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Conserved domains on  [gi|187661960|sp|A6NI47|]
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RecName: Full=Putative POTE ankyrin domain family member M

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];
137-367 9.76e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 9.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 137 REDLDKLHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQC 216
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 217 QEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKA 296
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187661960 297 NLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYKEKQILK 367
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
137-367 9.76e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 9.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 137 REDLDKLHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQC 216
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 217 QEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKA 296
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187661960 297 NLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYKEKQILK 367
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-361 2.61e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 158 IVMLKDTDmNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTAL-----TKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA03100  21 IIMEDDLN-DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 233 NIPDEYGNTALHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR----- 303
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyll 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187661960 304 -----------YGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYK 361
Cdd:PHA03100 180 sygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.26e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 3.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  177 LHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGtDPNIPDeYGNTALHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 187661960  257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 171-340 4.23e-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: 65.42  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 171 KQKRTA---LHLASANGNSEVVK-LLLDRRCqlnilDNKKR-----TALTKAVQCQEDECALMLLEhgTDP---NIP--- 235
Cdd:cd22192   12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTALHVAALYDNLEAAVVLME--AAPelvNEPmts 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 236 DEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRYGRTVLILAVC 314
Cdd:cd22192   85 DLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAAC 145

                        170       180
                 ....*....|....*....|....*.
gi 187661960 315 CGSASIVSLLLEQNIDVSSQDLSGQT 340
Cdd:cd22192  146 VGNEEIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-362 5.10e-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: 58.94  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  154 RKDLIVMLKDTDMNKKDKQK------RTAL-HLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEdECALMLL 226
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpdrlgRSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVE-AILLHLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  227 EHgtdpniPDEYGNTALHYAIYNEDklmakallLYgadiesknkHGLTPLLLGVHEQKQQVVKFLIKKKANLNA------ 300
Cdd:TIGR00870 106 AA------FRKSGPLELANDQYTSE--------FT---------PGITALHLAAHRQNYEIVKLLLERGASVPAracgdf 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  301 --------LDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVssrhnVICQLLSDYKE 362
Cdd:TIGR00870 163 fvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 1.55e-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: 38.72  E-value: 1.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 187661960   238 YGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
137-367 9.76e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 9.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 137 REDLDKLHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQC 216
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 217 QEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKA 296
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187661960 297 NLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYKEKQILK 367
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
139-391 2.28e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 2.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 139 DLDKLHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQE 218
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 219 DECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANL 298
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 299 NALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYKEKQILKVSSENSNPEQD 378
Cdd:COG0666  180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                        250
                 ....*....|...
gi 187661960 379 LKLTSEEESQRLK 391
Cdd:COG0666  260 AAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-341 5.26e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 5.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 143 LHRAAWWGkvpRKDLIVMLKD--TDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDE 220
Cdd:COG0666   91 LHAAARNG---DLEIVKLLLEagADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 221 CALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNA 300
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 187661960 301 LDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTA 341
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-357 2.61e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 2.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 157 LIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPD 236
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 237 EYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCG 316
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 187661960 317 SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLL 357
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-309 4.48e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 143 LHRAAWWGKVprkDLIVML--KDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDE 220
Cdd:COG0666  124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 221 CALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNA 300
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*....
gi 187661960 301 LDRYGRTVL 309
Cdd:COG0666  281 ALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-357 5.73e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 5.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 187 EVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 267 SKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAV 346
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        170
                 ....*....|.
gi 187661960 347 SSRHNVICQLL 357
Cdd:COG0666  162 ANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-361 2.61e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 158 IVMLKDTDmNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTAL-----TKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA03100  21 IIMEDDLN-DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 233 NIPDEYGNTALHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR----- 303
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyll 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187661960 304 -----------YGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYK 361
Cdd:PHA03100 180 sygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.26e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 3.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  177 LHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGtDPNIPDeYGNTALHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 187661960  257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-304 4.60e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.34  E-value: 4.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 158 IVMLKDTDMNKKDKQKRTALHLASAN--GNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECAL------------ 223
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIlkllidkgvdin 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 224 ------MLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:PHA03100 171 aknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                 ....*..
gi 187661960 298 LNALDRY 304
Cdd:PHA03100 251 IKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 155-359 6.21e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 6.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 155 KDLIVMLKDT--DMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA02874 104 KDMIKTILDCgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 233 NIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKqQVVKFLIkKKANLNALDRYGRTVLILA 312
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHA 261

