NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|309269136|ref|XP_001476038|]
View 

putative POTE ankyrin domain family member M isoform X2 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 1.92e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 1.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 1.92e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 1.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
89-180 1.47e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.96  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136   89 LHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHnADPNLIDfSGNTALHHAISRGNLRIVK 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 309269136  169 MLLEHNVDIEAK 180
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-191 1.41e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  78 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHH 157
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110
                 ....*....|....*....|....*....|....
gi 309269136 158 AISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 54-205 8.61e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 8.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLEN-----NSSINIRDDEGCTPLIKATQR 128
Cdd:cd22192   20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 129 DNVDCASVLLTHNADP---------------NLIDFsGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQ-LAT 192
Cdd:cd22192  100 QNLNLVRELIARGADVvspratgtffrpgpkNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVL 178

                        170
                 ....*....|....*.
gi 309269136 193 FEQKP---EMVEFLAA 205
Cdd:cd22192  179 QPNKTfacQMYDLILS 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-179 6.26e-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: 45.27  E-value: 6.26e-07
                           10        20
                   ....*....|....*....|....*....
gi 309269136   151 GNTALHHAISRGNLRIVKMLLEHNVDIEA 179
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 57-180 1.86e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136   57 RAASVGDLDTTEKLIHSSQH-HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSiniRDDEGCTPLIKATQR--DNV-D 132
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISLEyvDAVeA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 309269136  133 CASVLLTHNA---------DPNLIDFS-GNTALHHAISRGNLRIVKMLLEHNVDIEAK 180
Cdd:TIGR00870 100 ILLHLLAAFRksgplelanDQYTSEFTpGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 1.92e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 1.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 1.55e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-206 9.05e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 9.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIhssQHH--VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV 131
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLL---EAGadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309269136 132 DCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAK 206
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-208 2.99e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  55 LQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCA 134
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309269136 135 SVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCA 208
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
89-180 1.47e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.96  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136   89 LHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHnADPNLIDfSGNTALHHAISRGNLRIVK 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 309269136  169 MLLEHNVDIEAK 180
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-188 1.29e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIhssQH--HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV 131
Cdd:COG0666  156 PLHLAAANGNLEIVKLLL---EAgaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 309269136 132 DCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:COG0666  233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-206 9.20e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 9.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  122 LIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHnVDIEAKTeYGLTPLQLATFEQKPEMVE 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*
gi 309269136  202 FLAAK 206
Cdd:pfam12796  79 LLLEK 83
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-191 1.41e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  78 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHH 157
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110
                 ....*....|....*....|....*....|....
gi 309269136 158 AISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-148 2.02e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136   55 LQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSsINIRDDeGCTPLIKATQRDNVDCA 134
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 309269136  135 SVLLTHNADPNLID 148
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-206 2.41e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  70 LIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDF 149
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 309269136 150 SGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAK 206
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-203 1.68e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.09  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  68 EKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-----IKATQRDNVDCASVLLTHNA 142
Cdd:PHA03100  18 IKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGA 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309269136 143 DPNLIDFSGNTALHHAISR--GNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKP--EMVEFL 203
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLL 162
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-191 1.39e-13

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 64.67  E-value: 1.39e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136  137 LLTH-NADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 99-183 1.14e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIE 178
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....*
gi 309269136 179 AKTEY 183
Cdd:PHA03100 253 TIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 58-219 1.55e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  58 AASVGDLDTTEKLIHSSQHhVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVL 137
Cdd:PLN03192 532 VASTGNAALLEELLKAKLD-PDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 138 --LTHNADPNlidfSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLA---AKCAKSSV 212
Cdd:PLN03192 611 yhFASISDPH----AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImngADVDKANT 686


