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Conserved domains on  [gi|1039790471|ref|XP_017168417|]
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testis-specific gene with ankyrin repeats and PEST domain isoform X1 [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

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-197 1.34e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 121
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471 122 ASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 197
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-197 1.34e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 121
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471 122 ASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 197
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-168 1.23e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 97.11  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  77 LHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHnADPNLIDsSGNTAFHHAISRGNIRIVK 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039790471 157 MLLEHNVDIEAK 168
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 66-179 1.55e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  66 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHH 145
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039790471 146 AISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLA 179
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-193 5.25e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLEN-----NSSINIRDDEGCTPLIKATQR 116
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 117 DNVDCASVLLTHNADPNLIDSSGnTAFH-----------H----AISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQ-LAT 180
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATG-TFFRpgpknliyygeHplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVL 178

                         170
                  ....*....|....*.
gi 1039790471 181 FEQKP---EMVEFLAA 193
Cdd:cd22192   179 QPNKTfacQMYDLILS 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-167 1.79e-06

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: 1.79e-06
                           10        20
                   ....*....|....*....|....*....
gi 1039790471  139 GNTAFHHAISRGNIRIVKMLLEHNVDIEA 167
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 45-168 8.46e-04

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: 40.83  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  45 RAASVGDLDTTEKLIHSSQH-HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSiniRDDEGCTPLIKATQR--DNV-D 120
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISLEyvDAVeA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790471 121 CASVLLTHNAD------PNLIDSS----GNTAFHHAISRGNIRIVKMLLEHNVDIEAK 168
Cdd:TIGR00870 100 ILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-197 1.34e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 121
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471 122 ASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 197
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-197 1.44e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 1.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 121
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471 122 ASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 197
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-194 6.42e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 6.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIhssQHH--VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV 119
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLL---EAGadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039790471 120 DCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAK 194
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-196 2.99e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 2.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  43 LQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCA 122
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039790471 123 SVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCA 196
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-168 1.23e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 97.11  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  77 LHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHnADPNLIDsSGNTAFHHAISRGNIRIVK 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039790471 157 MLLEHNVDIEAK 168
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-176 1.45e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIhssQH--HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV 119
Cdd:COG0666   156 PLHLAAANGNLEIVKLLL---EAgaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039790471 120 DCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPL 176
Cdd:COG0666   233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-136 1.02e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  43 LQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSsINIRDDeGCTPLIKATQRDNVDCA 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1039790471 123 SVLLTHNADPNLID 136
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-194 2.15e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  58 LIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDS 137
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039790471 138 SGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAK 194
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-194 2.66e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 110 LIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHnVDIEAKTeYGLTPLQLATFEQKPEMVE 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*
gi 1039790471 190 FLAAK 194
Cdd:pfam12796  79 LLLEK 83
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 66-179 1.55e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  66 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHH 145
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039790471 146 AISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLA 179
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-191 9.89e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 9.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  56 EKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-----IKATQRDNVDCASVLLTHNA 130
Cdd:PHA03100   18 IKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039790471 131 DPNLIDSSGNTAFHHAISR--GNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKP--EMVEFL 191
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLL 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-191 5.98e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 5.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  37 YDPIGPLQRAASVGDLDTTEKLIHSSqHHVDESDRRKRTSLHYACAHNH-----PDVVTLLLENNSSINIRDDEGCTPLI 111
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 112 KA--TQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRI------------------VKMLLEHNVDIEAKTEY 171
Cdd:PHA03100  112 YAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVY 191

                         170       180
                  ....*....|....*....|
gi 1039790471 172 GLTPLQLATFEQKPEMVEFL 191
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYL 211
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-194 7.40e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 7.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  87 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASV---LLTHNADPNLIDSSGNTAFHHAISRGN-IRIVKMLLEHN 162
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039790471 163 VDIEAKTEYGLTPLQ--LATFEQKPEMVEFLAAK 194
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK 141
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-179 1.19e-12

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 61.59  E-value: 1.19e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471 125 LLTH-NADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLA 179
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-179 1.98e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  57 KLIHSSQHHVDESDRRK-RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLI 135
Cdd:PHA02878  151 KLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039790471 136 DSSGNTAFHHAISR-GNIRIVKMLLEHNVDIEAKTE-YGLTPLQLA 179
Cdd:PHA02878  231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 46-207 8.41e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 8.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  46 AASVGDLDTTEKLIHSSQHhVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVL 125
Cdd:PLN03192  532 VASTGNAALLEELLKAKLD-PDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 126 --LTHNADPNlidsSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLA---AKCAKSSV 200
Cdd:PLN03192  611 yhFASISDPH----AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImngADVDKANT 686


