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Conserved domains on  [gi|6624055|gb|AAF19231|]
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similar to ankyrin motif [Homo sapiens]; note: this is probably the ankryin motif gene; however, there is an extra 'C' at position 252 of D78334.1 (NID:g1655417) which disrupts the reading frame. EST matches confirm the sequence presented here; similar to BAA11348.1 (PID:g1655418), partial [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];
1-130 3.73e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 3.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-130 3.73e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 3.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-128 8.56e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 8.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     36 LIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYeADLEAKNkDGYTPLLVAVINNNPKMVK 115
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 6624055    116 FLLEKGADVNASD 128
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-131 2.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.92  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCG-QSLS 79
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6624055    80 LVEKLLEYEADLEAKNK-DGYTPLLVAVinNNPKMVKFLLEKGADVNASDNYQ 131
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYK 300
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-120 9.70e-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: 49.24  E-value: 9.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKIN---------VRDSENK-----SPLIKAVQCQNEDCATILLNFGADPDLRDIRYN 66
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6624055   67 TVLHYAVCGQSLSLV----EKLLEYEADLEA------KNKDGYTPLLVAVINNNPKMVKFLLEK 120
Cdd:cd22192 171 TVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 25-126 1.23e-07

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: 48.92  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     25 INVRDSENKSPLIK-AVQCQNEDCATILLNFGADPDLRDirynTVLHYAvcgqSLSLVEKLLEYEADLEAKNKDGY---- 99
Cdd:TIGR00870  45 INCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGD----TLLHAI----SLEYVDAVEAILLHLLAAFRKSGplel 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 6624055    100 -------------TPLLVAVINNNPKMVKFLLEKGADVNA 126
Cdd:TIGR00870 117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 97-126 4.50e-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: 40.65  E-value: 4.50e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 6624055      97 DGYTPLLVAVINNNPKMVKFLLEKGADVNA 126
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-130 3.73e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 3.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-130 4.88e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 4.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666 122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-130 2.17e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 2.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666  56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-130 3.77e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 3.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-130 5.49e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 5.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666 103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND 152
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-128 8.56e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 8.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     36 LIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYeADLEAKNkDGYTPLLVAVINNNPKMVK 115
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 6624055    116 FLLEKGADVNASD 128
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-131 2.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.92  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCG-QSLS 79
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6624055    80 LVEKLLEYEADLEAKNK-DGYTPLLVAVinNNPKMVKFLLEKGADVNASDNYQ 131
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYK 300
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-131 5.59e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 5.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGA--DPDLRdiryNTVLHYAVCGQSL 78
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHAA----GDLLCTAAKRNDL 635

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6624055    79 SLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQ 131
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-126 1.99e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACA-NGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQS-L 78
Cdd:PHA02876 343 TPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpY 422

