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Conserved domains on  [gi|26351335|dbj|BAC39304|]
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unnamed protein product [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-219 2.13e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 2.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  51 IHKAASVGDVAKVQHILILGKSgVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVD 210
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                ....*....
gi 26351335 211 QLGSNRQMF 219
Cdd:COG0666 250 KDGLTALLL 258
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-219 2.13e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 2.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  51 IHKAASVGDVAKVQHILILGKSgVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVD 210
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                ....*....
gi 26351335 211 QLGSNRQMF 219
Cdd:COG0666 250 KDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-177 7.84e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 7.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335    85 LHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHgADPNvMDSSGNTALHYAVYSENTSMAA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 26351335   165 KLLAHNANIEAKN 177
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 51-204 1.99e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.65  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   51 IHKAASVGDVAKVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26351335  131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKD-DLTPMLLAVKENKQHIVEFLVKKKA 204
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGA 226
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-207 1.25e-09

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: 59.26  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  83 TALHLACAYGHPEVVTLLVERKCE-IDARD-----SESSTALIK--------AVQCQEEECAAILLDHGADPNVMDSSGN 148
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADvVSPRAtgtffRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26351335 149 TALHYAVYSENTSMAAK----LLAHNANIEA------KNKDDLTPMLLAVKENKQHIVEFLVKKKASIH 207
Cdd:cd22192 171 TVLHILVLQPNKTFACQmydlILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQ 239
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-203 2.38e-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: 52.39  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335    74 VNDRDK----KDRTALHLACAYGHPEVVTLLVERKCEIDAR----------------DSESSTALIKAVQcqEEECAAIL 133
Cdd:TIGR00870 117 ANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvdsfyHGESPLNAAACLG--SPSIVALL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   134 LDHGADPNVMDSSGNTALHYAV-----YSENTSM-------AAKLLAHNANIEA----KNKDDLTPMLLAVKENK----Q 193
Cdd:TIGR00870 195 SEDPADILTADSLGNTLLHLLVmenefKAEYEELscqmynfALSLLDKLRDSKEleviLNHQGLTPLKLAAKEGRivlfR 274

                         170
                  ....*....|
gi 26351335   194 HIVEFLVKKK 203
Cdd:TIGR00870 275 LKLAIKYKQK 284
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-109 1.64e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.64e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 26351335     80 KDRTALHLACAYGHPEVVTLLVERKCEIDA 109
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-219 2.13e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 2.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  51 IHKAASVGDVAKVQHILILGKSgVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVD 210
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                ....*....
gi 26351335 211 QLGSNRQMF 219
Cdd:COG0666 250 KDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-213 7.33e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 7.33e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  42 HIHDKDMGKIHKAASVGDVAKVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKA 121
Cdd:COG0666  48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 122 VQCQEEECAAILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVK 201
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                       170
                ....*....|..
gi 26351335 202 KKASIHAVDQLG 213
Cdd:COG0666 208 AGADVNAKDNDG 219
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-215 4.08e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 4.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  51 IHKAASVGDVAKVQHILILGKSgVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVD 210
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                ....*
gi 26351335 211 QLGSN 215
Cdd:COG0666 283 LDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-213 2.94e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 2.94e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  43 IHDKDMGKIHKAASVGDVAKVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAV 122
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 123 QCQEEECAAILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKK 202
Cdd:COG0666  96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                       170
                ....*....|.
gi 26351335 203 KASIHAVDQLG 213
Cdd:COG0666 176 GADVNARDNDG 186
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-177 7.84e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 7.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335    85 LHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHgADPNvMDSSGNTALHYAVYSENTSMAA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 26351335   165 KLLAHNANIEAKN 177
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-184 7.74e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 7.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  51 IHKAASVGDVAKVQhILIlgKSG--VNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEE 128
Cdd:COG0666 157 LHLAAANGNLEIVK-LLL--EAGadVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26351335 129 CAAILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPM 184
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-144 2.10e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 2.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335    51 IHKAASVGDVAKVQHILILGkSGVNDRDKKDRTALHLACAYGHPEVVTLLVErKCEIDARDsESSTALIKAVQCQEEECA 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 26351335   131 AILLDHGADPNVMD 144
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-213 4.16e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 4.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  66 ILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHGADPNVMDS 145
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26351335 146 SGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVDQLG 213
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 51-204 1.99e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.65  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   51 IHKAASVGDVAKVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26351335  131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKD-DLTPMLLAVKENKQHIVEFLVKKKA 204
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGA 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-210 5.64e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 5.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   41 YHIHDKDMGKIHKAASVGDVAKVQHILILGkSGVNDRDKKDRTALHLACAYGHP---EVVTLLVERKCEIDARDSESSTA 117
Cdd:PHA03095   8 DIIMEAALYDYLLNASNVTVEEVRRLLAAG-ADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  118 LIKAVQCQ-EEECAAILLDHGADPNVMDSSGNTALHyaVY----SENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENK 192
Cdd:PHA03095  87 LHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRN 164

