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Conserved domains on  [gi|164664508|ref|NP_005169|]
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B-cell lymphoma 3 protein [Homo sapiens]

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];
121-359 9.42e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 9.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 121 LSADIAMATRADEDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 200
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDL----LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 201 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 280
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGA----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPL 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164664508 281 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILR 359
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-359 9.42e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 9.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 121 LSADIAMATRADEDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 200
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDL----LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 201 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 280
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGA----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPL 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164664508 281 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILR 359
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-272 2.27e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  176 LHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAapgtlDLEARNYdGLTALHVAVNTECQ 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 164664508  256 ETVQLLLERGADIDAVD 272
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-334 3.73e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 137 TPLHIAVvQGNLPAVhrLVNLFQQGGReLDIYNNLRQTPLHL-----AVITTLPSVVRLLVTAGASPMALDRHGQTAAHL 211
Cdd:PHA03100  37 LPLYLAK-EARNIDV--VKILLDNGAD-INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 212 ACEHR--SPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQET--VQLLLERGADIDA-------------VDIK 274
Cdd:PHA03100 113 AISKKsnSYSIVEYLLDNGA----NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAknrvnyllsygvpINIK 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164664508 275 S--GRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 334
Cdd:PHA03100 189 DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 174-314 8.70e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.88  E-value: 8.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 174 TPLHLAVITT-LPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDsAAPGTLDLEARN--YDGLTALHVAV 250
Cdd:cd22192   19 SPLLLAAKENdVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlYQGETALHIAV 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164664508 251 NTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALH 314
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 240-314 8.92e-08

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: 54.70  E-value: 8.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  240 YDGLTALHVAVNTECQETVQLLLERGADIDA------------VD-IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQM 306
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsFYHGESPLNAAACLGSPSIVALLSEDPADILTAD 205


                  ....*...
gi 164664508  307 YSGSSALH 314
Cdd:TIGR00870 206 SLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 276-304 4.80e-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: 42.96  E-value: 4.80e-06
                           10        20
                   ....*....|....*....|....*....
gi 164664508   276 GRSPLIHAVENNSLSMVQLLLQHGANVNA 304
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-359 9.42e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 9.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 121 LSADIAMATRADEDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 200
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDL----LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 201 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 280
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGA----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPL 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164664508 281 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILR 359
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-346 4.82e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 4.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 121 LSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLfqqgGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 200
Cdd:COG0666   73 LLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 201 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 280
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGA----DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTAL 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164664508 281 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL 346
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-359 6.13e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 6.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 152 HRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApg 231
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 232 tlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSS 311
Cdd:COG0666   79 --DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164664508 312 ALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILR 359
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-272 2.27e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  176 LHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAapgtlDLEARNYdGLTALHVAVNTECQ 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 164664508  256 ETVQLLLERGADIDAVD 272
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
246-339 2.48e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  246 LHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHgANVNAQMYsGSSALHSASGRGLLPLV 325
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 164664508  326 RTLVRSGADSSLKN 339
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-305 2.82e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  210 HLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERgADIDAVDikSGRSPLIHAVENNSL 289
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGA----DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHL 74

                          90
                  ....*....|....*.
gi 164664508  290 SMVQLLLQHGANVNAQ 305
Cdd:pfam12796  75 EIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-334 3.73e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 137 TPLHIAVvQGNLPAVhrLVNLFQQGGReLDIYNNLRQTPLHL-----AVITTLPSVVRLLVTAGASPMALDRHGQTAAHL 211
Cdd:PHA03100  37 LPLYLAK-EARNIDV--VKILLDNGAD-INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 212 ACEHR--SPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQET--VQLLLERGADIDA-------------VDIK 274
Cdd:PHA03100 113 AISKKsnSYSIVEYLLDNGA----NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAknrvnyllsygvpINIK 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164664508 275 S--GRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 334
Cdd:PHA03100 189 DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 134-303 1.81e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 134 DGDTPLHIAVVQGNLPAVHRLVNLfqqGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLAC 213
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDL---GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 214 EHRSPTCLRALLDSAApgTLDLEarNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQ 293
Cdd:PHA02875 144 MMGDIKGIELLIDHKA--CLDIE--DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVR 219

                        170
                 ....*....|
gi 164664508 294 LLLQHGANVN 303
Cdd:PHA02875 220 LFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 132-349 3.97e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 3.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 132 DEDGDTPLHIAVvqgNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSV-VRLLVTAGASPMALDRHGQTAAH 210
Cdd:PHA02876 270 DDCKNTPLHHAS---QAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 211 LACE-HRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSL 289
Cdd:PHA02876 347 QASTlDRNKDIVITLLELGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPY 422

