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Conserved domains on  [gi|10092619|ref|NP_065390|]
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NF-kappa-B inhibitor alpha [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];
75-256 9.42e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 9.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  75 DSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQ 154
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 155 GCLASVGVLtqscttphlhsiLK------ATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQ 228
Cdd:COG0666 131 GNLEIVKLL------------LEagadvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENG 197

                       170       180
                ....*....|....*....|....*...
gi 10092619 229 NPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:COG0666 198 HLEIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-256 9.42e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 9.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  75 DSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQ 154
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 155 GCLASVGVLtqscttphlhsiLK------ATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQ 228
Cdd:COG0666 131 GNLEIVKLL------------LEagadvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENG 197

                       170       180
                ....*....|....*....|....*...
gi 10092619 229 NPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:COG0666 198 HLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-212 1.47e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   115 LHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQscttphlHSILKATNyNGHTCLHLASIHG 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKD-NGRTALHYAARSG 72

                          90
                  ....*....|....*...
gi 10092619   195 YLGIVELLVSLGADVNAQ 212
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 113-253 4.96e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 4.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  113 TPLHL-----AVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQgCLASVGVLTqscTTPHLHSILKATNYNGHTCL 187
Cdd:PHA03100  70 TPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK-KSNSYSIVE---YLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  188 HLA--SIHGYLGIVELLVSLGADVNAQE----------PCN-----GRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQG 250
Cdd:PHA03100 146 HLYleSNKIDLKILKLLIDKGVDINAKNrvnyllsygvPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ...
gi 10092619  251 YSP 253
Cdd:PHA03100 226 DTP 228
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-244 2.48e-09

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: 58.17  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   105 NFQNNLQQTPLHLAVITNQP-EIAEALLGAGCDPELrdfrGNTPLHLACE---QGCLASVGVLTQ----SCTTPHLHSIL 176
Cdd:TIGR00870  46 NCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLeyvDAVEAILLHLLAafrkSGPLELANDQY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   177 KATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCN-------------GRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:TIGR00870 122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADI 201


                  .
gi 10092619   244 N 244
Cdd:TIGR00870 202 L 202
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 110-257 2.63e-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: 55.02  E-value: 2.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 110 LQQTPLHLAVITNQPEIAEALLGagCDPELRD-------FRGNTPLHLACEQGCLASVGVL------------TQSCTTP 170
Cdd:cd22192  50 LGETALHVAALYDNLEAAVVLME--AAPELVNepmtsdlYQGETALHIAVVNQNLNLVRELiargadvvspraTGTFFRP 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 171 HLHSILkatnYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEpCNGRTALHLAVDLQNPDLV----SLLLKCGADVNRV 246
Cdd:cd22192 128 GPKNLI----YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD-SLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQ 202

                       170
                ....*....|....*..
gi 10092619 247 T------YQGYSPYQLT 257
Cdd:cd22192 203 PldlvpnNQGLTPFKLA 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-211 5.05e-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: 42.57  E-value: 5.05e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 10092619    182 NGHTCLHLASIHGYLGIVELLVSLGADVNA 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-256 9.42e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 9.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  75 DSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQ 154
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 155 GCLASVGVLtqscttphlhsiLK------ATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQ 228
Cdd:COG0666 131 GNLEIVKLL------------LEagadvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENG 197

                       170       180
                ....*....|....*....|....*...
gi 10092619 229 NPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:COG0666 198 HLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-253 1.27e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 1.27e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  71 TEDGDSFLHLAIIHEEKaltmEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHL 150
Cdd:COG0666  84 DDGGNTLLHAAARNGDL----EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 151 ACEQGCLASVGVLTQSCTTPHlhsilkATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQNP 230
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVN------ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNL 232

                       170       180
                ....*....|....*....|...
gi 10092619 231 DLVSLLLKCGADVNRVTYQGYSP 253
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-253 8.57e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 8.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  73 DGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLAC 152
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 153 EQGCLASVGVLTQScttphlHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQNPDL 232
Cdd:COG0666  96 RNGDLEIVKLLLEA------GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEI 168