                  ....*..
gi 1039790471 201 TPSWSPS 207
Cdd:PLN03192  687 DDDFSPT 693
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-179 8.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 8.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471   1 MERLINSSQY-HVDEYNRRGRCMHPQKKK-KYPLYLIGYDPIGPLQRAASVG----DLDTTEKLIhssqhhVDESDRRKR 74
Cdd:PHA02878   57 LTRGHNVNQPdHRDLTPLHIICKEPNKLGmKEMIRSINKCSVFYTLVAIKDAfnnrNVEIFKIIL------TNRYKNIQT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  75 TSLHYACAHNHPD-----VVTLLLENNSSINIRD-DEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAIS 148
Cdd:PHA02878  131 IDLVYIDKKSKDDiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039790471 149 RGNIRIVKMLLEHNVDIEAKTEYGLTPLQLA 179
Cdd:PHA02878  211 HYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-179 1.21e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.52  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-IKATQRDNVD 120
Cdd:PHA02878  171 ALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYD 249

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039790471 121 CASVLLTHNADPNlIDSS--GNTAFHHAISrgNIRIVKMLLEHNVDIEAKTEYGLTPLQLA 179
Cdd:PHA02878  250 ILKLLLEHGVDVN-AKSYilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-171 1.38e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  84 NHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNV 163
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  ....*...
gi 1039790471 164 DIEAKTEY 171
Cdd:PHA03100  250 SIKTIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-126 1.74e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.74e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039790471  74 RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLL 126
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-193 2.39e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  66 VDESDRRKRTSLH-YACAHN-HPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASV--LLTHNADPNLIDSSGNT 141
Cdd:PHA03095  110 VNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDDRFRS 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039790471 142 AFH-HAIS-RGNIRIVKMLLEHNVDIEAKTEYGLTPLQ-LATFE--QKPEMVEFLAA 193
Cdd:PHA03095  190 LLHhHLQSfKPRARIVRELIRAGCDPAATDMLGNTPLHsMATGSscKRSLVLPLLIA 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-167 4.10e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  70 DRRKRTSLHYACAHNHPD--VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAI 147
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                          90       100
                  ....*....|....*....|
gi 1039790471 148 SRGNIRIVKMLLEHNVDIEA 167
Cdd:PHA03095  299 RNNNGRAVRAALAKNPSAET 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-200 1.05e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 121
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 122 ASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYG-LTPLQLATFEQKPEMVEFLAAKCAKSSV 200
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-179 2.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  55 TEKLIHSSQHHVDESDRRKRTSLHYACAH--NHPDVVTLLLENNSSINIRDDEGCTPL---------------------I 111
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlylesnkidlkilkllidkgV 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790471 112 KATQRDNVDCasvLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLA 179
Cdd:PHA03100  168 DINAKNRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-176 2.28e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  77 LHYACaHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV-DCASVLLTHNADPNLIDSSGNTAFHHAISRGNIR-- 153
Cdd:PHA03095   55 LHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpk 133

                          90       100
                  ....*....|....*....|...
gi 1039790471 154 IVKMLLEHNVDIEAKTEYGLTPL 176
Cdd:PHA03095  134 VIRLLLRKGADVNALDLYGMTPL 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-159 3.31e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039790471 108 TPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLL 159
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-206 3.98e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 3.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039790471 143 FHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSSVTPSWSP 206
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 74-208 2.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  74 RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIR 153
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471 154 IVKMLLEHNVDI-EAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSSVTPSWSPSP 208
Cdd:PHA02875   83 AVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-103 2.41e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 2.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039790471  42 PLQRAASVGDLDTTEKLIhsSQHHVDESDRrKRTSLHYACAHNHPDVVTLLLENNSSINIRD 103
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-176 3.56e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  65 HVDESDRRKRTSLH-YACAHNHPDVVTLLLENNSSINIRDDEGCTPLIK--ATQRDNVDCASVLLTHNADPNLIDSSGNT 141
Cdd:PHA03095   75 DVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039790471 142 AFHHAISRGN--IRIVKMLLEHNVDIEAKTEYGLTPL 176
Cdd:PHA03095  155 PLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLL 191
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-191 3.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039790471 139 GNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFL 191
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
69-113 7.46e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 7.46e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039790471  69 SDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKA 113
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 43-179 1.95e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  43 LQRAASVGDLDTTEKLIHSSQHhVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCA 122
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 123 SVLLTH-------------------------------NADPNLIDSSGNTAFHHAISRG-NIRIVKMLLEHNVDIEAKTE 170
Cdd:PHA02874  207 KLLIDHgnhimnkckngftplhnaiihnrsaiellinNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDN 286


