLKY 135
Cdd:PTZ00322 167 LSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-167 9.42e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.53  E-value: 9.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPL-------H----- 85
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifr 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  86 -------------------LAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADV---NAQD 143
Cdd:PLN03192 609 ilyhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDD 688

                        170       180
                 ....*....|....*....|....
gi 149242827 144 KFGKTafdisidngneDLAEILQK 167
Cdd:PLN03192 689 DFSPT-----------ELRELLQK 701
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 18-165 1.66e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 1.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGA--DVNAWD------------------ 77
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDieselhdaveegdvkave 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  78 --------------NYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQD 143
Cdd:PHA02875  86 elldlgkfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                        170       180
                 ....*....|....*....|..
gi 149242827 144 KFGKTAFDISIDNGNEDLAEIL 165
Cdd:PHA02875 166 CCGCTPLIIAMAKGDIAICKML 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-165 2.26e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 2.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  27 DDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADV 106
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149242827 107 NAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-139 1.15e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGAD----------------------------------V 73
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiealsqkigtalhfalcgtnpymsvktlidrganV 435

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827  74 NAWDNYGATPLHLAA-DNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAydGHLEIVEVLLKYGADV 139
Cdd:PHA02876 436 NSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-140 1.58e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVN 107
Cdd:PHA02875 116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149242827 108 AKDYEG-FTPLHLAAYDGHLEIVEVLLKYGADVN 140
Cdd:PHA02875 196 YFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 18-154 2.05e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHL------------------------------------- 60
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKlgmkemirsinkcsvfytlvaikdafnnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  61 ---------------------------EIVEVLLKYGADVNAWD-NYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYE 112
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 149242827 113 GFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISI 154
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
PHA02798 PHA02798
ankyrin-like protein; Provisional
 28-151 2.13e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 69.86  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPL-----HLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH---LEIVEVL 99
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFM 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149242827 100 LKHGADVNAKDYEGFTPLHLAAYDGH---LEIVEVLLKYGADVNA-QDKFGKTAFD 151
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLH 187
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 18-120 3.19e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLA-AKTGHLEIVEVLLKYGADVNAWDN-YGATPLHLAADNGhlEI 95
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RK 282

                         90       100
                 ....*....|....*....|....*
gi 149242827  96 VEVLLKHGADVNAKDYEGFTPLHLA 120
Cdd:PHA02878 283 LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02798 PHA02798
ankyrin-like protein; Provisional
 60-165 4.35e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 68.71  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPL-----HLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGH---LEIVEV 131
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 149242827 132 LLKYGADVNAQDKFGKTAFDISIDNGNE---DLAEIL 165
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-133 7.98e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 7.98e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 149242827   82 TPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLL 133
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-100 1.03e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 1.03e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 149242827   47 GHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLL 100
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-165 1.14e-13

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: 67.73  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  49 TPLHLAAKTGHLEIVEVLLKY-GADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGAD-VN----AKDYEGFTPLHLAAY 122
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtSDLYQGETALHIAVV 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149242827 123 DGHLEIVEVLLKYGADVNAQDKFGkTAFDISIDN---------------GNEDLAEIL 165
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATG-TFFRPGPKNliyygehplsfaacvGNEEIVRLL 155
PHA02946 PHA02946
ankyin-like protein; Provisional
 30-147 1.35e-13

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 67.39  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHL--AADNGHLEIVEVLLKHGADV- 106
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIn 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 149242827 107 NAKDYEGFTPLhLAAYDGHLEIVEVLLKYGADVNAQDKFGK 147
Cdd:PHA02946 135 NSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGK 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
99-152 2.17e-13

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 61.21  E-value: 2.17e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 149242827   99 LLKHG-ADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDI 152
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 12-141 1.84e-12