                 ....*..
gi 309269136 213 TPSWSPS 219
Cdd:PLN03192 687 DDDFSPT 693
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-191 3.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 3.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  69 KLIHSSQHHVDESDRRK-RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLI 147
Cdd:PHA02878 151 KLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 309269136 148 DFSGNTALHHAISR-GNLRIVKMLLEHNVDIEAKTE-YGLTPLQLA 191
Cdd:PHA02878 231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 99-191 3.89e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 3.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRD-DEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDI 177
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90
                 ....*....|....
gi 309269136 178 EAKTEYGLTPLQLA 191
Cdd:PHA02878 228 DARDKCGNTPLHIS 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-191 4.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 4.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-IKATQRDNVD 132
Cdd:PHA02878 171 ALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYD 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 133 CASVLLTHNADPNLIDF-SGNTALHHAISrgNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 99-206 5.75e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 5.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASV---LLTHNADPNLIDFSGNTALHHAISRGN-LRIVKMLLEHN 174
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                         90       100       110
                 ....*....|....*....|....*....|....
gi 309269136 175 VDIEAKTEYGLTPLQ--LATFEQKPEMVEFLAAK 206
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK 141
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-205 1.24e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  78 VDESDRRKRTSLH-YACAHN-HPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASV--LLTHNADPNLIDFSGNT 153
Cdd:PHA03095 110 VNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDDRFRS 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 309269136 154 ALH-HAIS-RGNLRIVKMLLEHNVDIEAKTEYGLTPLQ-LATFE--QKPEMVEFLAA 205
Cdd:PHA03095 190 LLHhHLQSfKPRARIVRELIRAGCDPAATDMLGNTPLHsMATGSscKRSLVLPLLIA 246
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 67-191 1.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  67 TEKLIHSSQHHVDESDRRKRTSLHYACAH--NHPDVVTLLLENNSSINIRDDEGCTPL---------------------I 123
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlylesnkidlkilkllidkgV 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309269136 124 KATQRDNVDCasvLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA03100 168 DINAKNRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 3.89e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 3.89e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 309269136   86 RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLL 138
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-218 8.51e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 8.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309269136  155 LHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSSVTPSWSP 218
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-188 1.14e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  89 LHYACaHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV-DCASVLLTHNADPNLIDFSGNTALHHAISRGNLR-- 165
Cdd:PHA03095  55 LHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpk 133

                         90       100
                 ....*....|....*....|...
gi 309269136 166 IVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 82-179 1.59e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  82 DRRKRTSLHYACAHNHPD--VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAI 159
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                         90       100
                 ....*....|....*....|
gi 309269136 160 SRGNLRIVKMLLEHNVDIEA 179
Cdd:PHA03095 299 RNNNGRAVRAALAKNPSAET 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-212 1.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYG-LTPLQLATFEQKPEMVEFLAAKCAKSSV 212
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-203 7.67e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 7.67e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 309269136  151 GNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFL 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-220 2.91e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  86 RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLR 165
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136 166 IVKMLLEHNVDI-EAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSSVTPSWSPSP 220
Cdd:PHA02875  83 AVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-115 3.21e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 3.21e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309269136   54 PLQRAASVGDLDTTEKLIhsSQHHVDESDRrKRTSLHYACAHNHPDVVTLLLENNSSINIRD 115
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-188 3.48e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  77 HVDESDRRKRTSLH-YACAHNHPDVVTLLLENNSSINIRDDEGCTPLIK--ATQRDNVDCASVLLTHNADPNLIDFSGNT 153
Cdd:PHA03095  75 DVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 309269136 154 ALHHAISRGN--LRIVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:PHA03095 155 PLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLL 191
Ank_5 pfam13857
Ankyrin repeats (many copies);
81-125 7.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 7.63e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 309269136   81 SDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKA 125
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-211 2.42e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 2.42e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309269136 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSS 211
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 87-190 3.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  87 TSLHYACAHNHPDVVTLLLENNSSINIRDdegcTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNL-R 165
Cdd:PHA02876 213 SVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsR 288

                         90       100
                 ....*....|....*....|....*
gi 309269136 166 IVKMLLEHNVDIEAKTEYGLTPLQL 190
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYL 313
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-201 4.92e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYACAHNHpDVVTLLLeNNSSINIRDDEGCTPLIKATQRD-NVD 132
Cdd:PHA02874 193 PLHNAAEYGDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDID 269

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 133 CASVLLTHNADPNLIDFSGNTALHHAISRGN-LRIVKMLLEHNVdieAKTEYGltPLQLATFEQKPEMVE 201
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKYINkDPVIKDIIANAV---LIKEAD--KLKDSDFLEHIEIKD 334
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 99-191 6.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 6.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIE 178
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90
                 ....*....|...
gi 309269136 179 AKTEYGLTPLQLA 191
Cdd:PHA02874 185 VKDNNGESPLHNA 197
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-158 6.94e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 6.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136  104 LLENNS-SINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHA 158
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 54-205 8.61e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 8.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLEN-----NSSINIRDDEGCTPLIKATQR 128
Cdd:cd22192   20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 129 DNVDCASVLLTHNADP---------------NLIDFsGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQ-LAT 192
Cdd:cd22192  100 QNLNLVRELIARGADVvspratgtffrpgpkNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVL 178

                        170
                 ....*....|....*.
gi 309269136 193 FEQKP---EMVEFLAA 205
Cdd:cd22192  179 QPNKTfacQMYDLILS 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-148 9.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 9.26e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309269136  77 HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLID 148
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 89-193 2.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  89 LHYACAHN---HPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV--DCASVLLTHNADPNLIDFSGNTALH-HAISRG 162
Cdd:PHA02859  91 LHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSGVSFLNKDFDNNNILYsYILFHS 170

