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Conserved domains on  [gi|1370507637|ref|XP_024302126|]
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ankyrin repeat domain-containing protein 6 isoform X11 [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];
14-229 1.43e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507637 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-229 1.43e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507637 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-232 1.16e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 107.80  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  19 YKGQTENVVQ-LINKGARV-AVTKHGRTPLHL-AANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  89 EIIAALIHEGCALDRQDKDGNTALHEaswhgFSQSAK-------LLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV-- 159
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlp 242

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507637 160 LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 232
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 1.33e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507637 126 LLIKAGANVLAKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-183 2.19e-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: 57.33  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  11 SERLLVAAYKgqtENVVQLINKGARVAVTK------HGRTPLHLAANKGHLPVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192    17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  80 HRATVVGNTEIIAALIHEG-----------CALDRQDKD---GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTAL 145
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507637 146 H-LACQNSHSQSTRV--LLLAGSRAD-------LKNNAGDTALHVAAA 183
Cdd:cd22192   174 HiLVLQPNKTFACQMydLILSYDKEDdlqpldlVPNNQGLTPFKLAAK 221
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 4.04e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 4.04e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370507637   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-195 6.93e-06

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: 49.31  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 107 DGNTALHeaswhgfsqsakllikaGANVLAKNKAGNTALHLACQNShsqstRVLLLAGSR-----ADLKNNAGDTALHVA 181
Cdd:TIGR00870 207 LGNTLLH-----------------LLVMENEFKAEYEELSCQMYNF-----ALSLLDKLRdskelEVILNHQGLTPLKLA 264

                         170
                  ....*....|....
gi 1370507637 182 AALNHKKVAKILLE 195
Cdd:TIGR00870 265 AKEGRIVLFRLKLA 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-229 1.43e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507637 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-211 1.25e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNN 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370507637 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 211
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-229 1.52e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637   1 MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  81 RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVL 160
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507637 161 LLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-229 1.82e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  24 ENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 104 QDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAA 183
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370507637 184 LNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-226 1.11e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  55 LPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 135 LAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 214
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170
                  ....*....|..
gi 1370507637 215 RYHNNPEVALLL 226
Cdd:COG0666   161 AANGNLEIVKLL 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-232 1.16e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 107.80  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  19 YKGQTENVVQ-LINKGARV-AVTKHGRTPLHL-AANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  89 EIIAALIHEGCALDRQDKDGNTALHEaswhgFSQSAK-------LLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV-- 159
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlp 242

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507637 160 LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 232
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSA 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-229 7.10e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.49  E-value: 7.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  24 ENVVQLINKGARVAVTK-HGRTPLHLAANKGHLP---VVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-IIAALIHEG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  99 CALDRQDKDGNTALH------------------------------EASWHGFSQSA-------KLLIKAGANVLAKNKAG 141
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvylsgfninpkvirlllrkgadvnaldlygMTPLAVLLKSRnanvellRLLIDAGADVYAVDDRF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 142 NTALHLACQNSHSQST--RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKI--LLEAGADTTIVNNAGQTPLETARYH 217
Cdd:PHA03095  188 RSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVF 267

                         250
                  ....*....|..
gi 1370507637 218 NNPEVALLLTKA 229
Cdd:PHA03095  268 NNPRACRRLIAL 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 1.33e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507637 126 LLIKAGANVLAKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 2.05e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 112 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTALHVAAALNHKKVAK 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507637 192 ILLEAGADTTIVN 204
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-232 5.09e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.19  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  26 VVQLINKGARVAV-TKHGRTPLHLAANKGH-----LPVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEIIAALIHE 97
Cdd:PHA03100   51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  98 GCALDRQDKDGNTALHEA--SWHGFSQSAKLLIKAGANVLAKNkagntalhlacqnshsqstRV--LLLAGSRADLKNNA 173
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKN-------------------RVnyLLSYGVPINIKDVY 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 174 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 232
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 2.85e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEIIA 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507637  93 ALIHEGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-214 7.72e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.78  E-value: 7.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  57 VVQILLKAGCDLDVQD-DGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVL 135
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 136 AKNKAGNTALHLACQNSHSQST-RVLLLAGSRADLKNNA-GDTALHVAaaLNHKKVAKILLEAGADTTIVNNAGQTPLET 213
Cdd:PHA02878  229 ARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSS 306


                  .
gi 1370507637 214 A 214
Cdd:PHA02878  307 A 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-229 2.14e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.32  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  10 LSERLLVAAYKGQTENVVQLI-NKGARVAVT-KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874    1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  88 TEIIAALIHEG---------------------CALD--RQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTA 144
Cdd:PHA02874   81 HDIIKLLIDNGvdtsilpipciekdmiktildCGIDvnIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 145 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVAL 224
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIEL 240