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: 64.33  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   12 SDLGKKLLEAARAGQDDEVRILMANGA--DVNATDWLGHTPLHLAAKTG-HLEIVEVLLKYGADVNAwdnyGATPLHLAA 88
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAIS 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827   89 DNGHlEIVEVLLKHGAD----------VNAKD----YEGFTPLHLAAYDGHLEIVEVLLKYGADVNA 141
Cdd:TIGR00870  91 LEYV-DAVEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02798 PHA02798
ankyrin-like protein; Provisional
 28-160 2.65e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.70  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHLAAKTGH---LEIVEVLLKYGADVNAWDNYGATPLHLAADNGH---LEIVEVLLK 101
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149242827 102 HGADVNA-KDYEGFTPLHL---AAYDG-HLEIVEVLLKYGADVNAQDKFGKTAF-----DISIDNGNED 160
Cdd:PHA02798 170 KGVDINThNNKEKYDTLHCyfkYNIDRiDADILKLFVDNGFIINKENKSHKKKFmeylnSLLYDNKRFK 238
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-134 3.79e-12

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: 63.11  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  12 SDL--GKKLLEAARAGQDDE-VRILMANGADVN---ATD-----------WLGHTPLHLAAKTGHLEIVEVLLKYGADVN 74
Cdd:cd22192   84 SDLyqGETALHIAVVNQNLNlVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIR 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  75 AWDNYGATPLHL----AADNGHLEIVEVLLKHGADVNA------KDYEGFTPLHLAAYDGHLEIVEVLLK 134
Cdd:cd22192  164 AQDSLGNTVLHIlvlqPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 26-133 4.08e-12

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: 63.24  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  26 QDDEVRILMANGADVNATD--------------WLGHTPLHLAAKTGHLEIVEVLL-KYGADVNAWDNYGATPLH---LA 87
Cdd:cd22194  153 QGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTV 232

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149242827  88 ADNGH------LEIVEVLLKHGADVN---AKDYEGFTPLHLAAYDGHLEIVEVLL 133
Cdd:cd22194  233 AEDSKtqndfvKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
66-120 4.83e-12

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 57.74  E-value: 4.83e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 149242827   66 LLKYG-ADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLA 120
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 13-121 1.16e-11

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: 62.02  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827   13 DLGKKLLEAARAGQDDEV----RILMANGAD------VNATD----WLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDN 78
Cdd:TIGR00870  80 AVGDTLLHAISLEYVDAVeailLHLLAAFRKsgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPARAC 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827   79 --------------YGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAA 121
Cdd:TIGR00870 160 gdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 16-148 1.27e-11

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: 61.70  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  16 KKLLEAARAGQDDEVRILMANGADVN-------ATDWLGHtplHLAAK-TGHL--------------EIVEVLLKYGADV 73
Cdd:cd22194   47 KKRLKKVSEAAVEELGELLKELKDLSrrrrktdVPDFLMH---KLTASdTGKTclmkallninentkEIVRILLAFAEEN 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  74 NAWD----------NY-GATPLHLAADNGHLEIVEVLLKHGADVNAK----------DYEGF----TPLHLAAYDGHLEI 128
Cdd:cd22194  124 GILDrfinaeyteeAYeGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI 203

                        170       180
                 ....*....|....*....|.
gi 149242827 129 VEVLL-KYGADVNAQDKFGKT 148
Cdd:cd22194  204 VQLLMeKESTDITSQDSRGNT 224
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-160 1.59e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.59e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149242827  93 LEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNED 160
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNID 225
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 50-165 3.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  50 PLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAA----------------------------------------- 88
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  89 -----------------------DNGHLEIVEVLLKHGADVNAKD-YEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDK 144
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskdDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180
                 ....*....|....*....|.
gi 149242827 145 FGKTAFDISIDNGNEDLAEIL 165
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHIL 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
38-87 9.65e-11

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 9.65e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 149242827   38 ADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLA 87
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-139 1.49e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKH--GADVN 107
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKnpSAETV 319