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164664508 290 SMVQLLLQHGANVNAQMYSGSSALHSASGRGLLP-LVRTLVRSGADSSLKNCHNDTPLMVA 349
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA03095 PHA03095
ankyrin-like protein; Provisional
 123-366 3.06e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 123 ADIAMATRAdedGDTPLHIAVVQGNlpaVHRLVNLFQQGGRELDIYNNLRQTPLH--LAVITTLPSVVRLLVTAGASPMA 200
Cdd:PHA03095  74 ADVNAPERC---GFTPLHLYLYNAT---TLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNA 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 201 LDRHGQTAahLACEHRSPTC----LRALLDSAApgtlDLEARNYDGLTALHV-AVNTECQETV-QLLLERGADIDAVDIk 274
Cdd:PHA03095 148 LDLYGMTP--LAVLLKSRNAnvelLRLLIDAGA----DVYAVDDRFRSLLHHhLQSFKPRARIvRELIRAGCDPAATDM- 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 275 SGRSPLIHAVENNSL--SMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSR 352
Cdd:PHA03095 221 LGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300

                        250
                 ....*....|....*
gi 164664508 353 RVIDILRGK-ATRPA 366
Cdd:PHA03095 301 NNGRAVRAAlAKNPS 315
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 133-363 3.73e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 3.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 133 EDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDrhgqtaahLA 212
Cdd:PHA02874  33 DETTTPLIDAIRSGDA----KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP--------IP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 213 CEHRSptCLRALLDSAapgtLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIkSGRSPLIHAVENNSLSMV 292
Cdd:PHA02874 101 CIEKD--MIKTILDCG----IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDII 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164664508 293 QLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKnCHND-TPLMVA--RSRRVIDILRGKAT 363
Cdd:PHA02874 174 KLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGfTPLHNAiiHNRSAIELLINNAS 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 239-359 3.97e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 3.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 239 NYDGL---TALHVAVNTECQ---ETVQLLLERGADIDAVDIkSGRSPLIHAVENNS-LSMVQLLLQHGANVNAQMYSGSS 311
Cdd:PHA03095  41 NFRGEygkTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER-CGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRT 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 164664508 312 ALHS-ASGRGLLP-LVRTLVRSGADSSLKNCHNDTPLMVA-RSRRV-IDILR 359
Cdd:PHA03095 120 PLHVyLSGFNINPkVIRLLLRKGADVNALDLYGMTPLAVLlKSRNAnVELLR 171
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 130-359 6.22e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.38  E-value: 6.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 130 RADEDGDTPLHIAVVQGNLPAV------------------------HRLVNLFQ-------QGGRELDIYNnLRQTPLHL 178
Cdd:PHA02878  65 QPDHRDLTPLHIICKEPNKLGMkemirsinkcsvfytlvaikdafnNRNVEIFKiiltnryKNIQTIDLVY-IDKKSKDD 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 179 AVITtlpSVVRLLVTAGASPMALDRH-GQTAAHLACEHRSPTCLRALLDSAA-PGTLDlEARNYdgltALHVAVNTECQE 256
Cdd:PHA02878 144 IIEA---EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGAnVNIPD-KTNNS----PLHHAVKHYNKP 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 257 TVQLLLERGADIDAVDiKSGRSPLIHAVEN-NSLSMVQLLLQHGANVNAQMY-SGSSALHSA--SGRGLlplvRTLVRSG 332
Cdd:PHA02878 216 IVHILLENGASTDARD-KCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSikSERKL----KLLLEYG 290

                        250       260
                 ....*....|....*....|....*...
gi 164664508 333 ADSSLKNCHNDTPL-MVARSRRVIDILR 359
Cdd:PHA02878 291 ADINSLNSYKLTPLsSAVKQYLCINIGR 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
 174-349 2.14e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 174 TPLHLAVITTLP---SVVRLLVTAGASPMALDRHGQTAAHLACEHRS-PTCLRALLDSAApgtlDLEARNYDGLTALHVA 249
Cdd:PHA03095  49 TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA----DVNAKDKVGRTPLHVY 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 250 VNTEC--QETVQLLLERGADIDAVDiKSGRSPLIHAVENN--SLSMVQLLLQHGANVNAQMYSGSSALHS--ASGRGLLP 323
Cdd:PHA03095 125 LSGFNinPKVIRLLLRKGADVNALD-LYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRAR 203