                  ....*....
gi 1039790471 171 YGLTPLQLA 179
Cdd:PHA02874  287 KGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 42-139 7.00e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 7.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYACAHNHpDVVTLLLeNNSSINIRDDEGCTPLIKATQRD-NVD 120
Cdd:PHA02874  193 PLHNAAEYGDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDID 269

                          90
                  ....*....|....*....
gi 1039790471 121 CASVLLTHNADPNLIDSSG 139
Cdd:PHA02874  270 IIDILLYHKADISIKDNKG 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-137 1.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 1.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039790471  65 HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDS 137
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 87-179 1.58e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  87 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIE 166
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90
                  ....*....|...
gi 1039790471 167 AKTEYGLTPLQLA 179
Cdd:PHA02874  185 VKDNNGESPLHNA 197
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-178 1.72e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  75 TSLHYACAHNHPDVVTLLLENNSSINIRDdegcTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNI-R 153
Cdd:PHA02876  213 SVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsR 288

                          90       100
                  ....*....|....*....|....*
gi 1039790471 154 IVKMLLEHNVDIEAKTEYGLTPLQL 178
Cdd:PHA02876  289 LVPKLLERGADVNAKNIKGETPLYL 313
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-146 3.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 3.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471  92 LLENNS-SINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHA 146
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-193 5.25e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  42 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLEN-----NSSINIRDDEGCTPLIKATQR 116
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 117 DNVDCASVLLTHNADPNLIDSSGnTAFH-----------H----AISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQ-LAT 180
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATG-TFFRpgpknliyygeHplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVL 178

                         170
                  ....*....|....*.
gi 1039790471 181 FEQKP---EMVEFLAA 193
Cdd:cd22192   179 QPNKTfacQMYDLILS 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 122-199 5.72e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 5.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790471 122 ASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSS 199
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-93 1.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039790471  42 PLQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLL 93
Cdd:pfam13637   4 ALHAAAASGHLELL-RLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-167 1.79e-06

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: 1.79e-06
                           10        20
                   ....*....|....*....|....*....
gi 1039790471  139 GNTAFHHAISRGNIRIVKMLLEHNVDIEA 167
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-167 1.79e-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: 43.79  E-value: 1.79e-06
                          10        20
                  ....*....|....*....|....*....
gi 1039790471 139 GNTAFHHAISRGNIRIVKMLLEHNVDIEA 167
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 68-162 2.25e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 48.11  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  68 ESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEgcTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAI 147
Cdd:PHA02791   25 KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102

                          90
                  ....*....|....*
gi 1039790471 148 SRGNIRIVKMLLEHN 162
Cdd:PHA02791  103 DSGNMQTVKLFVKKN 117
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 89-161 3.72e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039790471  89 VTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEH 161
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-179 8.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 8.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  39 PIGPLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYAC-AHNHPDVV-TLLLENNSSINIRD----------DEG 106
Cdd:PHA02876   41 PFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICiIPNVMDIViSLTLDCDIILDIKYasiilnkhklDEA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 107 CTPLIKAT-------------------------QRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEH 161
Cdd:PHA02876  121 CIHILKEAisgndihydkinesieymklikeriQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200

                         170
                  ....*....|....*...
gi 1039790471 162 NVDIEAKTEYGLTPLQLA 179
Cdd:PHA02876  201 GADVNIIALDDLSVLECA 218
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 139-195 8.99e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 8.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039790471 139 GNTAFHHAISRGNIRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFLAAKC 195
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKE 211
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 77-181 9.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 9.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  77 LHYACAHN---HPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV--DCASVLLTHNADPNLIDSSGNTAFH-HAISRG 150
Cdd:PHA02859   91 LHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSGVSFLNKDFDNNNILYsYILFHS 170

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039790471 151 NIRIVKMLLEHNVDIEAKTEYGLTPLQLATF 181
Cdd:PHA02859  171 DKKIFDFLTSLGIDINETNKSGYNCYDLIKF 201
PHA02798 PHA02798
ankyrin-like protein; Provisional
 87-178 2.05e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  87 DVVTLLLENNSSINIRDDEGCTPL--IKATQRD---NVDCASVLLTHNADPNLIDSSGNTAFHHAISRG---NIRIVKML 158
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctILSNIKDykhMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFM 131