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149242827 108 AKDYEGFTPLHLAAY-DGHLEIV-EVLLKYGADV 139
Cdd:PHA03095 320 AATLNTASVAGGDIPsDATRLCVaKVVLRGAFSL 353
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 30-157 1.94e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 57.14  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVN-ATDWLGHTPLHLAA---KTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH--LEIVEVLLKHG 103
Cdd:PHA02859  69 LKFLIENGADVNfKTRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNvrINVIKLLIDSG 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149242827 104 ADVNAKDYEGFTPLH-LAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNG 157
Cdd:PHA02859 149 VSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-165 3.56e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 3.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 149242827  115 TPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 33-158 4.11e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  33 LMANGADVNATDWLGHTPLHLAAKTGH---LEIVEVLLKYGADVNAWDN-YGATPLH----------------LAADNGH 92
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNkEKYDTLHcyfkynidridadilkLFVDNGF 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  93 L----------------------------EIVEVLLKHgADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDK 144
Cdd:PHA02798 211 IinkenkshkkkfmeylnsllydnkrfkkNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                        170
                 ....*....|....
gi 149242827 145 FGKTAFDISIDNGN 158
Cdd:PHA02798 290 LGNTCLFTAFENES 303
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-159 6.32e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 6.32e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827  86 LAADNGHLEIVEVLLKHGADVNAKDYEGFTPLH-LAAYDGH--LEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNE 159
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlYLHYSSEkvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 47-169 9.22e-10

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: 56.43  E-value: 9.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  47 GHTPLHLAA---KTGHLEIVEVLLKYGAD-------VNA--WDNY--GATPLHLAADNGHLEIVEVLLKHGADVNAKD-- 110
Cdd:cd21882   26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDsgnpkelVNApcTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149242827 111 -----------YEGFTPLHLAAYDGHLEIVEVLLKYGAD---VNAQDKFGKTAFDISI---DNGNEDLAEILQKLN 169
Cdd:cd21882  106 rffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALVlqaDNTPENSAFVCQMYN 181
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 73-158 1.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.21  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  73 VNAWDNYGATPLH--LAADNGHLEIVEVLLKHGADVNAK-DYEGFTPLH-LAAYDGHL--EIVEVLLKYGADVNAQDKFG 146
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKtRDNNLSALHhYLSFNKNVepEILKILIDSGSSITEEDEDG 123

                         90
                 ....*....|..
gi 149242827 147 KTAFDISIDNGN 158
Cdd:PHA02859 124 KNLLHMYMCNFN 135
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-165 1.19e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  77 DNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDN 156
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601


                 ....*....
gi 149242827 157 GNEDLAEIL 165
Cdd:PLN03192 602 KHHKIFRIL 610
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 12-118 1.30e-09

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: 55.96  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  12 SDLGKKLLEAA----RAGQDDEVRILMANGAD-------VNA--TD--WLGHTPLHLAAKTGHLEIVEVLLKYGADVNAW 76
Cdd:cd22193   26 SSTGKTCLMKAllnlNPGTNDTIRILLDIAEKtdnlkrfINAeyTDeyYEGQTALHIAIERRQGDIVALLVENGADVHAH 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149242827  77 DN--------------YGATPLHLAADNGHLEIVEVLLKHG---ADVNAKDYEGFTPLH 118
Cdd:cd22193  106 AKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH 164
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 30-134 1.50e-09

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: 55.66  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATD-------------WLGHTPLHLAAKTGHLEIVEVLLKYGAD---VNAWDNYGATPLH---LAADN 90
Cdd:cd21882   89 VRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHalvLQADN 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827  91 GH------LEIVEVLLKHGADVN-------AKDYEGFTPLHLAAYDGHLEIVEVLLK 134
Cdd:cd21882  169 TPensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 51-148 1.76e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 55.58  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  51 LHLAAKTGHLEIVevllkygadVNA--WDNY--GATPLHLAADNGHLEIVEVLLKHGADVNAKD--------------YE 112
Cdd:cd22196   70 LDIAEKTGNLKEF---------VNAayTDSYykGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYF 140

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 149242827 113 GFTPLHLAAYDGHLEIVEVLLK---YGADVNAQDKFGKT 148
Cdd:cd22196  141 GELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNT 179
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-150 2.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  21 AARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLA------------- 87
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnrsaiellin 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  88 ------AD-NGH------------LEIVEVLLKHGADVNAKDYEGFTPLHLA-AYDGHLEIVEVLLKYGADVNAQDKFGK 147
Cdd:PHA02874 244 nasindQDiDGStplhhainppcdIDIIDILLYHKADISIKDNKGENPIDTAfKYINKDPVIKDIIANAVLIKEADKLKD 323