                       170       180
                ....*....|....*....|.
gi 10092619 233 VSLLLKCGADVNRVTYQGYSP 253
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-212 1.47e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   115 LHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQscttphlHSILKATNyNGHTCLHLASIHG 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKD-NGRTALHYAARSG 72

                          90
                  ....*....|....*...
gi 10092619   195 YLGIVELLVSLGADVNAQ 212
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 113-253 4.96e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 4.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  113 TPLHL-----AVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQgCLASVGVLTqscTTPHLHSILKATNYNGHTCL 187
Cdd:PHA03100  70 TPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK-KSNSYSIVE---YLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  188 HLA--SIHGYLGIVELLVSLGADVNAQE----------PCN-----GRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQG 250
Cdd:PHA03100 146 HLYleSNKIDLKILKLLIDKGVDINAKNrvnyllsygvPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ...
gi 10092619  251 YSP 253
Cdd:PHA03100 226 DTP 228
PHA02741 PHA02741
hypothetical protein; Provisional
 140-256 6.21e-13

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 65.83  E-value: 6.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  140 RDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHG----YLGIVELLVSLGADVNAQEPC 215
Cdd:PHA02741  17 KNSEGENFFHEAARCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEML 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 10092619  216 NGRTALHLAVDLQNPDLVSLLL-KCGADVNRVTYQGYSPYQL 256
Cdd:PHA02741  97 EGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFEL 138
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 109-253 1.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  109 NLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQScttphlHSILKATNYNGHTCLH 188
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN------GASTDARDKCGNTPLH 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10092619  189 LASihGYL---GIVELLVSLGADVNAQEPCNGRTALHLAvdLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02878 240 ISV--GYCkdyDILKLLLEHGVDVNAKSYILGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTP 303
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-253 2.32e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   75 DSFLHLAIIHEE---------KALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQP---EIAEALLGAGCDPELRDF 142
Cdd:PHA03095   2 EEDESVDIIMEAalydyllnaSNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  143 RGNTPLHLaceqgCLasvgvltqscttphlhsilkatnYNGHTclhlasihgyLGIVELLVSLGADVNAQEPCnGRTALH 222
Cdd:PHA03095  82 CGFTPLHL-----YL-----------------------YNATT----------LDVIKLLIKAGADVNAKDKV-GRTPLH 122

                        170       180       190
                 ....*....|....*....|....*....|...
gi 10092619  223 --LAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA03095 123 vyLSGFNINPKVIRLLLRKGADVNALDLYGMTP 155
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 76-253 1.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   76 SFLHLAIiheeKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQG 155
Cdd:PHA02874 126 TFLHYAI----KKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  156 CLASVGVLTQscttpHLHSILKATNyNGHTCLHLASIHGYlGIVELLVSlGADVNAQEpCNGRTALHLAvdLQNP---DL 232
Cdd:PHA02874 202 DYACIKLLID-----HGNHIMNKCK-NGFTPLHNAIIHNR-SAIELLIN-NASINDQD-IDGSTPLHHA--INPPcdiDI 270

                        170       180
                 ....*....|....*....|.
gi 10092619  233 VSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02874 271 IDILLYHKADISIKDNKGENP 291
PHA03095 PHA03095
ankyrin-like protein; Provisional
 104-253 1.93e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  104 LNFQNNLQQTPLHLAVITNQ--PEIAEALLGAGCDPELRDFRGNTPLHLACeQGCLASVGV---LTQSCTTPhlhsilKA 178
Cdd:PHA03095 145 VNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHL-QSFKPRARIvreLIRAGCDP------AA 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10092619  179 TNYNGHTCLHLASIHGYL--GIVELLVSLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 113-247 1.94e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  113 TPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILkatnynGHTCLHLASI 192
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC------GCTPLIIAMA 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 10092619  193 HGYLGIVELLVSLGADVN--AQEPCngRTALHLAVDLQNPDLVSLLLKCGADVNRVT 247
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDyfGKNGC--VAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 104-253 6.76e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  104 LNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQScttphlHSILKATNYNG 183
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK------GAYANVKDNNG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10092619  184 HTCLHLASIHGYLGIVELLVSLGADVNAQepCN-GRTALHLAVdLQNPDLVSLLLKcGADVNRVTYQGYSP 253
Cdd:PHA02874 191 ESPLHNAAEYGDYACIKLLIDHGNHIMNK--CKnGFTPLHNAI-IHNRSAIELLIN-NASINDQDIDGSTP 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 114-244 9.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 9.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  114 PLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLAC----EQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHL 189
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10092619  190 ASIHGYLG---------------------IVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:PHA02878 120 ILTNRYKNiqtidlvyidkkskddiieaeITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVN 195
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-244 2.48e-09

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: 58.17  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   105 NFQNNLQQTPLHLAVITNQP-EIAEALLGAGCDPELrdfrGNTPLHLACE---QGCLASVGVLTQ----SCTTPHLHSIL 176
Cdd:TIGR00870  46 NCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLeyvDAVEAILLHLLAafrkSGPLELANDQY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   177 KATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCN-------------GRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:TIGR00870 122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADI 201


                  .
gi 10092619   244 N 244
Cdd:TIGR00870 202 L 202
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 128-256 9.06e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 9.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  128 EALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHL-----------------HSILK-----ATNYNGHT 185
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIrdangntalwnaisakhHKIFRilyhfASISDPHA 621

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10092619  186 ---CLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRV-TYQGYSPYQL 256
Cdd:PLN03192 622 agdLLCTAAKRNDLTAMKELLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPTEL 695
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 140-265 9.52e-09

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 53.73  E-value: 9.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  140 RDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHsILKATNYNGHTCLHLASIHGYLGIVE---LLVSLGADVNAQEPCN 216
Cdd:PHA02736  13 PDIEGENILHYLCRNGGVTDLLAFKNAISDENRY-LVLEYNRHGKQCVHIVSNPDKADPQEklkLLMEWGADINGKERVF 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 10092619  217 GRTALHLAVDLQNPDLVSLLL-KCGADVNRVTYQGYSPYQLTWGRPSTRI 265
Cdd:PHA02736  92 GNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKM 141
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-151 1.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 1.22e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 10092619   104 LNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLA 151
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 110-257 2.63e-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: 55.02  E-value: 2.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 110 LQQTPLHLAVITNQPEIAEALLGagCDPELRD-------FRGNTPLHLACEQGCLASVGVL------------TQSCTTP 170
Cdd:cd22192  50 LGETALHVAALYDNLEAAVVLME--AAPELVNepmtsdlYQGETALHIAVVNQNLNLVRELiargadvvspraTGTFFRP 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 171 HLHSILkatnYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEpCNGRTALHLAVDLQNPDLV----SLLLKCGADVNRV 246
Cdd:cd22192 128 GPKNLI----YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD-SLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQ 202

                       170
                ....*....|....*..
gi 10092619 247 T------YQGYSPYQLT 257
Cdd:cd22192 203 PldlvpnNQGLTPFKLA 219
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 118-256 4.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  118 AVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLhsilkatNYNG-HTCLHLASIHGYL 196
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV-------KYPDiESELHDAVEEGDV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  197 GIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:PHA02875  82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-141 1.42e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10092619    69 QLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLaflnfqNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRD 141
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL------KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 27-151 3.21e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   27 DDRHDSGLDSMKD--EEYEQMVKELQEIRLEPQEVPRGsepwkqqltedGDSFLHLAIIHEEKALTmeVIRQVKGDLAFL 104
Cdd:PHA03095 184 DDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDML-----------GNTPLHSMATGSSCKRS--LVLPLLIAGISI 250

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 10092619  105 NFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLA 151
Cdd:PHA03095 251 NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 30-253 4.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   30 HDSG-----LDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTedGDSFLHLAiihEEKALTMEVIRQVKGDLAFL 104
Cdd:PHA02876 260 YDAGfsvnsIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIK--GETPLYLM---AKNGYDTENIRTLIMLGADV 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  105 NFQNNLQQTPLHLA-VITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQscttphLHSILKATNYNG 183
Cdd:PHA02876 335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD------YGADIEALSQKI 408

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10092619  184 HTCLHLA--SIHGYLGiVELLVSLGADVNAQEPcNGRTALHLAVDLQ-NPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02876 409 GTALHFAlcGTNPYMS-VKTLIDRGANVNSKNK-DLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP 479
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-237 5.46e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 5.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 10092619   183 GHTCLHLASIHGYLGIVELLVSLGADVNAQePCNGRTALHLAVDLQNPDLVSLLL 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 180-269 1.30e-06

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 47.50  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  180 NYNGHTCLHLASIHGYLGIV---ELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLK-CGADVNRVTYQGYSPYQ 255
Cdd:PHA02743  54 DHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRqLGVNLGAINYQHETAYH 133

                         90
                 ....*....|....
gi 10092619  256 LTWGRPSTRIQQQL 269
Cdd:PHA02743 134 IAYKMRDRRMMEIL 147
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 105-253 1.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  105 NFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTphlhsILKATNYNGH 184
Cdd:PHA02875  29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKF-----ADDVFYKDGM 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  185 TCLHLASIHGYLGIVELLVSLGADVNAqePCNGRTA-LHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDI--PNTDKFSpLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-253 1.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  102 AFLNFQNNLQQTPLHL--AVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVgvltqsctTPHL---HSIL 176
Cdd:PHA02876 229 AIIDNRSNINKNDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL--------VPKLlerGADV 300

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10092619  177 KATNYNGHTCLHLASIHGY-LGIVELLVSLGADVNAQEPCNgRTALHLAVDL-QNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLY-ITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-215 1.53e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  104 LNFQNNLQQTPLHLAVITNQP--EIAEALL--GA--------------GCDPELRDFRGNTPLHLACEQGCLASVGVLTQ 165
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIdlKILKLLIdkGVdinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 10092619  166 SCTTPHLhsilkaTNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPC 215
Cdd:PHA03100 214 LGANPNL------VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 127-204 2.12e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 2.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10092619  127 AEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLhsilkaTNYNGHTCLHLASIHGYLGIVELLVS 204
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL------LDKDGKTPLELAEENGFREVVQLLSR 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 73-250 2.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   73 DGDSFLHLAIiheeKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGC---DPELRDfrGNTPLH 149
Cdd:PHA02875  34 DGISPIKLAM----KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLH 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  150 LACEQGCLASVGVLTQSCTTPHLHSILKATNynghtcLHLASIHGYLGIVELLVSLGADVNAqEPCNGRTALHLAVDLQN 229
Cdd:PHA02875 108 LATILKKLDIMKLLIARGADPDIPNTDKFSP------LHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGD 180

                        170       180
                 ....*....|....*....|.
gi 10092619  230 PDLVSLLLKCGADVNRVTYQG 250
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNG 201
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-212 2.40e-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: 43.43  E-value: 2.40e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 10092619   182 NGHTCLHLASIH-GYLGIVELLVSLGADVNAQ 212
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-247 3.53e-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: 43.05  E-value: 3.53e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 10092619   216 NGRTALHLAVD-LQNPDLVSLLLKCGADVNRVT 247
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 180-239 4.19e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 4.19e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  180 NYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKC 239
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-244 4.77e-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: 42.63  E-value: 4.77e-06
                          10        20
                  ....*....|....*....|....*....
gi 10092619   216 NGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-211 5.05e-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: 42.57  E-value: 5.05e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 10092619    182 NGHTCLHLASIHGYLGIVELLVSLGADVNA 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-224 7.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 10092619   171 HLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCnGRTALHLA 224
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE-GLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 125-253 1.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  125 EIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSIlkatnyNGHTCLHLASIHGYLGIVELLVS 204
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD------NGCYPIHIAIKHNFFDIIKLLLE 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 10092619  205 LGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02874 179 KGAYANVKDN-NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-244 2.18e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 2.18e-05
                           10        20
                   ....*....|....*....|....*....
gi 10092619    216 NGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 196-252 3.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 3.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 10092619  196 LGIVELLVSLGADVNAQEpCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYS 252
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-243 3.80e-05

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: 45.00  E-value: 3.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 100 DLAFLNFQNNLQQTPLHLAVITNQPEIAEALLG-AGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSctTPHL-HSILK 177
Cdd:cd22192   6 DELHLLQQKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELvNEPMT 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10092619 178 ATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCN-------------GRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:cd22192  84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 183-243 3.90e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 3.90e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10092619 183 GHTCLHLASIH---GYLGIVELLVSLGAD-------VNAQ---EPCNGRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:cd21882  26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPctdEFYQGQTALHIAIENRNLNLVRLLVENGADV 99
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 112-171 8.48e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 8.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  112 QTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPH 171
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 74-149 9.25e-05

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: 43.98  E-value: 9.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  74 GDSFLHLAIIHEEKALTMEVIR-------QVKGDlaFLNFQNNLQ-----QTPLHLAVITNQPEIAEALLGAGCDP-ELR 140
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAkgadvnaHAKGV--FFNPKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDiTSQ 218


                ....*....
gi 10092619 141 DFRGNTPLH 149
Cdd:cd22194 219 DSRGNTVLH 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
144-203 9.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 9.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   144 GNTPLHLACEQGCLASVGVLTQscttpHLHSILkATNYNGHTCLHLASIHGYLGIVELLV 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE-----KGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 97-253 1.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619   97 VKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGC------LASVGVLTQSCTTP 170
Cdd:PHA02874  21 IKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAhdiiklLIDNGVDTSILPIP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  171 HLH-----SILKA------TNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKC 239
Cdd:PHA02874 101 CIEkdmikTILDCgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDIIKLLLEK 179

                        170
                 ....*....|....
gi 10092619  240 GADVNRVTYQGYSP 253
Cdd:PHA02874 180 GAYANVKDNNGESP 193
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-243 1.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  102 AFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLA-CEQGCLASVGVLTQSCTTphlhsiLKATN 180
Cdd:PHA02876 366 ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGAN------VNSKN 439

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10092619  181 YNGHTCLHLASIHG-YLGIVELLVSLGADVNAqepCNGRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:PHA02876 440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNA---INIQNQYPLLIALEYHGIVNILLHYGAEL 500
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-155 2.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 10092619   113 TPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQG 155
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 180-237 3.29e-04

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: 42.44  E-value: 3.29e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10092619 180 NYNGHTCLHLASIHGYLGIVELLVSLGADVNAQ------EPCN-------GRTALHLAVDLQNPDLVSLLL 237
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffNPKYkhegfyfGETPLALAACTNQPEIVQLLM 208
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 40-203 3.83e-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: 41.99  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619    40 EEYEQMVKELQEIRLEpqeVPRGSEPWKQQLTEDGDSF------LHLAIIHEE----KALTME-------------VIRQ 96
Cdd:TIGR00870  91 LEYVDAVEAILLHLLA---AFRKSGPLELANDQYTSEFtpgitaLHLAAHRQNyeivKLLLERgasvparacgdffVKSQ 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619    97 VKGDLAFlnfqnnlQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLA-------CEQGCLAS------VGVL 163
Cdd:TIGR00870 168 GVDSFYH-------GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELSCqmynfaLSLL 240

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 10092619   164 TQSCTTPHLHSILkatNYNGHTCLHLASIHGYLGIVELLV 203
Cdd:TIGR00870 241 DKLRDSKELEVIL---NHQGLTPLKLAAKEGRIVLFRLKL 277
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-141 5.28e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 36.88  E-value: 5.28e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 10092619   112 QTPLHLAVI-TNQPEIAEALLGAGCDPELRD 141
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 184-256 5.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 5.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10092619  184 HTCLHLASIHgyLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQ---NPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:PHA02859  56 FSCLEKDKVN--VEILKFLIENGADVNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHM 129
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-204 6.41e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 6.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  74 GDSFLHLAIIHEEKALTMEVIR--------QVKGdLAFLNFQNNL---QQTPLHLAVITNQPEIAEALLGAGCDPELRDF 142
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIArgadvvspRATG-TFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10092619 143 RGNTPLH---------LACE--QGCLASVGVLtqscttpHLHSILKATNYNGHTCLHLASIHGYLGIVELLVS 204
Cdd:cd22192 168 LGNTVLHilvlqpnktFACQmyDLILSYDKED-------DLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-211 6.45e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 6.45e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 10092619   182 NGHTCLHLASIHGYLGIVELLVSLGADVNA 211
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 144-249 8.40e-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: 41.02  E-value: 8.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 144 GNTPLHLAC---EQGCLASVGVLTQSC-TTPHLHSILKATN----YNGHTCLHLASIHGYLGIVELLVSLGADVNA---- 211
Cdd:cd21882  26 GKTCLHKAAlnlNDGVNEAIMLLLEAApDSGNPKELVNAPCtdefYQGQTALHIAIENRNLNLVRLLVENGADVSAratg 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 10092619 212 ----QEPCN----GRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQ 249
Cdd:cd21882 106 rffrKSPGNlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ 151
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 181-238 9.34e-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: 40.93  E-value: 9.34e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10092619 181 YNGHTCLHLASIHGYLGIVELLVSLGADVNA-----------QEPC--NGRTALHLAVDLQNPDLVSLLLK 238
Cdd:cd22193  74 YEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffqpkyQGEGfyFGELPLSLAACTNQPDIVQYLLE 144
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 182-244 9.95e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.56  E-value: 9.95e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10092619 182 NGHTCLHLA----------SIHGYLGIVELLVSLGADVNAQEPCN---GRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:cd22196  46 TGKTCLLKAmlnlhngqndTISLLLDIAEKTGNLKEFVNAAYTDSyykGQTALHIAIERRNMHLVELLVQNGADVH 121
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 74-203 1.58e-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: 40.25  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  74 GDSFLHLAIIHEEKALT-------MEVIRQVKGDlAFLNFQNNL---QQTPLHLAVITNQPEIAEALLGAGCDP---ELR 140
Cdd:cd21882  73 GQTALHIAIENRNLNLVrllvengADVSARATGR-FFRKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10092619 141 DFRGNTPLHLACEQG----------CLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLV 203
Cdd:cd21882 152 DSLGNTVLHALVLQAdntpensafvCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
207-256 1.59e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 10092619   207 ADVNAQEPCnGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:pfam13857   7 IDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-139 1.61e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.61e-03
                           10        20
                   ....*....|....*....|....*..
gi 10092619    113 TPLHLAVITNQPEIAEALLGAGCDPEL 139
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 168-257 2.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  168 TTPHLHSIlkatNYNGHTClhlasihgylgiVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVT 247
Cdd:PHA02884  71 TNPLIYAI----DCDNDDA------------AKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQT 134

                         90
                 ....*....|
gi 10092619  248 YQGYSPYQLT 257
Cdd:PHA02884 135 NDMVTPIELA 144
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 183-253 3.71e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.12  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  183 GHTCLHLASIHGYLG--IVELLVSLGADVNaqEPCN-GRTALHL------AVDLQNP--------DLVSLLLKCGADVNR 245
Cdd:PHA02716 317 GRTCLHQYILRHNIStdIIKLLHEYGNDLN--EPDNiGNTVLHTylsmlsVVNILDPetdndirlDVIQCLISLGADITA 394


                 ....*...
gi 10092619  246 VTYQGYSP 253
Cdd:PHA02716 395 VNCLGYTP 402
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 102-240 4.47e-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: 38.62  E-value: 4.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 102 AFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELrdFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHS---ILKA 178
Cdd:cd22193  36 ALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEY--YEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrFFQP 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 179 TN-----YNGHTCLHLASIHGYLGIVELLVS---LGADVNAQEPcNGRTALHLAVDL-----QNPDLVS-----LLLKCG 240
Cdd:cd22193 114 KYqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDS-RGNTVLHALVTVadntkENTKFVTrmydmILIRGA 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 188-256 4.52e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 4.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10092619  188 HLASIHGYLGIvELLVSLGADVNAQEpCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:PTZ00322  88 QLAASGDAVGA-RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-137 4.60e-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: 34.16  E-value: 4.60e-03
                          10        20
                  ....*....|....*....|....*.
gi 10092619   112 QTPLHLAVITNQPEIAEALLGAGCDP 137
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADI 28
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 113-153 4.87e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.16  E-value: 4.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 10092619  113 TPLHLAVITNQPEIAEALLG-AGCDPELRDFRGNTPLHLACE 153
Cdd:PHA02736  94 TPLHIAVYTQNYELATWLCNqPGVNMEILNYAFKTPYYVACE 135
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 195-245 4.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.04  E-value: 4.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10092619  195 YLGIVELLVSLGADVNAQEPCN---GRTALHLAVDLQNPDLVSLLLKCGADVNR 245
Cdd:PHA02884  45 YTDIIDAILKLGADPEAPFPLSensKTNPLIYAIDCDNDDAAKLLIRYGADVNR 98
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 74-149 5.32e-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: 38.24  E-value: 5.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  74 GDSFLHLAIIHEEKALT-------MEVIRQVKGDLaflnFQNNLQ-------QTPLHLAVITNQPEIAEALLG---AGCD 136
Cdd:cd22193  76 GQTALHIAIERRQGDIVallvengADVHAHAKGRF----FQPKYQgegfyfgELPLSLAACTNQPDIVQYLLEnehQPAD 151

                        90
                ....*....|...
gi 10092619 137 PELRDFRGNTPLH 149
Cdd:cd22193 152 IEAQDSRGNTVLH 164
PHA02798 PHA02798
ankyrin-like protein; Provisional
 181-291 7.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619  181 YNGHTCLHLASIHGY---LGIVELLVSLGADVNAQEPcNGRTALHLAVD---LQNPDLVSLLLKCGADVNRVTYQGYSPY 254
Cdd:PHA02798  71 YSTPLCTILSNIKDYkhmLDIVKILIENGADINKKNS-DGETPLYCLLSngyINNLEILLFMIENGADTTLLDKDGFTML 149

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 10092619  255 QLtWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDT 291
Cdd:PHA02798 150 QV-YLQSNHHIDIEIIKLLLEKGVDINTHNNKEKYDT 185
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 102-229 8.04e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 37.94  E-value: 8.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092619 102 AFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELrdFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNY 181
Cdd:cd21882  33 AALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEF--YQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFFRK 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10092619 182 NGHTC-------LHLASIHGYLGIVELLVSLGADVNAQEPCN--GRTALHLAVDLQN 229
Cdd:cd21882 111 SPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPAALEAQDslGNTVLHALVLQAD 167
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 183-244 9.84e-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: 37.47  E-value: 9.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10092619 183 GHTCLHLASIH---GYLGIVELLVSLGAD-------VNAQ---EPCNGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:cd22193  29 GKTCLMKALLNlnpGTNDTIRILLDIAEKtdnlkrfINAEytdEYYEGQTALHIAIERRQGDIVALLVENGADVH 103
 
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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