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 187661960 313 V---CcgSASIVSLLLEQNIDVSSQDLSGQTAREYAVS--SRHNVICQLLSD 359
Cdd:PHA02874 262 InppC--DIDIIDILLYHKADISIKDNKGENPIDTAFKyiNKDPVIKDIIAN 311
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-332 9.13e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 9.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 154 RKDLIVMLKDT--DMNKKDKQKRTALHLAS-----ANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALM-- 224
Cdd:PHA03100  47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 225 LLEHGTDPNIPDEYGNTALH-YAIYNEDKL-MAKALLL----------------YGADIESKNKHGLTPLLLGVHEQKQQ 286
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 187661960 287 VVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVS 332
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-335 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  243 LHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIkKKANLNALDrYGRTVLILAVCCGSASIVS 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 187661960  323 LLLEQNIDVSSQD 335
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 2.41e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  143 LHRAAWWGKVprkDLIVML--KDTDMNKKDKQKRTALHLASANGNSEVVKLLLDrRCQLNIlDNKKRTALTKAVQCQEDE 220
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 187661960  221 CALMLLEHGTDPNIPD 236
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 224-349 4.50e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.54  E-value: 4.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 224 MLLEHGTDPNIPDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLIKKKANLN 299
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187661960 300 ALDRYGRTvlILAVCCGSASI----VSLLLEQNIDVSSQDLSGQTAREYAVSSR 349
Cdd:PHA03095 112 AKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 151-361 5.11e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 5.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 151 KVPRKDLIVMLKDTDMNKKDKQKRTALHlasaNGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGT 230
Cdd:PHA02878  83 KLGMKEMIRSINKCSVFYTLVAIKDAFN----NRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 231 DPNIPDEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVL 309
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187661960 310 ILAVC-CGSASIVSLLLEQNIDVSSQD-LSGQTAREYAVSSRHNVicQLLSDYK 361
Cdd:PHA02878 239 HISVGyCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERKL--KLLLEYG 290
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 158-360 1.33e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.80  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 158 IVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILD-----------------------------NKKRT 208
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 209 ALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNE--DKLMAKaLLLYGADIESKNKHGLTPL-LLGVHEQKQ 285
Cdd:PHA02876 243 SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDT 321

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187661960 286 QVVKFLIKKKANLNALDRYGRTVLILAVCCG-SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDY 360
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-328 6.65e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 6.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 165 DMNKKDKQKRTALH--LASANGNSEVVKLLLDRRCQLNILDNKKRTAL-TKAVQCQEDECAL-MLLEHGTDPNIPDEYGN 240
Cdd:PHA03095 144 DVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDMLGN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 241 TALHY-AIYNEDK--LMAKaLLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGS 317
Cdd:PHA03095 224 TPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                        170
                 ....*....|.
gi 187661960 318 ASIVSLLLEQN 328
Cdd:PHA03095 303 GRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-354 1.07e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 153 PRKDLIVMLKD--TDMNKKDKQKRTALHLASANGNSE-VVKLLLDRRCQLNILDNKKRTALTK--AVQCQEDECALMLLE 227
Cdd:PHA03095  61 KVKDIVRLLLEagADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLR 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 228 HGTDPNIPDEYGNTALHYAIYNEDKLMA--KALLLYGADIESKNKHGLTplLLGVHEQ----KQQVVKFLIKKKANLNAL 301
Cdd:PHA03095 141 KGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRS--LLHHHLQsfkpRARIVRELIRAGCDPAAT 218