                          90       100
                  ....*....|....*....|
gi 1039790471 159 LEHNVDIEAKTEYGLTPLQL 178
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQV 151
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-187 2.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  43 LQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYAC-AHNHPDVVTLLLENNSSINIRDDEGCTPL----------- 110
Cdd:PHA02876  244 LLKAIRNEDLETS-LLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLylmakngydte 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 111 -----------IKATQR-------------DNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDIE 166
Cdd:PHA02876  323 nirtlimlgadVNAADRlyitplhqastldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402

                         170       180
                  ....*....|....*....|.
gi 1039790471 167 AKTEYGLTPLQLATFEQKPEM 187
Cdd:PHA02876  403 ALSQKIGTALHFALCGTNPYM 423
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-104 2.43e-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: 2.43e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039790471  74 RTSLHYACAH-NHPDVVTLLLENNSSINIRDD 104
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-170 2.82e-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: 40.35  E-value: 2.82e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039790471 139 GNTAFHHAISR-GNIRIVKMLLEHNVDIEAKTE 170
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-152 6.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  66 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSsgntAFHH 145
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNT 325


                  ....*..
gi 1039790471 146 AISRGNI 152
Cdd:PHA03095  326 ASVAGGD 332
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 74-101 6.47e-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: 39.11  E-value: 6.47e-05
                           10        20
                   ....*....|....*....|....*...
gi 1039790471   74 RTSLHYACAHNHPDVVTLLLENNSSINI 101
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 87-165 6.79e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 6.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  87 DVVTLLLENNSSINIRDDEGCTP---LIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGN---IRIVKMLLE 160
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPlycLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169


                  ....*
gi 1039790471 161 HNVDI 165
Cdd:PHA02798  170 KGVDI 174
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 74-194 7.94e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  74 RTSLHYACAHNHPDVVTLLLENNSSINIR------DDEGCT-------PLIKATQRDNVDCASVLLTHNADPNLI---DS 137
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALeaqDS 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039790471 138 SGNTAFHHAISRGN---------------IRIVKMLLEHNVDIEAKTEY-GLTPLQLATFEQKPEMVEFLAAK 194
Cdd:cd21882   154 LGNTVLHALVLQADntpensafvcqmynlLLSYGAHLDPTQQLEEIPNHqGLTPLKLAAVEGKIVMFQHILQR 226
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-128 8.52e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 8.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039790471  67 DESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTH 128
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-101 1.13e-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: 38.39  E-value: 1.13e-04
                          10        20
                  ....*....|....*....|....*...
gi 1039790471  74 RTSLHYACAHNHPDVVTLLLENNSSINI 101
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 88-165 1.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790471  88 VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVDI 165
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 88-176 2.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.42  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  88 VVTLLLENNSSINIRDDEGCTPL---IKATQRDNVDCASVLLTHNADPN-LIDSSGNTAFHHAISRGNIR--IVKMLLEH 161
Cdd:PHA02989   90 IVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSF 169

                          90
                  ....*....|....*.
gi 1039790471 162 NVDIEAKTE-YGLTPL 176
Cdd:PHA02989  170 GVNLFEKTSlYGLTPM 185
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 98-160 2.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 2.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039790471  98 SINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLE 160
Cdd:PHA02989  248 KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 99-164 3.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 3.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790471  99 INIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEHNVD 164
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 45-168 8.46e-04

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: 40.83  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  45 RAASVGDLDTTEKLIHSSQH-HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSiniRDDEGCTPLIKATQR--DNV-D 120
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISLEyvDAVeA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790471 121 CASVLLTHNAD------PNLIDSS----GNTAFHHAISRGNIRIVKMLLEHNVDIEAK 168
Cdd:TIGR00870 100 ILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-202 1.05e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 108 TPLIKATQRDNVDCASVLLT-HNADPNLIDSSGNTAFHHAISRGNIRIVKMLLEH-----NVDIEAKTEYGLTPLQLATF 181
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVV 98