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 6624055    79 SLVEKLLEYEADLEAKNKDGYTPLLVAVINN-NPKMVKFLLEKGADVNA 126
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
PHA03095 PHA03095
ankyrin-like protein; Provisional
 13-130 2.79e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    13 DVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATI---LLNFGADPDLRDIRYNTVLHYAVC-GQSLSLVEKLLEYE 88
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAG 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6624055    89 ADLEAKNKDGYTPLLV--AVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLY 151
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-130 7.23e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 7.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACAN--GHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATI------------------LLNFGADPDL 60
Cdd:PHA03100 108 TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINI 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    61 RDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-130 6.62e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 6.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGH---TDVVLFLIEQQCKINVRDSENKSPLIKAVQCQN-EDCATILLNFGADPDLRDIRYNTVLHYAVCGQ 76
Cdd:PHA03095  49 TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGF 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6624055    77 SL--SLVEKLLEYEADLEAKNKDGYTPLLVAVINNN--PKMVKFLLEKGADVNASDNY 130
Cdd:PHA03095 129 NInpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-130 1.02e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGH-TDVVLFLIEQQCKINVRDSENKSPLIKAVQC-QNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSL 78
Cdd:PHA02876 309 TPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6624055    79 SLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKM-VKFLLEKGADVNASDNY 130
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKD 441
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-130 7.88e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 7.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQ-----------------------CQNEDCATILLNFGAD 57
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpipCIEKDMIKTILDCGID 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6624055    58 PDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-125 1.73e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKIN-VRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLS 79
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6624055    80 LVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVN 125
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-129 7.74e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLH--LACANGHTDVVLFLIEQQCKINVRDSENKSPL-IKAVQCQ-NEDCATILLNFGADPDLRDIRYNTVLHYAVCGQ 76
Cdd:PHA03095 154 TPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKpRARIVRELIRAGCDPAATDMLGNTPLHSMATGS 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6624055    77 SL--SLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDN 129
Cdd:PHA03095 234 SCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-129 4.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 4.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINvrdsENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLS- 79
Cdd:PHA02876 213 SVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSr 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6624055    80 LVEKLLEYEADLEAKNKDGYTPLLVAVINN-NPKMVKFLLEKGADVNASDN 129
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADR 339
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-62 8.84e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 8.84e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6624055      1 TPLHLACANGHTDVVLFLIEqQCKINVRDsENKSPLIKAVQCQNEDCATILLNFGADPDLRD 62
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-102 1.09e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                        90       100
                ....*....|....*....|..
gi 6624055   81 VEKLLEYEADLEAKNKDGYTPL 102
Cdd:COG0666 268 VKLLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 12-126 1.30e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    12 TDVVLFLIEQQCKINVRDSEN-KSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEAD 90
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 6624055    91 LEAKNKDGYTPLLVAVIN-NNPKMVKFLLEKGADVNA 126
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNA 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-129 3.38e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 3.38e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6624055     69 LHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKgADVNASDN 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN 60
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 48-118 6.57e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 6.57e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6624055    48 ATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 118
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-130 1.24e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    14 VVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQS-----LSLVEKLLEYE 88
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYG 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6624055    89 ADLEAKNKDGYTPLLVAVIN--NNPKMVKFLLEKGADVNASDNY 130
Cdd:PHA03100  97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-130 1.54e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   13 DVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLE 92
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6624055   93 AKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-130 2.36e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLH--LACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATI--LLNFGADPDLRDIRYNTVLHY--AVC 74
Cdd:PHA03095 119 TPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDDRFRSLLHHhlQSF 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6624055    75 GQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPK--MVKFLLEKGADVNASDNY 130
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-125 7.76e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 7.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6624055    81 VEKLLEYEADLEAKNKDG-YTPLLVAVINNNPKMVKFLLEKGADVN 125
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-118 3.05e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 3.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6624055     65 YNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLL 118
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-124 5.97e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    13 DVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLE 92
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110
                 ....*....|....*....|....*....|..
gi 6624055    93 AKNKDGYTPLLVAVINNNPKMVKFLLEKGADV 124
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-130 2.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDlrDIRY---NTVLHYAVCGQS 77
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYkdgMTPLHLATILKK 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6624055    78 LSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-128 3.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSL 80
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 6624055    81 VEKLLEYEADLEAKNKDGYTPLLVAVINNnpKMVKFLLEKGADVNASD 128
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQD 251
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-120 9.70e-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: 49.24  E-value: 9.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQCKIN---------VRDSENK-----SPLIKAVQCQNEDCATILLNFGADPDLRDIRYN 66
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6624055   67 TVLHYAVCGQSLSLV----EKLLEYEADLEA------KNKDGYTPLLVAVINNNPKMVKFLLEK 120
Cdd:cd22192 171 TVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 25-126 1.23e-07

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: 48.92  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     25 INVRDSENKSPLIK-AVQCQNEDCATILLNFGADPDLRDirynTVLHYAvcgqSLSLVEKLLEYEADLEAKNKDGY---- 99
Cdd:TIGR00870  45 INCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGD----TLLHAI----SLEYVDAVEAILLHLLAAFRKSGplel 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 6624055    100 -------------TPLLVAVINNNPKMVKFLLEKGADVNA 126
Cdd:TIGR00870 117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 6-128 2.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055     6 ACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLL 85
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6624055    86 E---YEADLeaKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASD 128
Cdd:PHA02875  89 DlgkFADDV--FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-130 4.50e-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: 47.31  E-value: 4.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    1 TPLHLACANGHTDVVLFLIEQQ-CKINVRDSENKSPLIKAVQCQNEDCATILLNfgADPDLRDIRYN-------TVLHYA 72
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTsdlyqgeTALHIA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6624055   73 VCGQSLSLVEKLLEYEADLEA---------KNKD-----GYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:cd22192  97 VVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 97-126 4.96e-07

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: 4.96e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 6624055     97 DGYTPLLVAVINNNPKMVKFLLEKGADVNA 126
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
1-52 6.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6624055      1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILL 52
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
50-105 7.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 7.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6624055     50 ILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVA 105
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 32-124 8.92e-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: 46.54  E-value: 8.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   32 NKSPLIKAVQcQNeDCATI---LLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADL--EAKNKD---GYTPLL 103
Cdd:cd22192  17 SESPLLLAAK-EN-DVQAIkklLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALH 94