                 ...
gi 149242827 148 TAF 150
Cdd:PHA02874 324 SDF 326
PHA02946 PHA02946
ankyin-like protein; Provisional
 21-154 2.92e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.67  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  21 AARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGH--LEIVEVLLKYGADVN-AWDNYGATPL------------- 84
Cdd:PHA02946  79 ASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINnSVDEEGCGPLlactdpservfkk 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  85 ---------------------HLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYD--GHLEIVEVLLKyGADVNA 141
Cdd:PHA02946 159 imsigfearivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNK 237

                        170
                 ....*....|...
gi 149242827 142 QDKFGKTAFDISI 154
Cdd:PHA02946 238 QNKFGDSPLTLLI 250
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 28-120 3.99e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 54.22  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGH----TPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGA-TPLHLAADNGHLEIVEVLLKH 102
Cdd:PHA02884  47 DIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                         90
                 ....*....|....*...
gi 149242827 103 GADVNAKDYEGFTPLHLA 120
Cdd:PHA02884 127 GADINIQTNDMVTPIELA 144
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 51-165 4.70e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 53.83  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  51 LHLAAKTGHLEIVEVLLKYGADVNAW----DNYGATPLHLAADNGHLEIVEVLLKHGADVNA-KDYEGFTPLHLAAYDGH 125
Cdd:PHA02884  37 LYSSIKFHYTDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGC 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 149242827 126 LEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:PHA02884 117 LKCLEILLSYGADINIQTNDMVTPIELALMICNNFLAFMI 156
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 28-140 4.78e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 54.36  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATdWLGHTPL--HLAAKTGHLEIVEVLLKYGADVNaWDNYGATPL------HLAADNGHLEIVEVL 99
Cdd:PHA02989  17 NALEFLLRTGFDVNEE-YRGNSILllYLKRKDVKIKIVKLLIDNGADVN-YKGYIETPLcavlrnREITSNKIKKIVKLL 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 149242827 100 LKHGADVNAKDYEGFTPLHLAAYDGH---LEIVEVLLKYGADVN 140
Cdd:PHA02989  95 LKFGADINLKTFNGVSPIVCFIYNSNinnCDMLRFLLSKGINVN 138
Ank_4 pfam13637
Ankyrin repeats (many copies);
18-67 8.78e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 8.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 149242827   18 LLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLL 67
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 30-134 1.87e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 52.50  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATD--------------WLGHTPLHLAAKTGHLEIVEVLLK---YGADVNAWDNYGATPLHL---AAD 89
Cdd:cd22196  110 VELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHAlveVAD 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149242827  90 NGHLEIVEV------LLKHGADVNAK-------DYEGFTPLHLAAYDGHLEIVEVLLK 134
Cdd:cd22196  190 NTPENTKFVtkmyneILILGAKIRPLlkleeitNKKGLTPLKLAAKTGKIGIFAYILG 247
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-165 2.78e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.14  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  85 HLAADNGHLEIVEVLLKHGADVNAKDYEGFTPL-----HLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNE 159
Cdd:PHA02798  43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYI 122


                 ....*.
gi 149242827 160 DLAEIL 165
Cdd:PHA02798 123 NNLEIL 128
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 79-110 4.06e-08

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 4.06e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 149242827   79 YGATPLHLAAD-NGHLEIVEVLLKHGADVNAKD 110
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-144 4.41e-08

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 4.41e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 149242827  112 EGFTPLHLAAYD-GHLEIVEVLLKYGADVNAQDK 144
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 25-118 4.50e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 51.35  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  25 GQDDEVRILM--ANGAD-----VNA--TD--WLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDN--------------Y 79
Cdd:cd22196   61 GQNDTISLLLdiAEKTGnlkefVNAayTDsyYKGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyF 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149242827  80 GATPLHLAADNGHLEIVEVLLKH---GADVNAKDYEGFTPLH 118
Cdd:cd22196  141 GELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLH 182
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 28-104 5.34e-08