                  ....*
gi 1370507637 225 LLTKA 229
Cdd:PHA02874  241 LINNA 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-229 2.30e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.00  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  89 EIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRAD 168
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507637 169 LKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-171 4.89e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 4.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQdkDGNTALHEASWHGFS 121
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507637 122 QSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKN 171
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-218 6.13e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 6.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  26 VVQLINKGARV-AVTKHGRTPLHLAANKGH-LPVVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEIIAALIHEGCALD 102
Cdd:PHA02876  290 VPKLLERGADVnAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 103 RQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLA-CQNSHSQSTRVLLLAGSRADLKNNAGDTALHVA 181
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370507637 182 AALNHK-KVAKILLEAGADTTIVNNAGQTPLETA-RYHN 218
Cdd:PHA02876  450 CKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAlEYHG 488
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-226 9.72e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 9.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 145 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1370507637 225 LL 226
Cdd:pfam12796  79 LL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-199 1.51e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  15 LVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAAN-KGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  93 ALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLIKAGANVLAKNKAGNTALHLACQ-NSHSQSTRVLLLAGSRADL 169
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVNA 471

                         170       180       190
                  ....*....|....*....|....*....|
gi 1370507637 170 KNNAGDTALHVaaALNHKKVAKILLEAGAD 199
Cdd:PHA02876  472 INIQNQYPLLI--ALEYHGIVNILLHYGAE 499
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-219 1.89e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  29 LINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHE---------- 97
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsninkndls 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  98 -------------------GCALDRQDKDGNTALHEASWH-GFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSH-SQS 156
Cdd:PHA02876  244 llkairnedletslllydaGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507637 157 TRVLLLAGSRADLKNNAGDTALHVAAALN-HKKVAKILLEAGADTTIVNNAGQTPLETARYHNN 219
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-268 3.44e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLA 136
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 137 KNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNnaGQTPLETA-R 215
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHAiN 263

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507637 216 YHNNPEV--ALLLTKAPQVLRFSRGRSLRK------KRERLKEERRAQSVPRDEVAQSKGS 268
Cdd:PHA02874  264 PPCDIDIidILLYHKADISIKDNKGENPIDtafkyiNKDPVIKDIIANAVLIKEADKLKDS 324
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 49-204 1.35e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  49 AANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 128
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507637 129 KAGAnvLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVN 204
Cdd:PLN03192  612 HFAS--ISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 43-250 3.80e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 3.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  43 RTPLHLAANKGHLPVVQILLKAGCDLD--VQDDGDqTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 121 SQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAGAD 199
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507637 200 TTI---VNNAGQTPLETAR-YHNNPEV-ALLLTKAPQVLR-----------FSRGRSLRKKRERLKE 250
Cdd:PHA02875  228 CNImfmIEGEECTILDMICnMCTNLESeAIDALIADIAIRihkktirrdegFKNNMSTIEDKEEFKD 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-228 1.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 121 SQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADT 200
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                         170       180
                  ....*....|....*....|....*....
gi 1370507637 201 TIVNNAGQ-TPLETARYHNNPEVALLLTK 228
Cdd:PHA02875  195 DYFGKNGCvAALCYAIENNKIDIVRLFIK 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-214 2.85e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  13 RLLVAAYKGQTENVVQLINkgaRVAVTKHGRT--------PLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878    3 KLYKSMYTDNYETILKYIE---YIDHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  85 VGNTEIIAALIHE--GCALDRQDKDGNTALHEASWHGF-----------------------------SQSAKLLIKAGAN 133
Cdd:PHA02878   80 EPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNRNVEIFkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 134 VLAKNK-AGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLE 212
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239


                  ..
gi 1370507637 213 TA 214
Cdd:PHA02878  240 IS 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 6.38e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 6.38e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507637  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-213 1.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  14 LLVAAYKGQTENVVQLINKGARVAVTK-HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNkaGNTALHLACQNSHSQS-TRVLLLAGSRADLKN 171
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHAINPPCDIDiIDILLYHKADISIKD 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370507637 172 NAGDTALHVAAA-LNHKKVAKILLeagADTTIVNNAGQTPLET 213
Cdd:PHA02874  286 NKGENPIDTAFKyINKDPVIKDII---ANAVLIKEADKLKDSD 325
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-169 1.81e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  17 AAYKGQTENVVQLI--NKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507637  95 IHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGN-TALHLACQNSHSQSTRVLLLAGSRADL 169
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 149-231 3.92e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 149 CQNSHSQST---RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALL 225
Cdd:PTZ00322   87 CQLAASGDAvgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....*.
gi 1370507637 226 LTKAPQ 231
Cdd:PTZ00322  167 LSRHSQ 172
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 4.64e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 4.64e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370507637  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 5.80e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507637  77 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 128
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-183 2.19e-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: 57.33  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  11 SERLLVAAYKgqtENVVQLINKGARVAVTK------HGRTPLHLAANKGHLPVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192    17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  80 HRATVVGNTEIIAALIHEG-----------CALDRQDKD---GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTAL 145
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507637 146 H-LACQNSHSQSTRV--LLLAGSRAD-------LKNNAGDTALHVAAA 183
Cdd:cd22192   174 HiLVLQPNKTFACQMydLILSYDKEDdlqpldlVPNNQGLTPFKLAAK 221
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 7.49e-08