                        170       180
                 ....*....|....*....|
gi 26351335  193 QHI--VEFLVKKKASIHAVD 210
Cdd:PHA03095 165 ANVelLRLLIDAGADVYAVD 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-226 4.55e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   66 ILILGKSGVNDRDKKDRTALHLACAYGHP--EVVTLLVERKCEIDARDSESSTAL-IKAVQCQeeeCAAI----LLDHGA 138
Cdd:PHA03095 172 LLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLhSMATGSS---CKRSlvlpLLIAGI 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  139 DPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAV----DQLGS 214
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVaatlNTASV 328

                        170
                 ....*....|..
gi 26351335  215 NRQMFEYDGKRL 226
Cdd:PHA03095 329 AGGDIPSDATRL 340
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-210 2.26e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   62 KVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTAL-----IKAVQCQEEECAAILLDH 136
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEY 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26351335  137 GADPNVMDSSGNTALHYAVY--SENTSMAAKLLAHNANIEAKNKDDLTPMLLAVK--ENKQHIVEFLVKKKASIHAVD 210
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKN 173
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-211 7.29e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 7.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   41 YHIHDKDMgkihkaASVGDVAKVQHILILGKSGVNDRDKKDRTALHLACAY--GHPEVVTLLVERKCEIDARDSESSTAL 118
Cdd:PHA03100  72 LHYLSNIK------YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  119 IKAVQC--QEEECAAILLDHGADPNVMDS----------------SGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDD 180
Cdd:PHA03100 146 HLYLESnkIDLKILKLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225

                        170       180       190
                 ....*....|....*....|....*....|.
gi 26351335  181 LTPMLLAVKENKQHIVEFLVKKKASIHAVDQ 211
Cdd:PHA03100 226 DTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-277 7.62e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.51  E-value: 7.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   54 AASVGDVAKVQHILILGKSGvNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAIL 133
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDP-DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  134 --LDHGADPNvmdsSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAV-- 209
Cdd:PLN03192 611 yhFASISDPH----AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnt 686

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26351335  210 DQLGSNRQMFEYDGKRlQRSENSNPVDNGSEDGSLTRSYNTPGPADSWPTSdeedynFDNKNVPKINL 277
Cdd:PLN03192 687 DDDFSPTELRELLQKR-ELGHSITIVDSVPADEPDLGRDGGSRPGRLQGTS------SDNQCRPRVSI 747
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 59-210 4.17e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   59 DVAKVQHILILGkSGVNDRDKKDRTALHLACAYG-HPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHG 137
Cdd:PHA02876 320 DTENIRTLIMLG-ADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26351335  138 ADPNVMDSSGNTALHYAVYSENTSMAAK-LLAHNANIEAKNKDDLTPMLLAVKEN-KQHIVEFLVKKKASIHAVD 210
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAIN 473
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 74-214 5.79e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 5.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   74 VNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHGADPNVMDSSGNTALHY 153
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26351335  154 AVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQhIVEFLVkKKASIHAVDQLGS 214
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI-NNASINDQDIDGS 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 43-190 5.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   43 IHDKDMGK--IHKAASVGDvAKVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIK 120
Cdd:PHA02878 162 MKDRHKGNtaLHYATENKD-QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26351335  121 AV-QCQEEECAAILLDHGADPNVMDS-SGNTALHYAVYSENTSMAakLLAHNANIEAKNKDDLTPMLLAVKE 190
Cdd:PHA02878 241 SVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKL--LLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-212 8.85e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 8.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   25 CVGFGRESASGSHVPRYHIHDK-DMGKIHKAASVGDVAKVQHILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVER 103
Cdd:PHA02876 121 CIHILKEAISGNDIHYDKINESiEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  104 ---------------KCEIDARDSESSTALI--------------KAVQCQEEECAAILLDHGADPNVMDSSGNTALHYA 154
Cdd:PHA02876 201 gadvniialddlsvlECAVDSKNIDTIKAIIdnrsninkndlsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA 280