                         90       100       110
                 ....*....|....*....|....*....|.
gi 309269136 163 NLRIVKMLLEHNVDIEAKTEYGLTPLQLATF 193
Cdd:PHA02859 171 DKKIFDFLTSLGIDINETNKSGYNCYDLIKF 201
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 148-207 4.73e-07

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: 51.30  E-value: 4.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309269136 148 DFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFLAAKC 207
Cdd:cd22194  138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKE 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-179 6.26e-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: 45.27  E-value: 6.26e-07
                           10        20
                   ....*....|....*....|....*....
gi 309269136   151 GNTALHHAISRGNLRIVKMLLEHNVDIEA 179
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-179 8.25e-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: 44.94  E-value: 8.25e-07
                          10        20
                  ....*....|....*....|....*....
gi 309269136  151 GNTALHHAISRGNLRIVKMLLEHNVDIEA 179
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-182 1.31e-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. 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: 44.20  E-value: 1.31e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 309269136  151 GNTALHHAISR-GNLRIVKMLLEHNVDIEAKTE 182
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
 80-174 1.51e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 49.27  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  80 ESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEgcTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAI 159
Cdd:PHA02791  25 KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102

                         90
                 ....*....|....*
gi 309269136 160 SRGNLRIVKMLLEHN 174
Cdd:PHA02791 103 DSGNMQTVKLFVKKN 117
Ank_4 pfam13637
Ankyrin repeats (many copies);
54-105 2.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 2.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 309269136   54 PLQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLL 105
Cdd:pfam13637   4 ALHAAAASGHLELL-RLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-191 2.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  51 PIGPLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYAC-AHNHPDVV-TLLLENNSSINIRD----------DEG 118
Cdd:PHA02876  41 PFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICiIPNVMDIViSLTLDCDIILDIKYasiilnkhklDEA 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 119 CTPLIKAT-------------------------QRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEH 173
Cdd:PHA02876 121 CIHILKEAisgndihydkinesieymklikeriQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200

                        170
                 ....*....|....*...
gi 309269136 174 NVDIEAKTEYGLTPLQLA 191
Cdd:PHA02876 201 GADVNIIALDDLSVLECA 218
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-199 3.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  55 LQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYAC-AHNHPDVVTLLLENNSSINIRDDEGCTPL----------- 122
Cdd:PHA02876 244 LLKAIRNEDLETS-LLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLylmakngydte 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 123 -----------IKATQR-------------DNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIE 178
Cdd:PHA02876 323 nirtlimlgadVNAADRlyitplhqastldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402

                        170       180
                 ....*....|....*....|.
gi 309269136 179 AKTEYGLTPLQLATFEQKPEM 199
Cdd:PHA02876 403 ALSQKIGTALHFALCGTNPYM 423
PHA02798 PHA02798
ankyrin-like protein; Provisional
 99-190 5.57e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 5.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRDDEGCTPL--IKATQRD---NVDCASVLLTHNADPNLIDFSGNTALHHAISRG---NLRIVKML 170
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLctILSNIKDykhMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFM 131

                         90       100
                 ....*....|....*....|
gi 309269136 171 LEHNVDIEAKTEYGLTPLQL 190
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQV 151
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-173 8.90e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 8.90e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309269136 101 VTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEH 173
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 57-180 1.86e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136   57 RAASVGDLDTTEKLIHSSQH-HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSiniRDDEGCTPLIKATQR--DNV-D 132
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISLEyvDAVeA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 309269136  133 CASVLLTHNA---------DPNLIDFS-GNTALHHAISRGNLRIVKMLLEHNVDIEAK 180
Cdd:TIGR00870 100 ILLHLLAAFRksgplelanDQYTSEFTpGITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-116 2.17e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 2.17e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 309269136   86 RTSLHYACAH-NHPDVVTLLLENNSSINIRDD 116
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 86-113 4.81e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 4.81e-05
                           10        20
                   ....*....|....*....|....*...
gi 309269136    86 RTSLHYACAHNHPDVVTLLLENNSSINI 113
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 99-177 5.20e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRDDEGCTP---LIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGN---LRIVKMLLE 172
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPlycLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169


                 ....*
gi 309269136 173 HNVDI 177
Cdd:PHA02798 170 KGVDI 174
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-177 6.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 6.58e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309269136 100 VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDI 177
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 79-140 9.11e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 9.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309269136  79 DESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTH 140
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-113 1.19e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 1.19e-04
                          10        20
                  ....*....|....*....|....*...
gi 309269136   86 RTSLHYACAHNHPDVVTLLLENNSSINI 113
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 149-203 1.67e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 1.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309269136 149 FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd22193   74 YEGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYL 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-163 1.91e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  78 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDfsgnTALHH 157
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325