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.49  E-value: 5.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149242827  28 DEVRILMANGADVNATDWL-GHTPLHLAAKTGHLEIVEVLLKY-GADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGA 104
Cdd:PHA02736  72 EKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02741 PHA02741
hypothetical protein; Provisional
 47-168 5.65e-08

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 49.66  E-value: 5.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  47 GHTPLHLAAKTGHLEIVEVLLKY------GADVNAWDNYGATPLHLAADNGH----LEIVEVLLKHGADVNAKD-YEGFT 115
Cdd:PHA02741  21 GENFFHEAARCGCFDIIARFTPFirgdchAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEmLEGDT 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 149242827 116 PLHLAAYDGHLEIVEVLLKY-GADVNAQDKFGKTAFDISIDNGNEDLAEILQKL 168
Cdd:PHA02741 101 ALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQILREI 154
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 40-146 6.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.20  E-value: 6.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  40 VNATDWLGHTPLH--LAAKTGHLEIVEVLLKYGADVN-AWDNYGATPLHLAA---DNGHLEIVEVLLKHGADVNAKDYEG 113
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNfKTRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 149242827 114 FTPLH--LAAYDGHLEIVEVLLKYGADVNAQDKFG 146
Cdd:PHA02859 124 KNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDN 158
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 30-134 6.53e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 51.01  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADVNATD-------------WLGHTPLHLAAKTGHLEIVEVLLKYGAD---VNAWDNYGATPLH---LAADN 90
Cdd:cd22197  110 VKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHalvMIADN 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827  91 G--HLEIV----EVLLKHGADVNAK-------DYEGFTPLHLAAYDGHLEIVEVLLK 134
Cdd:cd22197  190 SpeNSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHILQ 246
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 26-134 1.18e-07

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: 50.18  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  26 QDDEVRILMANGADVNATD--------------WLGHTPLHLAAKTGHLEIVEVLLKYG---ADVNAWDNYGATPLH--- 85
Cdd:cd22193   88 QGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLHalv 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149242827  86 LAADNGH------LEIVEVLLKHGADVNA-------KDYEGFTPLHLAAYDGHLEIVEVLLK 134
Cdd:cd22193  168 TVADNTKentkfvTRMYDMILIRGAKLCPtveleeiRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 47-78 1.77e-07

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: 45.36  E-value: 1.77e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 149242827   47 GHTPLHLAA-KTGHLEIVEVLLKYGADVNAWDN 78
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 79-108 2.07e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 2.07e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 149242827    79 YGATPLHLAADNGHLEIVEVLLKHGADVNA 108
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 47-75 3.18e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 3.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 149242827    47 GHTPLHLAAKTGHLEIVEVLLKYGADVNA 75
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 79-108 4.27e-07

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: 44.17  E-value: 4.27e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 149242827   79 YGATPLHLAADNGHLEIVEVLLKHGADVNA 108
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 80-148 5.29e-07

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: 48.25  E-value: 5.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  80 GATPLHLAADNGHLEIVEVLLKHGADVNA----------KDYEGF----TPLHLAAYDGHLEIVEVLLKYG---ADVNAQ 142
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrffqpkYQGEGFyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155


                 ....*.
gi 149242827 143 DKFGKT 148
Cdd:cd22193  156 DSRGNT 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 112-141 6.06e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 6.06e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 149242827   112 EGFTPLHLAAYDGHLEIVEVLLKYGADVNA 141
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 20-137 6.27e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.96  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  20 EAARAGQDDEVRILM------ANGADVNATDWLGHTPLHLAAKTGH----LEIVEVLLKYGADVNAWDNY-GATPLHLAA 88
Cdd:PHA02741  27 EAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMLeGDTALHLAA 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 149242827  89 DNGHLEIVEVLLKH-GADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGA 137
Cdd:PHA02741 107 HRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVA 156
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-107 6.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  21 AARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYG-ATPLHLAADNGHLEIVEVL 99
Cdd:PHA02875 142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221


                 ....*...
gi 149242827 100 LKHGADVN 107
Cdd:PHA02875 222 IKRGADCN 229
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 28-117 1.98e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.83  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLH--LAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHL-------------AADNG- 91
Cdd:PHA02716 298 SVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildpETDNDi 377