                        170       180
                 ....*....|....*....|....*.
gi 164664508 324 LVRTLVRSGADSSLKNCHNDTPLMVA 349
Cdd:PHA03095 204 IVRELIRAGCDPAATDMLGNTPLHSM 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 175-359 2.17e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 175 PLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSaapgtldleaRNYDGLTALHVAVNTEC 254
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS----------INKCSVFYTLVAIKDAF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 255 -------------------------------------QETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQ 297
Cdd:PHA02878 110 nnrnveifkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLS 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164664508 298 HGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRV-IDILR 359
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILK 252
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-304 8.24e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 137 TPLHIAVVQG-NLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTL--PSVVRLLVTAGASPMALDRHGQTAAHLA- 212
Cdd:PHA03100  70 TPLHYLSNIKyNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYl 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 213 -CEHRSPTCLRALLDSAA------------PGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKsGRSP 279
Cdd:PHA03100 150 eSNKIDLKILKLLIDKGVdinaknrvnyllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDTP 228

                        170       180
                 ....*....|....*....|....*
gi 164664508 280 LIHAVENNSLSMVQLLLQHGANVNA 304
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-359 1.84e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  280 LIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVrSGADSSLKNcHNDTPLMVARSRRVIDILR 359
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 174-314 8.70e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.88  E-value: 8.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 174 TPLHLAVITT-LPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDsAAPGTLDLEARN--YDGLTALHVAV 250
Cdd:cd22192   19 SPLLLAAKENdVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlYQGETALHIAV 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164664508 251 NTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALH 314
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 154-349 9.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 9.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 154 LVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPgtl 233
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY--- 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 234 dLEARNYDGLTALHVAVNTECQETVQLLLERGADIdAVDIKSGRSPLIHAVENNSlSMVQLLLQHgANVNAQMYSGSSAL 313
Cdd:PHA02874 183 -ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPL 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 164664508 314 HSAsgrgLLP-----LVRTLVRSGADSSLKNCHNDTPLMVA 349
Cdd:PHA02874 259 HHA----INPpcdidIIDILLYHKADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-296 1.80e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.80e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 164664508  242 GLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLL 296
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 153-351 1.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 153 RLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApgt 232
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS--- 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 233 ldleARNYDGLTALHVAVNTECqETVQLLLERGADIDAVDIKSgRSPLIHAVENNSLS-MVQLLLQHGANVNAQMYSGSS 311
Cdd:PHA02876 236 ----NINKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCK-NTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 164664508 312 ALHSASGRGL-LPLVRTLVRSGADSSLKNCHNDTPLMVARS 351
Cdd:PHA02876 310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAST 350
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 142-366 2.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 142 AVVQGNLPAVHRLVNLFQQGGREldIYNNLrqTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCL 221
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFE--IYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 222 RALLDSaapGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDaVDIKSGRSPLIHAVENNSLSMVQLLLQHGAN 301
Cdd:PHA02875  85 EELLDL---GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164664508 302 VNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLM-VARSRRVIDILRGKATRPA 366
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
132-202 3.33e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 3.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164664508  132 DEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGReldiynNLRQTPLHLAVITTLPSVVRLLVTAGASPMALD 202
Cdd:pfam12796  27 DKNGRTALHLAAKNGHLEIVKLLLEHADVNLK------DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 191-343 4.20e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 191 LVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGAdidA 270
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC----NVHIRDANGNTALWNAISAKHHKIFRILYHFAS---I 616

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164664508 271 VDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHND 343
Cdd:PLN03192 617 SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-346 6.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 6.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 139 LHIAVVQGNLPAVHrlvNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSP 218
Cdd:PHA02874   5 LRMCIYSGDIEAIE---KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 219 TCLRALLDsaapgtldlearnyDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSgRSPLIHAVENNSLSMVQLLLQH 298
Cdd:PHA02874  82 DIIKLLID--------------NGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEY 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164664508 299 GANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL 346
Cdd:PHA02874 147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 222-317 1.77e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 222 RALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQH--- 298
Cdd:PTZ00322  99 RILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KDGKTPLELAEENGFREVVQLLSRHsqc 173