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  155 VYSENTS-MAAKLLAHNANIEAKNKDDLTPMLLAVKEN-KQHIVEFLVKKKASIHAVDQL 212
Cdd:PHA02876 281 SQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRL 340
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 41-210 1.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   41 YHIHDKDMGKIHKAASVGdvAKVQHILILGKSGVNDRDK-KDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALI 119
Cdd:PHA02878 129 QTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  120 KAVQCQEEECAAILLDHGADPNVMDSSGNTALHYAV-YSENTSMAAKLLAHNANIEAKNK-DDLTPMLLAVKEnkQHIVE 197
Cdd:PHA02878 207 HAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLK 284

                        170
                 ....*....|...
gi 26351335  198 FLVKKKASIHAVD 210
Cdd:PHA02878 285 LLLEYGADINSLN 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 51-214 2.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   51 IHKAASVGDVAKVQHILILGKSgVNDRDKKDRTALHLACAY----GHPEVVTLLVERKCE-------------------- 106
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHN-VNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFytlvaikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  107 --IDARDSESSTALIKAVQCQ-----EEECAAILLDHGADPNVMD-SSGNTALHYAVYSENTSMAAKLLAHNANIEAKNK 178
Cdd:PHA02878 120 ilTNRYKNIQTIDLVYIDKKSkddiiEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 26351335  179 DDLTPMLLAVKENKQHIVEFLVKKKASIHAVDQLGS 214
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-207 1.25e-09

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: 59.26  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  83 TALHLACAYGHPEVVTLLVERKCE-IDARD-----SESSTALIK--------AVQCQEEECAAILLDHGADPNVMDSSGN 148
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADvVSPRAtgtffRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26351335 149 TALHYAVYSENTSMAAK----LLAHNANIEA------KNKDDLTPMLLAVKENKQHIVEFLVKKKASIH 207
Cdd:cd22192 171 TVLHILVLQPNKTFACQmydlILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQ 239
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-167 4.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 26351335   115 STALIKAVQCQEEECAAILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLL 167
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-121 5.71e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 5.71e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 26351335    74 VNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKA 121
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-224 5.85e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  130 AAILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHav 209
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF-- 175

                         90
                 ....*....|....*
gi 26351335  210 dQLGSNRQMFEYDGK 224
Cdd:PTZ00322 176 -ELGANAKPDSFTGK 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-202 1.59e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 1.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 26351335   151 LHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKK 202
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-203 2.38e-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: 52.39  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335    74 VNDRDK----KDRTALHLACAYGHPEVVTLLVERKCEIDAR----------------DSESSTALIKAVQcqEEECAAIL 133
Cdd:TIGR00870 117 ANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvdsfyHGESPLNAAACLG--SPSIVALL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   134 LDHGADPNVMDSSGNTALHYAV-----YSENTSM-------AAKLLAHNANIEA----KNKDDLTPMLLAVKENK----Q 193
Cdd:TIGR00870 195 SEDPADILTADSLGNTLLHLLVmenefKAEYEELscqmynfALSLLDKLRDSKEleviLNHQGLTPLKLAAKEGRivlfR 274