                        90       100
                ....*....|....*....|.
gi 6624055  104 VAVINNNPKMVKFLLEKGADV 124
Cdd:cd22192  95 IAVVNQNLNLVRELIARGADV 115
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-131 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    51 LLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPL-----LVAVINNNPKMVKFLLEKGADVN 125
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVN 100


                 ....*.
gi 6624055   126 ASDNYQ 131
Cdd:PHA03100 101 APDNNG 106
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 50-130 1.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    50 ILLNFGADPDLRDIRY-NTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASD 128
Cdd:PHA02878 152 LLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231


                 ..
gi 6624055   129 NY 130
Cdd:PHA02878 232 KC 233
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 97-129 1.57e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.57e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 6624055     97 DGYTPLLVAVI-NNNPKMVKFLLEKGADVNASDN 129
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 97-126 4.50e-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: 40.65  E-value: 4.50e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 6624055      97 DGYTPLLVAVINNNPKMVKFLLEKGADVNA 126
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-39 5.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 5.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 6624055      1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKA 39
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-52 6.85e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 6.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6624055     1 TPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILL 52
Cdd:PTZ00322 117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-128 7.42e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    48 ATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNAS 127
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240


                 .
gi 6624055   128 D 128
Cdd:PHA02876 241 D 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
84-130 3.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 3.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 6624055     84 LLEYE-ADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
PHA02798 PHA02798
ankyrin-like protein; Provisional
 12-129 4.65e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    12 TDVVLFLIEQQCKINVRDSENKSPLikavqcqnedcATILLNFgadpdlrdIRYNTvlhyavcgqSLSLVEKLLEYEADL 91
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL-----------CTILSNI--------KDYKH---------MLDIVKILIENGADI 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6624055    92 EAKNKDGYTPLLVAVIN---NNPKMVKFLLEKGADVNASDN 129
Cdd:PHA02798 103 NKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDK 143
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 16-126 5.11e-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: 41.40  E-value: 5.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   16 LFLIEQQCKINVRDSENKSP------LIKAV---QCQNEDCATILLNfgADPDLRDIRY-------------NTVLHYAV 73
Cdd:cd21882   4 LLGLLECLRWYLTDSAYQRGatgktcLHKAAlnlNDGVNEAIMLLLE--AAPDSGNPKElvnapctdefyqgQTALHIAI 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6624055   74 CGQSLSLVEKLLEYEADLEAK------NKDGYT-------PLLVAVINNNPKMVKFLLEKGADVNA 126
Cdd:cd21882  82 ENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAA 147
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1-27 6.54e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 6.54e-05
                          10        20
                  ....*....|....*....|....*..
gi 6624055      1 TPLHLACANGHTDVVLFLIEQQCKINV 27
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
34-85 7.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 7.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6624055     34 SPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLL 85
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 30-128 9.11e-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: 40.55  E-value: 9.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   30 SENKSPLIKAV---QCQNEDCATILLNFGADPD---------LRDIRY--NTVLHYAVCGQSLSLVEKLLEYEADLEAKN 95
Cdd:cd22193  27 STGKTCLMKALlnlNPGTNDTIRILLDIAEKTDnlkrfinaeYTDEYYegQTALHIAIERRQGDIVALLVENGADVHAHA 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6624055   96 KD--------------GYTPLLVAVINNNPKMVKFLLE---KGADVNASD 128
Cdd:cd22193 107 KGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQD 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1-29 2.93e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.93e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 6624055      1 TPLHLACA-NGHTDVVLFLIEQQCKINVRD 29
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 64-129 3.00e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.02  E-value: 3.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   64 RYNTVLHYAVCGQSLSLVEKLLEYEADLEA----------KNKDGY----TPLLVAVINNNPKMVKFLLE---KGADVNA 126
Cdd:cd22196  93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISA 172


                ...
gi 6624055  127 SDN 129
Cdd:cd22196 173 RDS 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
25-72 3.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 6624055     25 INVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYA 72
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 33-127 3.33e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.97  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   33 KSPLIKAVQCQNE---DCATILLNFGADPDLRDIRYN-----------TVLHYAVCGQSLSLVEKLLEYEADLEAKNK-- 96
Cdd:cd22194  95 KTCLMKALLNINEntkEIVRILLAFAEENGILDRFINaeyteeayegqTALNIAIERRQGDIVKLLIAKGADVNAHAKgv 174