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: 48.82  E-value: 7.49e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370507637  41 HGRTPLHLAANK-GHLPVVQILLKAGCDLDVQDD 73
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-237 7.59e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 7.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  53 GHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGA 132
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 133 ---NVLAKNkaGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQT 209
Cdd:PHA02875   93 fadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                         170       180
                  ....*....|....*....|....*....
gi 1370507637 210 PLETARYHNNPEVA-LLLTKAPQVLRFSR 237
Cdd:PHA02875  171 PLIIAMAKGDIAICkMLLDSGANIDYFGK 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 1.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507637 174 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 226
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 5.47e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507637 108 GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-211 5.89e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  44 TPLHLAANKGHLPVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDK-----DGNTALHEASW 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 118 HGFSQSAKLLIKAGANVlAKNKAGNTALHLacqnshsqstrvlllagsRADLKNNAGDTALHVAAALNHKKVAKILLEAG 197
Cdd:cd22192    99 NQNLNLVRELIARGADV-VSPRATGTFFRP------------------GPKNLIYYGEHPLSFAACVGNEEIVRLLIEHG 159

                         170
                  ....*....|....
gi 1370507637 198 ADTTIVNNAGQTPL 211
Cdd:cd22192   160 ADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 6.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507637 127 LIKAG-ANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-148 9.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 9.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507637  96 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLA 148
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-194 1.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507637 141 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILL 194
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-240 2.07e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507637 178 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRS 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 79-226 4.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  79 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaganVLAKNKAGNT--ALHLACQNSH--- 153
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNvei 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 154 ------------------------------SQSTRVLLLAGSRADLKN-NAGDTALHVAAALNHKKVAKILLEAGADTTI 202
Cdd:PHA02878  117 fkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                         170       180
                  ....*....|....*....|....*
gi 1370507637 203 VNNAGQTPLETA-RYHNNPEVALLL 226
Cdd:PHA02878  197 PDKTNNSPLHHAvKHYNKPIVHILL 221
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 4.04e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 4.04e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370507637   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-70 6.55e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.01  E-value: 6.55e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370507637  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-195 6.93e-06

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: 49.31  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 107 DGNTALHeaswhgfsqsakllikaGANVLAKNKAGNTALHLACQNShsqstRVLLLAGSR-----ADLKNNAGDTALHVA 181
Cdd:TIGR00870 207 LGNTLLH-----------------LLVMENEFKAEYEELSCQMYNF-----ALSLLDKLRdskelEVILNHQGLTPLKLA 264