                         90       100
                 ....*....|....*....|...
gi 164664508 299 ----GANVNAQMYSGSSALHSAS 317
Cdd:PTZ00322 174 hfelGANAKPDSFTGKPPSLEDS 196
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 135-251 3.95e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 3.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 135 GDTPLHIAVVQGNLPAVHRLVN-------------LFQQGGRELDIYNnlrQTPLHLAVITTLPSVVRLLVTAGASPMAL 201
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIArgadvvspratgtFFRPGPKNLIYYG---EHPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164664508 202 DRHGQTAAH---------LACEhrsptCLRALLDSAAPG---TLDLeARNYDGLTALHVAVN 251
Cdd:cd22192  166 DSLGNTVLHilvlqpnktFACQ-----MYDLILSYDKEDdlqPLDL-VPNNQGLTPFKLAAK 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 132-280 6.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 132 DEDGDTPLHIAVVQGNlpavHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHL 211
Cdd:PHA02874 154 DDNGCYPIHIAIKHNF----FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164664508 212 ACEH-RSPTCLraLLDSAAPGTLDLearnyDGLTALHVAVNTEC-QETVQLLLERGADIDAVDIKsGRSPL 280
Cdd:PHA02874 230 AIIHnRSAIEL--LINNASINDQDI-----DGSTPLHHAINPPCdIDIIDILLYHKADISIKDNK-GENPI 292
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-272 8.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 8.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 132 DEDGDTPLHIAVVqgNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLP--SVVRLLVTAGASPMALDR------ 203
Cdd:PHA03100 103 DNNGITPLLYAIS--KKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnylls 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164664508 204 ----------HGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVD 272
Cdd:PHA03100 181 ygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGA----NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 240-314 8.92e-08

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: 54.70  E-value: 8.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  240 YDGLTALHVAVNTECQETVQLLLERGADIDA------------VD-IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQM 306
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsFYHGESPLNAAACLGSPSIVALLSEDPADILTAD 205


                  ....*...
gi 164664508  307 YSGSSALH 314
Cdd:TIGR00870 206 SLGNTLLH 213
Ank_4 pfam13637
Ankyrin repeats (many copies);
276-329 1.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164664508  276 GRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLV 329
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 220-315 1.98e-07

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 53.22  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 220 CLRALLDSAapgtldLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAV-------------DIKSGRSPLIHAVEN 286
Cdd:cd22194  125 ILDRFINAE------YTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykheGFYFGETPLALAACT 198

                         90       100       110
                 ....*....|....*....|....*....|
gi 164664508 287 NSLSMVQLLLQHGA-NVNAQMYSGSSALHS 315
Cdd:cd22194  199 NQPEIVQLLMEKEStDITSQDSRGNTVLHA 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 238-349 2.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 238 RNYDGLTALHVAVNTECQETVQLLLERGADIDAVdIKSGRSPL-----IHAVENNSLSMVQLLLQHGANVNAQMYSGSSA 312
Cdd:PHA03100  31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSS-TKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITP 109

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 164664508 313 LHSASGR--GLLPLVRTLVRSGADSSLKNCHNDTPLMVA 349
Cdd:PHA03100 110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 220-346 3.58e-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: 52.71  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 220 CLRALLDSAapgTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKS----GRSPLIHAVENNSLSMVQLL 295
Cdd:cd22192   32 AIKKLLKCP---SCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAVVNQNLNLVREL 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164664508 296 LQHGANVN--------------AQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL 346
Cdd:cd22192  109 IARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 205-314 1.15e-06

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: 51.03  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 205 GQTAAHLAC--EHRSPTCLRALLDSAAPGTLDLE--------ARNYDGLTALHVAVNTECQETVQLLLERGADIDAVD-- 272
Cdd:cd21882   26 GKTCLHKAAlnLNDGVNEAIMLLLEAAPDSGNPKelvnapctDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164664508 273 ----------IKSGRSPLIHAVENNSLSMVQLLLQHG---ANVNAQMYSGSSALH 314
Cdd:cd21882  106 rffrkspgnlFYFGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 135-307 1.99e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 135 GDTPLHIAVVQGNLPA-------VHRLVNLFQQGgrelDIYnnLRQTPLHLAVITTLPSVVRLLVTAGASPmaldrhgQT 207
Cdd:cd22192   51 GETALHVAALYDNLEAavvlmeaAPELVNEPMTS----DLY--QGETALHIAVVNQNLNLVRELIARGADV-------VS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 208 A-AHLACEHRSPTCLRalldsaapgtldlearnYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHaven 286
Cdd:cd22192  118 PrATGTFFRPGPKNLI-----------------YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD-SLGNTVLHI---- 175

                        170       180
                 ....*....|....*....|.
gi 164664508 287 nslsmvqLLLQHGANVNAQMY 307
Cdd:cd22192  176 -------LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 276-304 4.80e-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: 42.96  E-value: 4.80e-06
                           10        20
                   ....*....|....*....|....*....
gi 164664508   276 GRSPLIHAVENNSLSMVQLLLQHGANVNA 304
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 241-272 6.82e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 6.82e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 164664508  241 DGLTALHVAV-NTECQETVQLLLERGADIDAVD 272
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-264 1.40e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  135 GDTPLHIAVVQGNLPAVHRLV------------NLFQQGGRELDIYNNlrQTPLHLAVITTLPSVVRLLVTAGASPMALD 202
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLergasvparacgDFFVKSQGVDSFYHG--ESPLNAAACLGSPSIVALLSEDPADILTAD 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164664508  203 RHGQTAAHLA-------CEHRSPTC-----LRALLDSAAPgTLDLEA-RNYDGLTALHVAVNTECQETVQLLLER 264
Cdd:TIGR00870 206 SLGNTLLHLLvmenefkAEYEELSCqmynfALSLLDKLRD-SKELEViLNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PHA02741 PHA02741
hypothetical protein; Provisional
 268-359 1.67e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.03  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 268 IDAVDIKSGRSPLIHAVENN---SLSMVQLLLQHGANVNAQ-MYSGSSALHSASGRGLLPLVRTLVRS-GADSSLKNCHN 342
Cdd:PHA02741  53 LNATDDAGQMCIHIAAEKHEaqlAAEIIDHLIELGADINAQeMLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADN 132

                         90       100
                 ....*....|....*....|
gi 164664508 343 DTPLMVA---RSRRVIDILR 359
Cdd:PHA02741 133 KSPFELAidnEDVAMMQILR 152
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 123-179 1.97e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.48  E-value: 1.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164664508 123 ADIAMATRADedGDTPLHIAVVQGNlpavHRLVN-LFQQGGRELDIYNNLRQTPLHLA 179
Cdd:PHA02736  82 ADINGKERVF--GNTPLHIAVYTQN----YELATwLCNQPGVNMEILNYAFKTPYYVA 133
PHA03095 PHA03095
ankyrin-like protein; Provisional
 131-266 2.70e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 131 ADEDGDTPLHIAVVQGNLPAVhrLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAH 210
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKRS--LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164664508 211 LACEHRSPTCLRALLDSAAPgtLDLEARNYDGLTALHVAVNTEC-QETVQLLLERGA 266
Cdd:PHA03095 296 LMVRNNNGRAVRAALAKNPS--AETVAATLNTASVAGGDIPSDAtRLCVAKVVLRGA 350
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 292-349 3.81e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 3.81e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164664508 292 VQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 349
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 121-280 5.28e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 121 LSADIAmatraDEDGDTPLHIAVVQGNLPAVhrLVNLfqQGGRELDIYNNLRQTPLHLAVITTLPSVVRLL--VTAGASP 198
Cdd:PLN03192 549 LDPDIG-----DSKGRTPLHIAASKGYEDCV--LVLL--KHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDP 619

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 199 maldrhgQTAAHLACE---HRSPTCLRALLDSAapgtLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKS 275
Cdd:PLN03192 620 -------HAAGDLLCTaakRNDLTAMKELLKQG----LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688


                 ....*
gi 164664508 276 GRSPL 280
Cdd:PLN03192 689 DFSPT 693
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 240-315 5.37e-05

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: 45.57  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 240 YDGLTALHVAVNTECQETVQLLLERGADIDAV-------DIKS------GRSPLIHAVENNSLSMVQLLLQH---GANVN 303
Cdd:cd22196   92 YKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkKKKGgpgfyfGELPLSLAACTNQLDIVKFLLENphsPADIS 171

                         90
                 ....*....|..
gi 164664508 304 AQMYSGSSALHS 315
Cdd:cd22196  172 ARDSMGNTVLHA 183
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-212 5.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 5.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164664508  157 LFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLA 212
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 276-305 5.79e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 5.79e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 164664508  276 GRSPLIHAV-ENNSLSMVQLLLQHGANVNAQ 305
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 276-304 7.64e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 7.64e-05
                          10        20
                  ....*....|....*....|....*....
gi 164664508  276 GRSPLIHAVENNSLSMVQLLLQHGANVNA 304
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 240-315 1.24e-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: 44.40  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 240 YDGLTALHVAVNTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHG---ANVN 303
Cdd:cd22193   74 YEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegFYFGELPLSLAACTNQPDIVQYLLENEhqpADIE 153

                         90
                 ....*....|..
gi 164664508 304 AQMYSGSSALHS 315
Cdd:cd22193  154 AQDSRGNTVLHA 165
Ank_5 pfam13857
Ankyrin repeats (many copies);
231-283 1.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 164664508  231 GTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHA 283
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
261-316 2.56e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164664508  261 LLERG-ADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSA 316
Cdd:pfam13857   1 LLEHGpIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-249 3.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  190 LLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDsaapGTLDLEARNYDGLTALHVA 249
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA----YGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 241-270 6.61e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 6.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 164664508   241 DGLTALHVAVNTECQETVQLLLERGADIDA 270
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 240-315 6.98e-04

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


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 42.15  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 240 YDGLTALHVAVNTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHG---ANVN 303
Cdd:cd22195  135 YRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyFYFGELPLSLAACTNQPDIVHYLTENAhkkADLR 214

                         90
                 ....*....|..
gi 164664508 304 AQMYSGSSALHS 315
Cdd:cd22195  215 RQDSRGNTVLHA 226
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 239-333 7.56e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 239 NYDGLTALHVAVN---TECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLL-QHGANVNAQMYSGSSALH 314
Cdd:PHA02736  52 NRHGKQCVHIVSNpdkADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYY 131

                         90
                 ....*....|....*....
gi 164664508 315 SASGRGLLPLVRTLVRSGA 333
Cdd:PHA02736 132 VACERHDAKMMNILRAKGA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
295-349 1.12e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164664508  295 LLQHG-ANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 349
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 155-214 1.17e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 155 VNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACE 214
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 135-264 1.41e-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: 41.02  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 135 GDTPLHIAVVQGNLPAVHRLV------------NLFQQGGRELDIYNNLrqtPLHLAVITTLPSVVRLLVTAGASPMAL- 201
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVengadvsaratgRFFRKSPGNLFYFGEL---PLSLAACTNQEEIVRLLLENGAQPAALe 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164664508 202 --DRHGQTAAHLACEHRSPTCLR-ALLDSAAPGTLDLEAR-----------NYDGLTALHVAVNTECQETVQLLLER 264
Cdd:cd21882  150 aqDSLGNTVLHALVLQADNTPENsAFVCQMYNLLLSYGAHldptqqleeipNHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-262 1.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 164664508  207 TAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAV---NTECqetVQLLL 262
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGA----DINAVDGNGETALHFAAsngNVEV---LKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 258-374 2.65e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 258 VQLLLERGADIDAVDIkSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLvrsgadSSL 337
Cdd:PTZ00322  98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL------SRH 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 164664508 338 KNCHNDtplmvARSRRVIDILRGKATR----PASTSQPDPS 374
Cdd:PTZ00322 171 SQCHFE-----LGANAKPDSFTGKPPSledsPISSHHPDFS 206
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-204 2.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164664508 132 DEDGDTPLHIAVVQGNLPAVHRLVNLfqqgGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRH 204
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLDL----GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-225 2.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 164664508  174 TPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALL 225
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 205-301 3.02e-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: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508 205 GQTAAHLACEHRSPTCLRALLDSAApgtlDLEARN--------------YDGLTALHVAVNTECQETVQLLLE---RGAD 267
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGA----DVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPAD 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 164664508 268 IDAVDikSGRSPLIHA--------VENNSL--SMVQLLLQHGAN 301
Cdd:cd22193  152 IEAQD--SRGNTVLHAlvtvadntKENTKFvtRMYDMILIRGAK 193
Ank_4 pfam13637
Ankyrin repeats (many copies);
135-192 5.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 5.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164664508  135 GDTPLHIAVVQGNLPAVHRLVNLfqqgGRELDIYNNLRQTPLHLAVITTLPSVVRLLV 192
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK----GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 241-303 5.61e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 5.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164664508 241 DGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL--IHAVENNSLSMVQLLLQHGANVN 303
Cdd:PHA02946  71 DGNYPLHIASKINNNRIVAMLLTHGADPNACD-KQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 230-343 6.86e-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: 38.91  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664508  230 PGTLDLEARNYDGLTAL-HVAVNTECQETVQLLLERGADIDAVDiksgrsPLIHAVENNSLSMVQLLLQHGAN------- 301
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGD------TLLHAISLEYVDAVEAILLHLLAafrksgp 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 164664508  302 ---VNAQM----YSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHND 343
Cdd:TIGR00870 114 lelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDF 162
 
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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