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 187661960 302 DRYGRTVLILAVCCGS--ASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVIC 354
Cdd:PHA03095 219 DMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC 273
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 184-359 8.59e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 8.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 184 GNSEVVKLLLDRRCQLNILdnkkrtaltkAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGA 263
Cdd:PHA02874  79 GAHDIIKLLIDNGVDTSIL----------PIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 264 DIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTARE 343
Cdd:PHA02874 149 DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228

                        170
                 ....*....|....*.
gi 187661960 344 YAVSSRHNVICQLLSD 359
Cdd:PHA02874 229 NAIIHNRSAIELLINN 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-354 4.55e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 4.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 165 DMNKKDKQKRTALH--LASANGNSEVVKLLLDRRCQLNILDNKKRT---ALTKAVQCqEDECALMLLEHGTDPNIPDEYG 239
Cdd:PHA03095 109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDDRF 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 240 NTALHY-AIY---NEDKLmaKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAV 313
Cdd:PHA03095 188 RSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 187661960 314 CCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVsSRHNVIC 354
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMV-RNNNGRA 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-346 9.86e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.99  E-value: 9.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 185 NSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGAD 264
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 265 IESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVcCGSASIVSLLLeQNIDVSSQDLSGQTAREY 344
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHH 260


                 ..
gi 187661960 345 AV 346
Cdd:PHA02874 261 AI 262
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 156-304 2.36e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.51  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 156 DLIVMLKDTDMNkkDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALML--LEHGTDPN 233
Cdd:PLN03192 543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPH 620

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187661960 234 IpdeyGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRY 304
Cdd:PLN03192 621 A----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 165-280 2.69e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 165 DMNKKDKQK-RTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTAL 243
Cdd:PHA02878 159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187661960 244 HYA-----------------------------------IYNEDKLmaKALLLYGADIESKNKHGLTPLLLGV 280
Cdd:PHA02878 239 HISvgyckdydilklllehgvdvnaksyilgltalhssIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 143-299 6.97e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 143 LHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECA 222
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187661960 223 LMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHG-LTPLLLGVHEQKQQVVKFLIKKKANLN 299
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-359 1.22e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 174 RTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKL 253
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 254 MAKALLLYGADIESK-NKHGLTPLLLGVHEQKQQVVKFLIKKKA--NLNALDRYgrTVLILAVCCGSASIVSLLLEQNID 330
Cdd:PHA02875  83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKAC 160

                        170       180
                 ....*....|....*....|....*....
gi 187661960 331 VSSQDLSGQTAREYAVSSRHNVICQLLSD 359
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 143-374 1.30e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 143 LHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANG-NSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQED-E 220
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 221 CALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQV-VKFLIKKKANLN 299
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 300 ALDRYGRTVLILAvCCGSA--SIVSLLLEQNIDVSSQDLSGQ----TAREYavssrHNVICQLL---SDYKEKQILKvSS 370
Cdd:PHA02876 437 SKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQypllIALEY-----HGIVNILLhygAELRDSRVLH-KS 509


                 ....
gi 187661960 371 ENSN 374
Cdd:PHA02876 510 LNDN 513
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 158-330 1.87e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 158 IVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLN-ILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPD 236
Cdd:PHA02875  53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 237 EYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGR-TVLILAVCC 315
Cdd:PHA02875 133 TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIEN 212

                        170
                 ....*....|....*
gi 187661960 316 GSASIVSLLLEQNID 330
Cdd:PHA02875 213 NKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 175-334 3.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 175 TALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPN-IPDEYGNTALHYAIYNEDKL 253
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 254 MAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQ--NIDV 331
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDY 196


                 ...
gi 187661960 332 SSQ 334
Cdd:PHA02875 197 FGK 199
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 171-340 4.23e-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: 65.42  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 171 KQKRTA---LHLASANGNSEVVK-LLLDRRCqlnilDNKKR-----TALTKAVQCQEDECALMLLEhgTDP---NIP--- 235
Cdd:cd22192   12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTALHVAALYDNLEAAVVLME--AAPelvNEPmts 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 236 DEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRYGRTVLILAVC 314
Cdd:cd22192   85 DLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAAC 145

                        170       180
                 ....*....|....*....|....*.
gi 187661960 315 CGSASIVSLLLEQNIDVSSQDLSGQT 340
Cdd:cd22192  146 VGNEEIVRLLIEHGADIRAQDSLGNT 171
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-360 7.47e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 7.47e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187661960  287 VVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEqNIDVSSQDlSGQTAREYAVSSRHNVICQLLSDY 360
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEK 83
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 217-340 3.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 217 QEDE--CALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02876 154 QQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187661960 295 KANL-----------------------------NALDRYGRTVLILAVCCGSAS-IVSLLLEQNIDVSSQDLSGQT 340
Cdd:PHA02876 234 RSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-362 5.10e-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: 58.94  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  154 RKDLIVMLKDTDMNKKDKQK------RTAL-HLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEdECALMLL 226
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpdrlgRSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVE-AILLHLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  227 EHgtdpniPDEYGNTALHYAIYNEDklmakallLYgadiesknkHGLTPLLLGVHEQKQQVVKFLIKKKANLNA------ 300
Cdd:TIGR00870 106 AA------FRKSGPLELANDQYTSE--------FT---------PGITALHLAAHRQNYEIVKLLLERGASVPAracgdf 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960  301 --------LDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVssrhnVICQLLSDYKE 362
Cdd:TIGR00870 163 fvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-276 1.42e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 1.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187661960  225 LLEHGT-DPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPL 276
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 3.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 3.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187661960  207 RTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALL 259
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 2.75e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 2.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 187661960  192 LLDRR-CQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 157-374 2.89e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.91  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 157 LIVMLKDTDMNKKDKQKRTALHLASANG---NSEVVKLLLDRRCQLNILDNKKRTALTKAVQ--CQED-ECALMLLEHGT 230
Cdd:PHA02798  93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 231 DPN-IPDEYGNTALH-YAIYN---------------------EDKLMAKALLLY---------------------GADIE 266
Cdd:PHA02798 173 DINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 267 SKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAV 346
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKLRKHIL 332

                        250       260
                 ....*....|....*....|....*...
gi 187661960 347 SSRHNVICQLLSDYKEKQILKVSSENSN 374
Cdd:PHA02798 333 NVEGDFINQLEFDIIKKFIAYVILYVKN 360
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 172-295 3.13e-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: 53.09  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 172 QKRTALHLASANGNSEVVKLLLDRR--------CQLNILDNKKRT------ALTKAVQCQEDECALMLLEHGTDPNIPDE 237
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGadvvspraTGTFFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDS 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187661960 238 YGNTALHYAIYNEDKLMAKAL--LLYGADIES--------KNKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd22192  168 LGNTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
165-213 4.40e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 4.40e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 187661960  165 DMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKA 213
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 172-295 6.15e-07

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: 52.19  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 172 QKRTALHLASANGNSEVVKLLLDRRCQLNILDNK---KRTA----------LTKAVQCQEDECALMLLEHGTDP---NIP 235
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffRKSPgnlfyfgelpLSLAACTNQEEIVRLLLENGAQPaalEAQ 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187661960 236 DEYGNTALHYAIYNEDKL---------MAKALLLYGADI-------ESKNKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd21882  152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-325 6.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 6.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187661960  272 GLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLL 325
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 180-357 1.13e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 180 ASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTAL-------HYAIYNedk 252
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFR--- 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 253 lmakaLLLYGADIEskNKHGLTPLLLgvheqkqqvvkfLIKKKANLNALDRygrtvlilavccgsasivslLLEQNIDVS 332
Cdd:PLN03192 609 -----ILYHFASIS--DPHAAGDLLC------------TAAKRNDLTAMKE--------------------LLKQGLNVD 649

                        170       180
                 ....*....|....*....|....*
gi 187661960 333 SQDLSGQTAREYAVSSRHNVICQLL 357
Cdd:PLN03192 650 SEDHQGATALQVAMAEDHVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-193 1.97e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187661960  143 LHRAAWWGKVprkDLIVMLKDT--DMNKKDKQKRTALHLASANGNSEVVKLLL 193
Cdd:pfam13637   5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 185-340 3.03e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 185 NSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLL--YG 262
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 263 ADI-ESKNKHGLTPlLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGS--ASIVSLLLEQNIDVSSQDLSGQ 339
Cdd:PHA02946 131 AKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGN 209


                 .
gi 187661960 340 T 340
Cdd:PHA02946 210 T 210
Ank_5 pfam13857
Ankyrin repeats (many copies);
296-345 5.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 5.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 187661960  296 ANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYA 345
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-292 9.22e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 9.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187661960  239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLI 292
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 207-309 1.08e-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: 47.95  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 207 RTALTKAV---QCQEDECALMLLEHGTDPNIP---------DEY--GNTALHYAIYNEDKLMAKALLLYGADIESK---- 268
Cdd:cd21882   27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARatgr 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187661960 269 --NKHGLT-------PLLLGVHEQKQQVVKFLIK---KKANLNALDRYGRTVL 309
Cdd:cd21882  107 ffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNTVL 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 222-293 1.31e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 1.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187661960 222 ALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-360 1.44e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 1.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 187661960  309 LILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDY 360
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 251-338 1.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 251 DKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNID 330
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                 ....*...
gi 187661960 331 VSSQDLSG 338
Cdd:PTZ00322 174 HFELGANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 1.88e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 1.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 187661960  238 YGNTALHYAIYNEDKL-MAKALLLYGADIESKNK 270
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-204 4.24e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 4.24e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 187661960  174 RTALHLASA-NGNSEVVKLLLDRRCQLNILDN 204
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 207-309 5.42e-05

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: 45.94  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 207 RTALTKAV---QCQEDECALMLLEHGTDPNIPDEY-----------GNTALHYAIYNEDKLMAKALLLYGADIESK---- 268
Cdd:cd22193   30 KTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAHakgr 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187661960 269 --NKH--------GLTPLLLGVHEQKQQVVKFLIK---KKANLNALDRYGRTVL 309
Cdd:cd22193  110 ffQPKyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVL 163
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 288-360 9.46e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 9.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187661960 288 VKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDY 360
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02798 PHA02798
ankyrin-like protein; Provisional
 178-332 9.68e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 9.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 178 HLASANGNSEVVKLLLDRRCQLNILDNKKRTALtkavqcqedeCALMllehgtdPNIPDeygntalhyaiYNEDKLMAKA 257
Cdd:PHA02798  43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPL----------CTIL-------SNIKD-----------YKHMLDIVKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 258 LLLYGADIESKNKHGLTPLLLGVHE---QKQQVVKFLIKKKANLNALDRYGRTVLILAV---CCGSASIVSLLLEQNIDV 331
Cdd:PHA02798  95 LIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDI 174


                 .
gi 187661960 332 S 332
Cdd:PHA02798 175 N 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 1.55e-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: 38.72  E-value: 1.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 187661960   238 YGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 1.73e-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: 38.72  E-value: 1.73e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 187661960   172 QKRTALHLASANGNSEVVKLLLDRRCQLNI 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-265 2.82e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.82e-04
                          10        20
                  ....*....|....*....|....*...
gi 187661960  238 YGNTALHYAIYNEDKLMAKALLLYGADI 265
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 280-350 3.92e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 3.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187661960 280 VHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRH 350
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-201 3.98e-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: 37.62  E-value: 3.98e-04
                          10        20
                  ....*....|....*....|....*...
gi 187661960  174 RTALHLASANGNSEVVKLLLDRRCQLNI 201
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 155-247 5.51e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 155 KDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKkrTALTKAVQCQEDECALMLLEHGTDPNI 234
Cdd:PHA02791  12 KQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQ 89

                         90
                 ....*....|...
gi 187661960 235 PDEYGNTALHYAI 247
Cdd:PHA02791  90 FDDKGNTALYYAV 102
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-228 6.42e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 6.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187661960 165 DMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEH 228
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 183-275 1.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 183 NGNSEVVKLLLDRRCQLNILDNKKRTALTKAVqcqeDECAL------MLLEHGTDPNIPDEYGNTALH-YAIYNEDKLMA 255
Cdd:PHA02859 100 NVEPEILKILIDSGSSITEEDEDGKNLLHMYM----CNFNVrinvikLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIF 175

                         90       100
                 ....*....|....*....|
gi 187661960 256 KALLLYGADIESKNKHGLTP 275
Cdd:PHA02859 176 DFLTSLGIDINETNKSGYNC 195
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 174-309 1.36e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 174 RTALHLASANGNSEVVKLLLD--RRCQLNILDNK------KRTALTKAVQCQED---ECALMLLEHGTDPNIP------- 235
Cdd:cd22197    7 RDRLFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAVLNLQDgvnACIMPLLEIDKDSGNPkplvnaq 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 236 --DEY--GNTALHYAIYNEDKLMAKALLLYGADIESK------NKH-------GLTPLLLGVHEQKQQVVKFLIKKK--- 295
Cdd:cd22197   87 ctDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARacgrffQKKqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqp 166

                        170
                 ....*....|....
gi 187661960 296 ANLNALDRYGRTVL 309
Cdd:cd22197  167 ASLQAQDSLGNTVL 180
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 260-340 1.53e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.28  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 260 LYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDR--------------YGRTVLILAVCCGSASIVSLLL 325
Cdd:cd22194  129 FINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLM 208

                         90
                 ....*....|....*.
gi 187661960 326 EQ-NIDVSSQDLSGQT 340
Cdd:cd22194  209 EKeSTDITSQDSRGNT 224
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 224-276 2.64e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 2.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187661960 224 MLLEHGTDPNIPDEYGNTALHY-------------AIYNEDKL-MAKALLLYGADIESKNKHGLTPL 276
Cdd:PHA02716 337 LLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildpETDNDIRLdVIQCLISLGADITAVNCLGYTPL 403
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 236-309 4.08e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.79  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 236 DEY--GNTALHYAIYNEDKLMAKALLLYGADIES--------KNK------HGLTPLLLGVHEQKQQVVKFLIK---KKA 296
Cdd:cd22196   89 DSYykGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPA 168

                         90
                 ....*....|...
gi 187661960 297 NLNALDRYGRTVL 309
Cdd:cd22196  169 DISARDSMGNTVL 181
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 170-337 8.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 170 DKQKRTALHLASANGNSEVVKLLLDRRCQLnILDNKKRTALTKAVQCqeDECALMLLEHGTDPN-IPDEYGNTALHYA-- 246
Cdd:PHA02876  72 DHKCHSTLHTICIIPNVMDIVISLTLDCDI-ILDIKYASIILNKHKL--DEACIHILKEAISGNdIHYDKINESIEYMkl 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187661960 247 ----IYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVS 322
Cdd:PHA02876 149 ikerIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                        170
                 ....*....|....*
gi 187661960 323 LLLEQNIDVSSQDLS 337
Cdd:PHA02876 229 AIIDNRSNINKNDLS 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-303 9.47e-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. 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: 33.80  E-value: 9.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 187661960  271 HGLTPLLLGV-HEQKQQVVKFLIKKKANLNALDR 303
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
 
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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