                         170
                  ....*....|....
gi 1370507637 182 AALNHKKVAKILLE 195
Cdd:TIGR00870 265 AKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
160-214 7.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 7.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507637 160 LLLAGSRA-DLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 214
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 76-205 1.34e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  76 QTALHRATVvgNTEIIAALIHEGCALDRQDKDGNTAL-----HEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQ 150
Cdd:PHA02798   41 QKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLS 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507637 151 NSHSQSTRVLLLA---GSRADLKNNAGDTALHVAAALNHK---KVAKILLEAGADTTIVNN 205
Cdd:PHA02798  119 NGYINNLEILLFMienGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNN 179
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-194 1.36e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  71 QDDGDQTALHRATVvgnteiiaalihEGCALdrqdkdgntalhEASwhGFSQSAKLLIKAGANVLAKNKAGNTALHLACQ 150
Cdd:PTZ00322   71 EEVIDPVVAHMLTV------------ELCQL------------AAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACA 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370507637 151 NSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILL 194
Cdd:PTZ00322  125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-205 1.98e-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: 41.89  E-value: 1.98e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370507637 174 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 205
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-111 2.26e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  10 LSERLLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                          90       100
                  ....*....|....*....|...
gi 1370507637  89 EIIAALIheGCALDRQDKDGNTA 111
Cdd:PTZ00322  162 EVVQLLS--RHSQCHFELGANAK 182
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 3.60e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 3.60e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370507637 107 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-147 3.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.20  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  29 LINKGARV-AVTKH-GRTPLH--LAANKGHLP-VVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEIIAALIHEGCAL 101
Cdd:PHA02859   72 LIENGADVnFKTRDnNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507637 102 DRQDKDGNTALHE-ASWHGFSQSAKLLIKAGANVLAKNKAGNTALHL 147
Cdd:PHA02859  152 LNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-129 1.50e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  47 HLAANkGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKL 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 1370507637 127 LIK 129
Cdd:PTZ00322  167 LSR 169
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-141 1.71e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 44.26  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100
                  ....*....|....*....|.
gi 1370507637 121 SQSAKLLIKAGANVLAKNKAG 141
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTG 127
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.95e-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: 39.11  E-value: 1.95e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370507637  174 GDTALHVAAALNHKKVAKILLEAGADTTI 202
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 131-232 3.02e-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: 43.85  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 131 GANVLAKNKAGNTALHLACQNSHSQSTRVLLLAgSRADL--KNNAGDTALHVAAALNHKKVAKILLEagADTTIVNNA-- 206
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmt 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370507637 207 -----GQTPLETARYHNNPE-VALLLTKAPQV 232
Cdd:cd22192    84 sdlyqGETALHIAVVNQNLNlVRELIARGADV 115
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 87-218 1.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  87 NTEIIAALIHEGCALDRQDKDGN-TALHeaSWHGFSQSA-----KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVL 160
Cdd:PHA02859   65 NVEILKFLIENGADVNFKTRDNNlSALH--HYLSFNKNVepeilKILIDSGSSITEEDEDGKNLLHMYMCNFNVRINVIK 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507637 161 LL--AGSRADLKNNAGDTALHVAAAL-NHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 218
Cdd:PHA02859  143 LLidSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02946 PHA02946
ankyin-like protein; Provisional
 46-225 1.99e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  46 LHLAANKGHLPVVQILLKAgcdldVQDDGDQTALHRATVVG--NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS 123
Cdd:PHA02946   13 LYAKYNSKNLDVFRNMLQA-----IEPSGNYHILHAYCGIKglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 124 AKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALH--VAAALNHKKVAKILLEAGADTT 201
Cdd:PHA02946   88 VAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGAKINNSVDEEGCGplLACTDPSERVFKKIMSIGFEAR 167

                         170       180
                  ....*....|....*....|....
gi 1370507637 202 IVNNAGQTPLETARYHNNPEVALL 225
Cdd:PHA02946  168 IVDKFGKNHIHRHLMSDNPKASTI 191
PHA02791 PHA02791
ankyrin-like protein; Provisional
 141-235 3.17e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 141 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNagDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNP 220
Cdd:PHA02791   30 GHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107

                          90
                  ....*....|....*
gi 1370507637 221 EVALLLTKAPQVLRF 235
Cdd:PHA02791  108 QTVKLFVKKNWRLMF 122
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 101-198 3.87e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637 101 LDRQDKDGNTALHEASWHGFSQSA---KLLIKAGANVLAKN-KAGNTALHLACqnshsqSTRVLLLA-------GSRADL 169
Cdd:PHA02743   50 LHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARElGTGNTLLHIAA------STKNYELAewlcrqlGVNLGA 123

                          90       100
                  ....*....|....*....|....*....
gi 1370507637 170 KNNAGDTALHVAAALNHKKVAKILLEAGA 198
Cdd:PHA02743  124 INYQHETAYHIAYKMRDRRMMEILRANGA 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-134 3.90e-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: 3.90e-03
                           10        20
                   ....*....|....*....|....*...
gi 1370507637  107 DGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-199 5.30e-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: 34.93  E-value: 5.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370507637 174 GDTALHVAAALNHKKVAKILLEAGAD 199
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-150 5.93e-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: 39.74  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIaALIHEGCALD--RQD 105
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIV-QLLMEKESTDitSQD 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507637 106 KDGNTALH---EASWHGFSQSA-------KLLIKAGANVLAK--NKAGNTALHLACQ 150
Cdd:cd22194   220 SRGNTVLHalvTVAEDSKTQNDfvkrmydMILLKSENKNLETirNNEGLTPLQLAAK 276
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 42-113 7.88e-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: 39.45  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507637  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------------QTALHRATVVGNTEIIAALI---HEGCALDRQD 105
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLenpHQPASLQAQD 173


                  ....*...
gi 1370507637 106 KDGNTALH 113
Cdd:cd22197   174 SLGNTVLH 181
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 170-230 9.50e-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: 39.36  E-value: 9.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507637 170 KNNAGDTALHVAAALNHKKVAKILLEAGADTTI---------VNNA-----GQTPLETARYHNNPE-VALLLTKAP 230
Cdd:cd22194   137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKES 212
 
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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