                 ....*.
gi 309269136 158 AISRGN 163
Cdd:PHA03095 326 ASVAGG 331
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 86-206 2.17e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  86 RTSLHYACAHNHPDVVTLLLENNSSINIR------DDEGCT-------PLIKATQRDNVDCASVLLTHNADPNLI---DF 149
Cdd:cd21882   74 QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALeaqDS 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309269136 150 SGNTALHHAISRGN---------------LRIVKMLLEHNVDIEAKTEY-GLTPLQLATFEQKPEMVEFLAAK 206
Cdd:cd21882  154 LGNTVLHALVLQADntpensafvcqmynlLLSYGAHLDPTQQLEEIPNHqGLTPLKLAAVEGKIVMFQHILQR 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 111-176 2.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309269136 111 INIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVD 176
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 100-188 2.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.42  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 100 VVTLLLENNSSINIRDDEGCTPL---IKATQRDNVDCASVLLTHNADPN-LIDFSGNTALHHAISRGNLR--IVKMLLEH 173
Cdd:PHA02989  90 IVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSF 169

                         90
                 ....*....|....*.
gi 309269136 174 NVDIEAKTE-YGLTPL 188
Cdd:PHA02989 170 GVNLFEKTSlYGLTPM 185
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-214 4.06e-04

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: 42.31  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 120 TPLIKATQRDNVDCASVLLT-HNADPNLIDFSGNTALHHAISRGNLRIVKMLLEH-----NVDIEAKTEYGLTPLQLATF 193
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVV 98

                         90       100
                 ....*....|....*....|.
gi 309269136 194 EQKPEMVEFLAAKCAkSSVTP 214
Cdd:cd22192   99 NQNLNLVRELIARGA-DVVSP 118
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 118-203 4.11e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136 118 GCTPLIKATQRDN---VDCASVLLthNADPNLID-------------FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKT 181
Cdd:cd21882   26 GKTCLHKAALNLNdgvNEAIMLLL--EAAPDSGNpkelvnapctdefYQGQTALHIAIENRNLNLVRLLVENGADVSARA 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 309269136 182 E-------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd21882  104 TgrffrkspgnlfyFGELPLSLAACTNQEEIVRLL 138
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 149-203 4.59e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.10  E-value: 4.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309269136 149 FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd22196   92 YKGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFL 160
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 110-172 1.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309269136 110 SINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLE 172
Cdd:PHA02989 248 KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02917 PHA02917
ankyrin-like protein; Provisional
 82-140 1.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 40.75  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  82 DRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-IKATQRDNVDCASVLLTH 140
Cdd:PHA02917 449 DKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIaIAINESRNIELLKMLLCH 508
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 120-192 2.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 2.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309269136 120 TPLIKATQRDNVDCASVLLTHNADPN-LIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLAT 192
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAL 145
PHA02946 PHA02946
ankyin-like protein; Provisional
 89-192 3.62e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  89 LHYACAHNHPD--VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRI 166
Cdd:PHA02946  41 LHAYCGIKGLDerFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVI 120

                         90       100
                 ....*....|....*....|....*....
gi 309269136 167 --VKMLLEHNVDIEAKT-EYGLTPLQLAT 192
Cdd:PHA02946 121 erINLLVQYGAKINNSVdEEGCGPLLACT 149
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 5.76e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 5.76e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 309269136   117 EGCTPLIKATQRDNVDCASVLLTHNADPNL 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 80-203 6.13e-03

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: 38.30  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  80 ESDRRKRTSLHYACAHNHPDVVTLLLE--NNSSINIRDDE------GCTPLIKA--TQRDNVD-CASVLLTHNADPN--- 145
Cdd:cd22197    1 DPNRFDRDRLFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAvlNLQDGVNaCIMPLLEIDKDSGnpk 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309269136 146 -LID-------FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE-------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd22197   81 pLVNaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYL 159
PHA02798 PHA02798
ankyrin-like protein; Provisional
 111-177 6.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 6.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 309269136 111 INIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDI 177
Cdd:PHA02798 251 INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNK 317
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 99-188 7.62e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 38.35  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309269136  99 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNV--DCASVLLTHNADPNLIDFSGNTALHHAISRG-------------- 162
Cdd:PHA02716 298 SVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndi 377

                         90       100
                 ....*....|....*....|....*.
gi 309269136 163 NLRIVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:PHA02716 378 RLDVIQCLISLGADITAVNCLGYTPL 403
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH