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Conserved domains on  [gi|1757249820|ref|WP_150993256|]
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ankyrin repeat domain-containing protein [Cupriavidus basilensis]

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];
1-209 7.40e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 7.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820   1 MNAIRRLVAVAAMLVGAAAWAGPVDDMRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKd 80
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  81 IDFDKTNAAGETPLMMASLQNELDLVKLMVDQ-MEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPL 158
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 159 MMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAEGLKSR 209
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-209 7.40e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 7.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820   1 MNAIRRLVAVAAMLVGAAAWAGPVDDMRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKd 80
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  81 IDFDKTNAAGETPLMMASLQNELDLVKLMVDQ-MEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPL 158
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 159 MMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAEGLKSR 209
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-184 1.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  94 LMMASLQNELDLVKLMVDQmEVEIN---KTGWTPLHYAATNGNNDIVKFLVDHAAyIDAESpNGTTPLMMAARGGHIETV 170
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANlqdKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1757249820 171 KLLLDEGADMRLKN 184
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-179 1.06e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  30 AVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREK--SLKVAEALIrAKDIDFDKTNAAGETPLMMA--SLQNELDL 105
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLL-DNGANVNIKNSDGENLLHLYleSNKIDLKI 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 106 VKLMVDQmEVEINKT-------------------GWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGH 166
Cdd:PHA03100  159 LKLLIDK-GVDINAKnrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237

                         170
                  ....*....|...
gi 1757249820 167 IETVKLLLDEGAD 179
Cdd:PHA03100  238 KEIFKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-191 1.79e-13

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 68.89  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  60 LVVALREKSLKVAEALIRAKDIDFDKTNAAGETPLMMASLQNELDLVKLMVDQMEVEINK-------TGWTPLHYAATNG 132
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsdlyQGETALHIAVVNQ 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757249820 133 NNDIVKFLVDHAAyiDAESPNGTT----------------PLMMAARGGHIETVKLLLDEGADMRLKNQQGMTVI 191
Cdd:cd22192   101 NLNLVRELIARGA--DVVSPRATGtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 153-180 5.22e-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: 41.80  E-value: 5.22e-06
                           10        20
                   ....*....|....*....|....*...
gi 1757249820  153 NGTTPLMMAARGGHIETVKLLLDEGADM 180
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 65-179 3.25e-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: 41.22  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  65 REKSLKVAEALIRAKDIDFDKTNAAGETPLMMASLQNE-LDLVKLMVD-QMEVEINKTgwtpLHYAATNGNNDIVKFLVD 142
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENEnLELTELLLNlSCRGAVGDT----LLHAISLEYVDAVEAILL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 143 HAAYIDAESPN--------------GTTPLMMAARGGHIETVKLLLDEGAD 179
Cdd:TIGR00870 103 HLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-209 7.40e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 7.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820   1 MNAIRRLVAVAAMLVGAAAWAGPVDDMRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKd 80
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  81 IDFDKTNAAGETPLMMASLQNELDLVKLMVDQ-MEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPL 158
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 159 MMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAEGLKSR 209
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-204 2.41e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820   2 NAIRRLVAVAAMLVGAAAWAGPVDDMRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIrAKDI 81
Cdd:COG0666    66 DLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  82 DFDKTNAAGETPLMMASLQNELDLVKLMVDQmEVEIN---KTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPL 158
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNardNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1757249820 159 MMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAE 204
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-204 7.93e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.96  E-value: 7.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820   4 IRRLVAVAAMLVGAAAWAGPVDDMRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKDIDF 83
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  84 DKTNAAGETPLMMASLQNELDLVKLMVDQ-MEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMA 161
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAgADVNArDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1757249820 162 ARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAE 204
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-184 1.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  94 LMMASLQNELDLVKLMVDQmEVEIN---KTGWTPLHYAATNGNNDIVKFLVDHAAyIDAESpNGTTPLMMAARGGHIETV 170
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANlqdKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1757249820 171 KLLLDEGADMRLKN 184
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-189 3.87e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 3.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  29 HAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKdIDFDKTNAAGETPLMMASLQNELDLVKL 108
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 109 MVDQM-EVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGADMRLKNQQ 186
Cdd:COG0666   205 LLEAGaDVNAkDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                  ...
gi 1757249820 187 GMT 189
Cdd:COG0666   285 LLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
60-149 6.95e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 6.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  60 LVVALREKSLKVAEALIRaKDIDFDKTNAAGETPLMMASLQNELDLVKLMVDQMEVEINKTGWTPLHYAATNGNNDIVKF 139
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1757249820 140 LVDHAAYIDA 149
Cdd:pfam12796  80 LLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-206 9.05e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 9.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 125 LHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEgADMRLKNqQGMTVIDFAERYHQKEIAE 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ..
gi 1757249820 205 GL 206
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-179 1.06e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  30 AVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREK--SLKVAEALIrAKDIDFDKTNAAGETPLMMA--SLQNELDL 105
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLL-DNGANVNIKNSDGENLLHLYleSNKIDLKI 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 106 VKLMVDQmEVEINKT-------------------GWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGH 166
Cdd:PHA03100  159 LKLLIDK-GVDINAKnrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237

                         170
                  ....*....|...
gi 1757249820 167 IETVKLLLDEGAD 179
Cdd:PHA03100  238 KEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-179 1.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.33  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  30 AVEFDDVKAAQKLLARGVDPNlVDAKG--NPMLVVALREKSLKVAEALIRAKDIDfDKTNAAGETPLMMASLQNELDLVK 107
Cdd:PHA02875   42 AMKFRDSEAIKLLMKHGAIPD-VKYPDieSELHDAVEEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMK 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1757249820 108 LMVD-QMEVEINKTG-WTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGAD 179
Cdd:PHA02875  120 LLIArGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-191 1.79e-13

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 68.89  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  60 LVVALREKSLKVAEALIRAKDIDFDKTNAAGETPLMMASLQNELDLVKLMVDQMEVEINK-------TGWTPLHYAATNG 132
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsdlyQGETALHIAVVNQ 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757249820 133 NNDIVKFLVDHAAyiDAESPNGTT----------------PLMMAARGGHIETVKLLLDEGADMRLKNQQGMTVI 191
Cdd:cd22192   101 NLNLVRELIARGA--DVVSPRATGtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-189 2.01e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  31 VEFDDVKaaqKLLARGVDPNLVDAKGNPMLVVALR---EKSLKVAEALIRAkDIDFDKTNAAGETPLMM-ASLQNELDLV 106
Cdd:PHA03095   25 VTVEEVR---RLLAAGADVNFRGEYGKTPLHLYLHyssEKVKDIVRLLLEA-GADVNAPERCGFTPLHLyLYNATTLDVI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 107 KLMVDqMEVEINKT---GWTPLH-YAAT-NGNNDIVKFLVDHAAYIDAESPNGTTPL--MMAARGGHIETVKLLLDEGAD 179
Cdd:PHA03095  101 KLLIK-AGADVNAKdkvGRTPLHvYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGAD 179

                         170
                  ....*....|
gi 1757249820 180 MRLKNQQGMT 189
Cdd:PHA03095  180 VYAVDDRFRS 189
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 26-179 6.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  26 DMRHAVEFDDVKAAQKLLARGVDPN-LVDAKGNPMLVVALREKSLKVAEALIRAKdIDFDKTNAAGETPLMMASLQNELD 104
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1757249820 105 LVKLMVDQ---MEVEiNKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLM-MAARGGHIETVKLLLDEGAD 179
Cdd:PHA02875  150 GIELLIDHkacLDIE-DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 27-200 7.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 7.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  27 MRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRaKDIDFDKTNAAGETPLMMASLQNELDLV 106
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-KGAYANVKDNNGESPLHNAAEYGDYACI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 107 KLMVDQMEVEINK--TGWTPLHYAATNgNNDIVKFLVDHAAyIDAESPNGTTPLMMAAR-GGHIETVKLLLDEGADMRLK 183
Cdd:PHA02874  207 KLLIDHGNHIMNKckNGFTPLHNAIIH-NRSAIELLINNAS-INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIK 284

                         170
                  ....*....|....*..
gi 1757249820 184 NQQGMTVIDFAERYHQK 200
Cdd:PHA02874  285 DNKGENPIDTAFKYINK 301
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-202 4.79e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  30 AVEFDDVKAAQKLLARGVDPNLVDAK-GNPMLVvALREKSLKVAEALIR-------------AKD---------IDFDKT 86
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKiPHPLLT-AIKIGAHDIIKLLIDngvdtsilpipciEKDmiktildcgIDVNIK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  87 NAAGETPLMMASLQNELDLVKLMVD-QMEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARG 164
Cdd:PHA02874  121 DAELKTFLHYAIKKGDLESIKMLFEyGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1757249820 165 GHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEI 202
Cdd:PHA02874  201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI 238
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-174 3.68e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 3.68e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1757249820 121 GWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLL 174
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 26-206 6.66e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 6.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  26 DMRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKDIDfDKTNAAGETPLMMASLQNELDL 105
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 106 VKLMVDQ---MEVEINKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGADMRL 182
Cdd:PHA02875   84 VEELLDLgkfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                         170       180
                  ....*....|....*....|....
gi 1757249820 183 KNQQGMTVIDFAERYHQKEIAEGL 206
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKML 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-192 9.01e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 9.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  64 LREKSLKVAE-ALIRAKDIDFDKTNAAGETPL---MMASLQNELDLVKLMVDQmEVEINKT---GWTPLHYAATNGNN-D 135
Cdd:PHA03095   20 LNASNVTVEEvRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEA-GADVNAPercGFTPLHLYLYNATTlD 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1757249820 136 IVKFLVDHAAYIDAESPNGTTPLMMAARGGHI--ETVKLLLDEGADMRLKNQQGMTVID 192
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-200 1.41e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  85 KTNAAGETPLMMASLQNELDLVKLMVDQ-MEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMA- 161
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYgANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISv 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1757249820 162 ARGGHIETVKLLLDEGADMRLKNQ-QGMTVIDFAERYHQK 200
Cdd:PHA02878  243 GYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK 282
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 58-184 1.56e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  58 PMLVVALREKSLKVAEALIRaKDIDFDKTNAAGETPLM-----MASLQNELDLVKLMVdQMEVEINKT---GWTPLHYAA 129
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLD-NGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLL-EYGANVNAPdnnGITPLLYAI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1757249820 130 TN--GNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIET--VKLLLDEGADMRLKN 184
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKN 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-194 3.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820   1 MNAIRRLVAVAAMLVGAAAWA-GPVDD-----MRHAVEFDDV-KAAQKLLARGVDPNLVDAKG-NPMLVVALREKSLKVA 72
Cdd:PHA02876  245 LKAIRNEDLETSLLLYDAGFSvNSIDDckntpLHHASQAPSLsRLVPKLLERGADVNAKNIKGeTPLYLMAKNGYDTENI 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  73 EALIrAKDIDFDKTNAAGETPLMMASLQNELDLVKLMVDQMEVEINKTGW---TPLHYAATNGNNDIVKFLVDHAAYIDA 149
Cdd:PHA02876  325 RTLI-MLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYcdkTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1757249820 150 ESPNGTTPLMMAARGGH-IETVKLLLDEGADMRLKNQQGMTVIDFA 194
Cdd:PHA02876  404 LSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-149 7.29e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 7.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  42 LLARGVDPNLVDAKGNPMLVVALR--EKSLKVAEALIR------AKD---------IDFDKTNAAGETPLMMASLQNELD 104
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDkgvdinAKNrvnyllsygVPINIKDVYGFTPLHYAVYNNNPE 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1757249820 105 LVKLMVDQmEVEIN---KTGWTPLHYAATNGNNDIVKFLVDHAAYIDA 149
Cdd:PHA03100  207 FVKYLLDL-GANPNlvnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-191 6.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  92 TPLMMASLQNELDLVKLMVDQ--MEVEINKTGWTPLHYAATNGNN-----DIVKFLVDHAAYIDAESPNGTTPLMMAA-- 162
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNgaDINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                          90       100
                  ....*....|....*....|....*....
gi 1757249820 163 RGGHIETVKLLLDEGADMRLKNQQGMTVI 191
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLL 145
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 35-189 9.44e-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: 48.86  E-value: 9.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  35 DVKAAQKLL-ARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKD--IDFDKTNA--AGETPLMMASLQNELDLVKLM 109
Cdd:cd22192    29 DVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNEPMTSDlyQGETALHIAVVNQNLNLVREL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 110 V----DQMEVEINKT------------GWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLL 173
Cdd:cd22192   109 IargaDVVSPRATGTffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQM 188

                         170       180
                  ....*....|....*....|....*.
gi 1757249820 174 LD-------EGADMRL---KNQQGMT 189
Cdd:cd22192   189 YDlilsydkEDDLQPLdlvPNNQGLT 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-204 1.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 154 GTTPLMMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAE 204
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 27-180 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  27 MRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRAKDiDFDKTNAAGETPLMMASLQNELDLV 106
Cdd:PHA02876  182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS-NINKNDLSLLKAIRNEDLETSLLLY 260

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1757249820 107 KLMVDQMEVEINKTgwTPLHYAA-TNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGH-IETVKLLLDEGADM 180
Cdd:PHA02876  261 DAGFSVNSIDDCKN--TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 77-211 1.73e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  77 RAKDIDFDKtnaagetplmMASLQNELDLVKLMVDQMEVEINKTGwTPLHYAAT---------------------NGNND 135
Cdd:PTZ00322   28 RAKPISFER----------MAAIQEEIARIDTHLEALEATENKDA-TPDHNLTTeevidpvvahmltvelcqlaaSGDAV 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1757249820 136 IVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYHQKEIAEGLKSRWQ 211
Cdd:PTZ00322   97 GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-174 1.77e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  42 LLARGVDPNLVDAKGNPMLVVALR--EKSLKVAEALIRAkDIDFDKTNAAGETPL---MMASLQNELDLVKLMVDQMEVE 116
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRA-GCDPAATDMLGNTPLhsmATGSSCKRSLVLPLLIAGISIN 251

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1757249820 117 I-NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLL 174
Cdd:PHA03095  252 ArNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 27-194 2.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  27 MRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLKVAEALIRakdidfdktNAAGetplmmaslqneldlv 106
Cdd:PHA02878  172 LHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE---------NGAS---------------- 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 107 klmVDQMeveiNKTGWTPLHYAATNGNN-DIVKFLVDHAAYIDAESP-NGTTPLMMAARGGhiETVKLLLDEGADMRLKN 184
Cdd:PHA02878  227 ---TDAR----DKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLN 297

                         170
                  ....*....|
gi 1757249820 185 QQGMTVIDFA 194
Cdd:PHA02878  298 SYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
92-141 2.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 2.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1757249820  92 TPLMMASLQNELDLVKLMVDQmEVEINKT---GWTPLHYAATNGNNDIVKFLV 141
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVdgnGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-180 2.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  64 LREKSLKVAEALIRAKDIDFDKTNAAGE-TPLMMASLQNELDLVKLMVDQMEVEINKT---GWTPLHYAATNGNNDIVKF 139
Cdd:PHA02876  117 LDEACIHILKEAISGNDIHYDKINESIEyMKLIKERIQQDELLIAEMLLEGGADVNAKdiyCITPIHYAAERGNAKMVNL 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1757249820 140 LVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGADM 180
Cdd:PHA02876  197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 121-149 3.76e-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: 42.24  E-value: 3.76e-06
                          10        20
                  ....*....|....*....|....*....
gi 1757249820 121 GWTPLHYAATNGNNDIVKFLVDHAAYIDA 149
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 67-194 3.79e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  67 KSLKVAEALIRAKDIDFDKTNAAgeTPLMMASLQNELDLVKLMVDQMEVEI-NKTGWTPLHYAATNGNNDIVKFLVDHAA 145
Cdd:PLN03192  505 HDLNVGDLLGDNGGEHDDPNMAS--NLLTVASTGNAALLEELLKAKLDPDIgDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 146 YIDAESPNGTTP-------------------------------LMMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFA 194
Cdd:PLN03192  583 NVHIRDANGNTAlwnaisakhhkifrilyhfasisdphaagdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-220 4.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 108 LMVDQMEVEINKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHI-----ETVKLLLDEGADMRL 182
Cdd:PHA03100   22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1757249820 183 KNQQGMTVIDFA--ERYHQKEIAEGLKSRWQKLYPQTPIS 220
Cdd:PHA03100  102 PDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDG 141
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 153-180 5.22e-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: 41.80  E-value: 5.22e-06
                           10        20
                   ....*....|....*....|....*...
gi 1757249820  153 NGTTPLMMAARGGHIETVKLLLDEGADM 180
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 121-149 5.37e-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: 41.80  E-value: 5.37e-06
                           10        20
                   ....*....|....*....|....*....
gi 1757249820  121 GWTPLHYAATNGNNDIVKFLVDHAAYIDA 149
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 153-184 1.07e-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: 41.12  E-value: 1.07e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1757249820 153 NGTTPLMMAA-RGGHIETVKLLLDEGADMRLKN 184
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 102-191 1.09e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 45.67  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 102 ELDLVKLMVDQMEVEIN----KTGWTPLHYAATNGN--NDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHI--ETVKLL 173
Cdd:PHA02716  154 DLDLIKYMVDVGIVNLNyvckKTGYGILHAYLGNMYvdIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKI 233

                          90
                  ....*....|....*...
gi 1757249820 174 LDEGADMRLKNQQGMTVI 191
Cdd:PHA02716  234 IELGGDMDMKCVNGMSPI 251
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 121-149 1.31e-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: 41.12  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1757249820 121 GWTPLHYAAT-NGNNDIVKFLVDHAAYIDA 149
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-194 1.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1757249820 140 LVDH-AAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFA 194
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 103-184 2.37e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 103 LDLVKLMVDQmEVEINK---TGWTPLHYAATNG---NNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGH---IETVKLL 173
Cdd:PHA02798   89 LDIVKILIEN-GADINKknsDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLL 167

                          90
                  ....*....|.
gi 1757249820 174 LDEGADMRLKN 184
Cdd:PHA02798  168 LEKGVDINTHN 178
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 27-180 4.60e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  27 MRHAVEFDDVKAAQKLLARGVDPNLVDAKGNPMLVVALREKSLkvAEALIRAKdIDFDKTNAAGETPLMMASLQNELDLV 106
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAAL--LEELLKAK-LDPDIGDSKGRTPLHIAASKGYEDCV 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 107 KLM------VDQMEVEINKTGWTPL---HY------------------------AATNGNNDIVKFLVDHAAYIDAESPN 153
Cdd:PLN03192  575 LVLlkhacnVHIRDANGNTALWNAIsakHHkifrilyhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                         170       180
                  ....*....|....*....|....*..
gi 1757249820 154 GTTPLMMAARGGHIETVKLLLDEGADM 180
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_5 pfam13857
Ankyrin repeats (many copies);
118-161 2.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 2.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1757249820 118 NKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMA 161
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 66-191 2.45e-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: 41.79  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  66 EKSLKVAEALIRAKDIDFDKTNAAGETPLMMASL-----QNELDLVKLMVDQMEVEINK-----------TGWTPLHYAA 129
Cdd:cd21882     2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAALnlndgVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757249820 130 TNGNNDIVKFLVDHAAYIDA--------ESPN-----GTTPLMMAARGGHIETVKLLLDEGADMRLKNQQ---GMTVI 191
Cdd:cd21882    82 ENRNLNLVRLLVENGADVSAratgrffrKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVL 159
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 65-179 3.25e-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: 41.22  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  65 REKSLKVAEALIRAKDIDFDKTNAAGETPLMMASLQNE-LDLVKLMVD-QMEVEINKTgwtpLHYAATNGNNDIVKFLVD 142
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENEnLELTELLLNlSCRGAVGDT----LLHAISLEYVDAVEAILL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 143 HAAYIDAESPN--------------GTTPLMMAARGGHIETVKLLLDEGAD 179
Cdd:TIGR00870 103 HLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGAS 153
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 123-179 4.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 4.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1757249820 123 TPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETVKLLLDEGAD 179
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
Ank_5 pfam13857
Ankyrin repeats (many copies);
75-128 4.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 4.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1757249820  75 LIRAKDIDFDKTNAAGETPLMMASLQNELDLVKLMVDqMEVEIN---KTGWTPLHYA 128
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNlkdEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 55-174 8.96e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.78  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  55 KGNPMLVVALREKSLKVAEALI--------RAKDIDFDKTNAA-----GETPLMMASLQNELDLVKLMVD--QMEVEINK 119
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVengadvhaHAKGRFFQPKYQGegfyfGELPLSLAACTNQPDIVQYLLEneHQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1757249820 120 T---GWTPLHYAA-----TNGNNDIVKFLVDHAAYIDAE-----------SPNGTTPLMMAARGGHIETVKLLL 174
Cdd:cd22193   155 QdsrGNTVLHALVtvadnTKENTKFVTRMYDMILIRGAKlcptveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 87-208 1.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  87 NAAGETPLMmASLQNE---LDLVKLMVDQ---MEVEINKTGWTPLHYAAT---NGNNDIVKFLVDHAAYIDAESPNGTTP 157
Cdd:PHA02859   48 NDLYETPIF-SCLEKDkvnVEILKFLIENgadVNFKTRDNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1757249820 158 L--MMAARGGHIETVKLLLDEGADMRLKNQQGMTVIDFAERYH-QKEIAEGLKS 208
Cdd:PHA02859  127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHsDKKIFDFLTS 180
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 102-191 1.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.34  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 102 ELDLVKLMVDQmEVEINKTGW--TPL------HYAATNGNNDIVKFLVDHAAYIDAESPNGTTPLMMAARGGHIETV--- 170
Cdd:PHA02989   49 KIKIVKLLIDN-GADVNYKGYieTPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCdml 127

                          90       100
                  ....*....|....*....|..
gi 1757249820 171 KLLLDEGADMR-LKNQQGMTVI 191
Cdd:PHA02989  128 RFLLSKGINVNdVKNSRGYNLL 149
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 156-179 2.73e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 2.73e-03
                          10        20
                  ....*....|....*....|....
gi 1757249820 156 TPLMMAARGGHIETVKLLLDEGAD 179
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 30-190 3.27e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.14  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  30 AVEFDDVKAAQKLL--ARGVDPNLVDAKG-NPMLVVALREKSLKVAEALIrakdiDFDKTNAAGETPLMMASL-----QN 101
Cdd:TIGR00870  24 AAERGDLASVYRDLeePKKLNINCPDRLGrSALFVAAIENENLELTELLL-----NLSCRGAVGDTLLHAISLeyvdaVE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 102 ELDLVKLMVD------QMEVEINKT----GWTPLHYAATNGNNDIVKFLVDHAAYIDA--------ESPN------GTTP 157
Cdd:TIGR00870  99 AILLHLLAAFrksgplELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvKSQGvdsfyhGESP 178

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1757249820 158 LMMAARGGHIETVKLLLDEGADMRLKNQQGMTV 190
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSEDPADILTADSLGNTL 211
PHA02798 PHA02798
ankyrin-like protein; Provisional
 103-191 4.99e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 103 LDLVKLM------VDQMEVEINktgwTPLHYAATNGNN-----DIVKFLVDHAAYIDAESPNGTTPLMMAARGGHI---E 168
Cdd:PHA02798   51 TDIVKLFinlganVNGLDNEYS----TPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlE 126

                          90       100
                  ....*....|....*....|...
gi 1757249820 169 TVKLLLDEGADMRLKNQQGMTVI 191
Cdd:PHA02798  127 ILLFMIENGADTTLLDKDGFTML 149
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 55-174 5.01e-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: 37.82  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  55 KGNPMLVVALREKSLKVAEALI--------RAKDIDFDKTNAA-----GETPLMMASLQNELDLVKLMVDQMEVEI---N 118
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIakgadvnaHAKGVFFNPKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDItsqD 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757249820 119 KTGWTPLHYAAT-----NGNNDIVKFLVDHaayIDAESPN----------GTTPLMMAARGGHIETVKLLL 174
Cdd:cd22194   220 SRGNTVLHALVTvaedsKTQNDFVKRMYDM---ILLKSENknletirnneGLTPLQLAAKMGKAEILKYIL 287
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 67-179 6.80e-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: 37.05  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820  67 KSLKVAEALIRAKDIDFDKTNAA--GETPLMMASLQ----------------NELDLVKLMVDQMEVEINKTGWTPLHYA 128
Cdd:cd22194    69 KDLSRRRRKTDVPDFLMHKLTASdtGKTCLMKALLNinentkeivrillafaEENGILDRFINAEYTEEAYEGQTALNIA 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757249820 129 ATNGNNDIVKFLVDHAAYIDAESPN--------------GTTPLMMAARGGHIETVKLLLDEGAD 179
Cdd:cd22194   149 IERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEST 213
PHA02946 PHA02946
ankyin-like protein; Provisional
 116-209 6.91e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 36.96  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757249820 116 EINKTGWTPLHYAATNGNNDIVKFLVDHAAYIDAESPNGTTPL--MMAARGGHIETVKLLLDEGADMRLK-NQQG----M 188
Cdd:PHA02946   67 ETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINNSvDEEGcgplL 146

                          90       100
                  ....*....|....*....|.
gi 1757249820 189 TVIDFAERYHQKEIAEGLKSR 209
Cdd:PHA02946  147 ACTDPSERVFKKIMSIGFEAR 167
 
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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