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6624055   97 --------DGY----TPLLVAVINNNPKMVKFLLEKGADVNAS 127
Cdd:cd22194 175 ffnpkykhEGFyfgeTPLALAACTNQPEIVQLLMEKESTDITS 217
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-128 4.14e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 4.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6624055    70 HYAVCGQSLSlVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASD 128
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
98-130 6.37e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 6.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 6624055     98 GYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1-27 7.20e-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: 34.87  E-value: 7.20e-04
                           10        20
                   ....*....|....*....|....*..
gi 6624055       1 TPLHLACANGHTDVVLFLIEQQCKINV 27
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-125 7.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 7.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6624055    61 RDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVN 125
Cdd:PHA02876 141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-125 8.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 8.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    34 SPLIKAVQCQNEDCATILLNFGADpdlrdirYNTVLHYAVCgqslslveklleyeadleaknkdgyTPLLVAVINNNPKM 113
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGAD-------VNRYAEEAKI-------------------------TPLYISVLHGCLKC 119

                         90
                 ....*....|..
gi 6624055   114 VKFLLEKGADVN 125
Cdd:PHA02884 120 LEILLSYGADIN 131
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 28-123 9.96e-04

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: 37.53  E-value: 9.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   28 RDSENKSPLIKAvQCQNEDcatillnfgadpdlrdIRYNTVLHYAVCGQSLSLVEKLLEYEADLEA--------KNKD-- 97
Cdd:cd22197  74 KDSGNPKPLVNA-QCTDEY----------------YRGHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqKKQGtc 136

                        90       100
                ....*....|....*....|....*....
gi 6624055   98 ---GYTPLLVAVINNNPKMVKFLLEKGAD 123
Cdd:cd22197 137 fyfGELPLSLAACTKQWDVVNYLLENPHQ 165
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-130 1.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 36.95  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6624055    77 SLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNY 130
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKN 67
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 60-129 2.59e-03

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


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 36.37  E-value: 2.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055   60 LRDIRY--NTVLHYAVCGQSLSLVEKLLEYEADLEA---------KNKDGY-----TPLLVAVINNNPKMVKFLLE---K 120
Cdd:cd22195 130 FRDVYYrgQTALHIAIERRCKHYVELLVEKGADVHAqargrffqpKDEGGYfyfgeLPLSLAACTNQPDIVHYLTEnahK 209


                ....*....
gi 6624055  121 GADVNASDN 129
Cdd:cd22195 210 KADLRRQDS 218
PHA02741 PHA02741
hypothetical protein; Provisional
 50-129 3.82e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 35.40  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    50 ILLNFGADPDLRD-IRYNTVLHYAVCGQSLSLVEKLL-EYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNAS 127
Cdd:PHA02741  82 HLIELGADINAQEmLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSRGF 161


                 ..
gi 6624055   128 DN 129
Cdd:PHA02741 162 SN 163
PHA02798 PHA02798
ankyrin-like protein; Provisional
 13-129 5.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 35.58  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    13 DVVLFLIEQQCKINVRDSENKSPLIkavqcqnedcatILLNFGADPDLRDIRYntvlhyavcgqslslvekLLEYEADLE 92
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLY------------CLLSNGYINNLEILLF------------------MIENGADTT 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6624055    93 AKNKDGYTPLLVAVINNNP---KMVKFLLEKGADVNASDN 129
Cdd:PHA02798 140 LLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNN 179
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 80-129 5.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 35.49  E-value: 5.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6624055    80 LVEKLLEYEADLEAKNKDGYTPLLVAVIN---NNPKMVKFLLEKGADVNASDN 129
Cdd:PHA02989  90 IVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINVNDVKN 142
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-128 6.10e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 35.61  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6624055    34 SPLIKAVQCQNEDCATILLNF-------------------GADPDLRDIRYNtVLHYAVCGQSlSLVEKLLEYEADLEAK 94
Cdd:PLN03192 477 STLIEAMQTRQEDNVVILKNFlqhhkelhdlnvgdllgdnGGEHDDPNMASN-LLTVASTGNA-ALLEELLKAKLDPDIG 554

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6624055    95 NKDGYTPLLVAVINNNPKMVKFLLEKGADVNASD 128
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD 588
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 50-122 7.37e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 34.47  E-value: 7.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6624055    50 ILLNFGADPDLRD-IRYNTVLHYAVCGQSLSLVEKLLEY-EADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGA 122
Cdd:PHA02736  76 LLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
 
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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