                         90       100
                 ....*....|....*....|....*.
gi 149242827  92 HLEIVEVLLKHGADVNAKDYEGFTPL 117
Cdd:PHA02716 378 RLDVIQCLISLGADITAVNCLGYTPL 403
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-165 3.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  57 TGHLEIVEVLLKYGAD-VNAWDNYGATPLHLAADNGHLEIVEVLLKHGAD------------------------------ 105
Cdd:PHA02874  11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADinhintkiphplltaikigahdiikllidn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827 106 --------------------------VNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNE 159
Cdd:PHA02874  91 gvdtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170


                 ....*.
gi 149242827 160 DLAEIL 165
Cdd:PHA02874 171 DIIKLL 176
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-165 3.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  64 EVLLKYGADVNAWDNYGAT-------PLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLA---------------- 120
Cdd:PHA02878  14 ETILKYIEYIDHTENYSTSaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemirsi 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827 121 ----------------------------------------------AYDGHLE--IVEVLLKYGADVNAQDK-FGKTAFD 151
Cdd:PHA02878  94 nkcsvfytlvaikdafnnrnveifkiiltnrykniqtidlvyidkkSKDDIIEaeITKLLLSYGADINMKDRhKGNTALH 173

                        170
                 ....*....|....
gi 149242827 152 ISIDNGNEDLAEIL 165
Cdd:PHA02878 174 YATENKDQRLTELL 187
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-167 3.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  54 AAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGA--DVNAKDYE------------------- 112
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIEselhdaveegdvkaveell 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827 113 -------------GFTPLHLAAYDGHLEIVEVLLKYGA--DVNAQDKFgkTAFDISIDNGNEDLAEILQK 167
Cdd:PHA02875  89 dlgkfaddvfykdGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLID 156
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-141 4.74e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 4.74e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 149242827  112 EGFTPLHLAAYDGHLEIVEVLLKYGADVNA 141
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 47-75 5.20e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 5.20e-06
                          10        20
                  ....*....|....*....|....*....
gi 149242827   47 GHTPLHLAAKTGHLEIVEVLLKYGADVNA 75
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 47-137 5.75e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.10  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  47 GHTPLHLAAKTGHLEIVE---VLLKYGADVNAWDN-YGATPLHLAADNGHLEIVEVLLKH-GADVNAKDYEGFTPLHLAA 121
Cdd:PHA02736  55 GKQCVHIVSNPDKADPQEklkLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134

                         90
                 ....*....|....*.
gi 149242827 122 YDGHLEIVEVLLKYGA 137
Cdd:PHA02736 135 ERHDAKMMNILRAKGA 150
PHA02795 PHA02795
ankyrin-like protein; Provisional
 60-134 8.36e-06

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 44.60  E-value: 8.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDG--------HLEIVEV 131
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEI 280


                 ...
gi 149242827 132 LLK 134
Cdd:PHA02795 281 LLR 283
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 47-118 9.20e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.85  E-value: 9.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  47 GHTPLHLAAKTGHLEIVEVLLKYGADVNAWDN-------------YGATPLHLAADNGHLEIVEVLLKHGAD---VNAKD 110
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQpasLQAQD 173


                 ....*...
gi 149242827 111 YEGFTPLH 118
Cdd:cd22197  174 SLGNTVLH 181
PHA02795 PHA02795
ankyrin-like protein; Provisional
 93-158 9.28e-06

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 44.60  E-value: 9.28e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149242827  93 LEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGN 158
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGS 266
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 55-140 1.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.96  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  55 AKTGHLEIVEVLLKYGADVNA-WDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGfTPLHLAAYDGHL------E 127
Cdd:PHA02989  11 SDTVDKNALEFLLRTGFDVNEeYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREItsnkikK 89