                          90       100
                  ....*....|....*....|.
gi 1039790471 182 EQKPEMVEFLAAKCAkSSVTP 202
Cdd:cd22192    99 NQNLNLVRELIARGA-DVVSP 118
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 104-191 1.19e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 104 DEGCTPLIKAT---QRDNVDCASVLL-----THNADPnLIDSS-------GNTAFHHAISRGNIRIVKMLLEHNVDIEAK 168
Cdd:cd22193    27 STGKTCLMKALlnlNPGTNDTIRILLdiaekTDNLKR-FINAEytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAH 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039790471 169 TE--------------YGLTPLQLATFEQKPEMVEFL 191
Cdd:cd22193   106 AKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYL 142
PHA02917 PHA02917
ankyrin-like protein; Provisional
 70-128 1.36e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.98  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  70 DRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-IKATQRDNVDCASVLLTH 128
Cdd:PHA02917  449 DKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIaIAINESRNIELLKMLLCH 508
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 139-191 2.76e-03

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: 39.02  E-value: 2.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039790471 139 GNTAFHHAISRGNIRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFL 191
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFL 160
PHA02946 PHA02946
ankyin-like protein; Provisional
 77-180 3.01e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  77 LHYACAHNHPD--VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDSSGNTAFHHAISRGN--I 152
Cdd:PHA02946   41 LHAYCGIKGLDerFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevI 120

                          90       100
                  ....*....|....*....|....*....
gi 1039790471 153 RIVKMLLEHNVDIEAKT-EYGLTPLQLAT 180
Cdd:PHA02946  121 ERINLLVQYGAKINNSVdEEGCGPLLACT 149
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 68-191 3.07e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.97  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  68 ESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIR----------DDEGC----TPLIKATQRDNVDCASVLLTHNADP- 132
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEIVQLLMEKESTDi 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039790471 133 NLIDSSGNTAFHHAI-----SRGN----IRIVKMLLE--HNVDIEA-KTEYGLTPLQLATFEQKPEMVEFL 191
Cdd:cd22194   216 TSQDSRGNTVLHALVtvaedSKTQndfvKRMYDMILLksENKNLETiRNNEGLTPLQLAAKMGKAEILKYI 286
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 75-193 4.77e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.52  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  75 TSLHYACAHNHPDVVTLLLENNSSINIR---------DDEGC-----TPLIKATQRDNVDCASVLLTHNADPNLIDSSGN 140
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvksQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039790471 141 TAFHHAI-----SRGNIRIVKM----------LLEHNVDIEAKTEY-GLTPLQLATFEQKPEMVEFLAA 193
Cdd:TIGR00870 210 TLLHLLVmenefKAEYEELSCQmynfalslldKLRDSKELEVILNHqGLTPLKLAAKEGRIVLFRLKLA 278
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 72-187 5.84e-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: 37.91  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  72 RKRTSLHYACAHNHPDVVTLLLENNSSINIR-------DDEGCT------PLIKATQRDNVDCASVLLTHNADPNLI--- 135
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARacgrffqKKQGTCfyfgelPLSLAACTKQWDVVNYLLENPHQPASLqaq 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039790471 136 DSSGNTAFHHAI-----SRGNIRIV-KML---------LEHNVDIEAKTEY-GLTPLQLATFEQKPEM 187
Cdd:cd22197   173 DSLGNTVLHALVmiadnSPENSALViKMYdgllqagarLCPTVQLEEISNHeGLTPLKLAAKEGKIEI 240
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-134 7.03e-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: 33.33  E-value: 7.03e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039790471  105 EGCTPLIKATQRDNVDCASVLLTHNADPNL 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 106-191 7.76e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 37.55  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471 106 GCTPLIKATQRDN---VDCASVLLthNADPN------LIDSS-------GNTAFHHAISRGNIRIVKMLLEHNVDIEAKT 169
Cdd:cd21882    26 GKTCLHKAALNLNdgvNEAIMLLL--EAAPDsgnpkeLVNAPctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARA 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039790471 170 E-------------YGLTPLQLATFEQKPEMVEFL 191
Cdd:cd21882   104 TgrffrkspgnlfyFGELPLSLAACTNQEEIVRLL 138
PHA02792 PHA02792
ankyrin-like protein; Provisional
 71-174 8.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 37.62  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790471  71 RRKRTSLHYACAHNH-PDVVTLLLENNSSINIRDDE--GCTPLIKATQRDNVDCASVLLT---HNADPNLIDSSGNTAFH 144
Cdd:PHA02792  336 RFKHINKYFQKFDNRdPKVVEYILKNGNVVVEDDDNiiNIMPLFPTLSIHESDVLSILKLckpYIDDINKIDKHGRSILY 415

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039790471 145 HAISRGNIRIVKMLLEHNVDIEAKTEYGLT 174
Cdd:PHA02792  416 YCIESHSVSLVEWLIDNGADINITTKYGST 445
 
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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