                         90
                 ....*....|...
gi 149242827 128 IVEVLLKYGADVN 140
Cdd:PHA02989  90 IVKLLLKFGADIN 102
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 63-137 1.79e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 42.88  E-value: 1.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149242827  63 VEVLLKYGADVNAWD-NYGATPLHLAADNGHLEIVEVLLKH-GADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGA 137
Cdd:PHA02743  76 IELLVNMGADINARElGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 96-169 1.91e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.50  E-value: 1.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149242827  96 VEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAfdISIDNGNEDlaEILQKLN 169
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP--LYYLSGTDD--EVIERIN 124
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 29-104 3.34e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 42.11  E-value: 3.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149242827  29 EVRILMANGADVNATDWL-GHTPLHLAAKTGHLEIVEVLLK-YGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGA 104
Cdd:PHA02743  75 KIELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRqLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 28-166 3.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.81  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADV-NATDWLGHTPLHLAAKTG----HLEIVEVLLKYGADVNAWDNYGATPLHLAADNGH------LEIV 96
Cdd:PHA02989 161 DVIKILLSFGVNLfEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLESFLDNNKilskkeFKVL 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149242827  97 EVLLKHgADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNED-LAEILQ 166
Cdd:PHA02989 241 NFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDmLNRILQ 310
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 73-167 5.63e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  73 VNAWDNYGATPLHLAADNGHLEIVE---VLLKHGADVNAKD-YEGFTPLHLAAYDGHLEIVEVLLKY-GADVNAQDKFGK 147
Cdd:PHA02736  48 VLEYNRHGKQCVHIVSNPDKADPQEklkLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFK 127

                         90       100
                 ....*....|....*....|
gi 149242827 148 TAFDISIDNGNEDLAEILQK 167
Cdd:PHA02736 128 TPYYVACERHDAKMMNILRA 147
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 15-84 9.25e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 9.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149242827  15 GKKLLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADV---NAWDNYGATPL 84
Cdd:PLN03192 623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
PHA02795 PHA02795
ankyrin-like protein; Provisional
 39-101 3.52e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.98  E-value: 3.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149242827  39 DVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNG--------HLEIVEVLLK 101
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLR 283
PHA02917 PHA02917
ankyrin-like protein; Provisional
 60-133 4.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.60  E-value: 4.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDG-HLEIVEVLL 133
Cdd:PHA02917 432 LSTINICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESrNIELLKMLL 506
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 60-165 5.01e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPLHLAA----DNGHLEIvEVLLKHGADVNAKDYE-GFTPLHLAAYDGHLEIVEVLLK 134
Cdd:PHA02743  37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAwydrANAVMKI-ELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCR 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 149242827 135 -YGADVNAQDKFGKTAFDISIDNGNEDLAEIL 165
Cdd:PHA02743 116 qLGVNLGAINYQHETAYHIAYKMRDRRMMEIL 147
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 60-148 5.09e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.51  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPLH--LAADNGHLEIVEVLLKHGADVNAKDYEGFTPLH--------LAAYDG----- 124
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvVNILDPetdnd 376

                         90       100
                 ....*....|....*....|....*
gi 149242827 125 -HLEIVEVLLKYGADVNAQDKFGKT 148
Cdd:PHA02716 377 iRLDVIQCLISLGADITAVNCLGYT 401
PHA02792 PHA02792
ankyrin-like protein; Provisional
 61-154 6.27e-04

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 39.16  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  61 EIVEVLLKYGADVNAWDNYGAT-----PLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKY 135
Cdd:PHA02792 353 KVVEYILKNGNVVVEDDDNIINimplfPTLSIHESDVLSILKLCKPYIDDINKIDKHGRSILYYCIESHSVSLVEWLIDN 432

                         90
                 ....*....|....*....
gi 149242827 136 GADVNAQDKFGKTAFDISI 154
Cdd:PHA02792 433 GADINITTKYGSTCIGICV 451
PHA02791 PHA02791
ankyrin-like protein; Provisional
 77-169 1.14e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.10  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  77 DNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEgfTPLHLAAYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDN 156
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90
                 ....*....|...
gi 149242827 157 GNEDLAEILQKLN 169
Cdd:PHA02791 105 GNMQTVKLFVKKN 117
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 28-124 1.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLH--LAAKTGHLEIVEVLLKYGADVNAWDNYGATPLH----LAADNghlEIVEVLLK 101
Cdd:PHA02859 104 EILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyilFHSDK---KIFDFLTS 180

                         90       100
                 ....*....|....*....|...
gi 149242827 102 HGADVNAKDYEGFTPLHLAAYDG 124
Cdd:PHA02859 181 LGIDINETNKSGYNCYDLIKFRN 203
PHA02791 PHA02791
ankyrin-like protein; Provisional
 50-101 1.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.10  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149242827  50 PLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLK 101
Cdd:PHA02791  64 PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK 115
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 47-118 1.58e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 38.29  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  47 GHTPLHLAAKTGHLEIVEVLLKYGADVNA--------------WDNYGATPLHLAADNGHLEIVEVLLKHG---ADVNAK 109
Cdd:cd22195  137 GQTALHIAIERRCKHYVELLVEKGADVHAqargrffqpkdeggYFYFGELPLSLAACTNQPDIVHYLTENAhkkADLRRQ 216


                 ....*....
gi 149242827 110 DYEGFTPLH 118
Cdd:cd22195  217 DSRGNTVLH 225
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 28-148 1.67e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 37.97  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  28 DEVRILMANGADVNATDWLGHTPLHLAAKTGHL--EIVEVLLKYGADVNAWDNYGATP---------------------- 83
Cdd:PHA02716 193 DILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPimtyiinidninpeitniyies 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  84 ------------LHL---AADNGHLEIVEVLLKHGADVNAKDYEGFTPLH--LAAYDGHLEIVEVLLKYGADVNAQDKFG 146
Cdd:PHA02716 273 ldgnkvknipmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIG 352


                 ..
gi 149242827 147 KT 148
Cdd:PHA02716 353 NT 354
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 80-148 1.75e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 37.91  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  80 GATPLHLAADNGHLEIVEVLLKHGADVNA---------KD-----YEGFTPLHLAAYDGHLEIVEVLLKYG---ADVNAQ 142
Cdd:cd22195  137 GQTALHIAIERRCKHYVELLVEKGADVHAqargrffqpKDeggyfYFGELPLSLAACTNQPDIVHYLTENAhkkADLRRQ 216


                 ....*.
gi 149242827 143 DKFGKT 148
Cdd:cd22195  217 DSRGNT 222
PHA02798 PHA02798
ankyrin-like protein; Provisional
 39-111 2.35e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 2.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149242827  39 DVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDY 111
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISY 322
PHA02917 PHA02917
ankyrin-like protein; Provisional
 39-102 2.78e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 37.28  E-value: 2.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149242827  39 DVNATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNG-HLEIVEVLLKH 102
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESrNIELLKMLLCH 508
PHA02730 PHA02730
ankyrin-like protein; Provisional
 60-150 3.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 165098 [Multi-domain]  Cd Length: 672  Bit Score: 37.31  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  60 LEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGF-TPLHLAAY--DGHLEIVEVLLKYG 136
Cdd:PHA02730 442 IDVFDILSKYMDDIDMIDNENKTLLYYAVDVNNIQFARRLLEYGASVNTTSRSIInTAIQKSSYrrENKTKLVDLLLSYH 521

                         90
                 ....*....|....*
gi 149242827 137 ADVNAQ-DKFGKTAF 150
Cdd:PHA02730 522 PTLETMiDAFNRDIR 536
PHA02792 PHA02792
ankyrin-like protein; Provisional
 30-134 4.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 36.47  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149242827  30 VRILMANGADV-----NATDWLGHTPLHLAAKTGHLEIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGA 104
Cdd:PHA02792 355 VEYILKNGNVVvedddNIINIMPLFPTLSIHESDVLSILKLCKPYIDDINKIDKHGRSILYYCIESHSVSLVEWLIDNGA 434

                         90       100       110
                 ....*....|....*....|....*....|...
gi 149242827 105 DVNAKDYEGFTPLHLAAYDGHL---EIVEVLLK 134
Cdd:PHA02792 435 DINITTKYGSTCIGICVILAHAcipEIAELYIK 467
PHA02798 PHA02798
ankyrin-like protein; Provisional
 62-140 5.16e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 36.35  E-value: 5.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149242827  62 IVEVLLKYgADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLAAYDGHLEIVEVLLKYGADVN 140
Cdd:PHA02798 241 ILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
 
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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