                         170
                  ....*....|
gi 26351335   194 HIVEFLVKKK 203
Cdd:TIGR00870 275 LKLAIKYKQK 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-251 2.54e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   56 SVGDVAKVqhILILGKSG--VNDRDKKDRTALHL-ACAYGHPEVVTLLVERKCEIDARDSESSTALIK--AVQCQEEECA 130
Cdd:PHA03095  58 SSEKVKDI--VRLLLEAGadVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  131 AILLDHGADPNVMDSSGNTALHYAVYSENTSMA--AKLLAHNANIEAKNKDDLTP---MLLAVKENKQhIVEFLVKKKAS 205
Cdd:PHA03095 136 RLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLlhhHLQSFKPRAR-IVRELIRAGCD 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 26351335  206 IHAVDQLGSNRQMFEYDGKRLQRSENSNPVDNGSEDGSLTRSYNTP 251
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTP 260
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 67-211 3.96e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   67 LILGKSG--VNDRDKKDRTALHLAC-AYGHPEVVTLLVERKCEIDARDSESSTAL-IKAVQCQEEECAAILLDHGADPNV 142
Cdd:PHA02876 257 LLLYDAGfsVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNA 336

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  143 MDSSGNTALHYA-VYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVDQ 211
Cdd:PHA02876 337 ADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 80-205 5.30e-07

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.42  E-value: 5.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  80 KDRTALHLACAYGHPEVVTLLVERKCEIDARdseSSTALIKAVQC----------------QEEECAAILLDHGADP--- 140
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADVSAR---ATGRFFRKSPGnlfyfgelplslaactNQEEIVRLLLENGAQPaal 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 141 NVMDSSGNTALHYAVYSEN---------TSMAAKLLAHNANI-------EAKNKDDLTPMLLAVKENKQHIVEFLVKKKA 204
Cdd:cd21882 149 EAQDSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQREF 228


                .
gi 26351335 205 S 205
Cdd:cd21882 229 S 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 52-136 6.11e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 6.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   52 HKAASvGDVAKVQhILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAA 131
Cdd:PTZ00322  88 QLAAS-GDAVGAR-ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                 ....*
gi 26351335  132 ILLDH 136
Cdd:PTZ00322 166 LLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-200 7.63e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 7.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 26351335   147 GNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLV 200
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-187 8.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 8.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 26351335   133 LLDHG-ADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLA 187
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 98-213 1.04e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  98 TLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDhgADP----NVMDSS---GNTALHYAVYSENTSMAAKLLAHN 170
Cdd:cd22192  35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARG 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26351335 171 ANIEA---------KNKDDLT-----PMLLAVKENKQHIVEFLVKKKASIHAVDQLG 213
Cdd:cd22192 113 ADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 51-212 1.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   51 IHKAASVGDVAKVQHILILGkSGVNDRDKKDRTALHLACAYGHPEVVTLLVERKCEIDARDSESSTALIKAVQCQEEECA 130
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  131 AILLDHG-------------------------------ADPNVMDSSGNTALHYAV-YSENTSMAAKLLAHNANIEAKNK 178
Cdd:PHA02874 207 KLLIDHGnhimnkckngftplhnaiihnrsaiellinnASINDQDIDGSTPLHHAInPPCDIDIIDILLYHKADISIKDN 286

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 26351335  179 DDLTPMLLAVKE-NKQHIVEFLVKKKASIHAVDQL 212
Cdd:PHA02874 287 KGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKL 321
Ank_5 pfam13857
Ankyrin repeats (many copies);
99-154 2.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 26351335    99 LLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHGADPNVMDSSGNTALHYA 154
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 80-207 2.25e-06

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: 49.37  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  80 KDRTALHLACAYGHPEVVTLLVERKCEIDARDSE--------------SSTALIKAVQCQEEECAAILLDHGADPNVM-D 144
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSqD 219

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26351335 145 SSGNTALHYAVY----SEN-----TSMAAKLL--AHNANIEA-KNKDDLTPMLLAVKENK----QHIVEFLVKKKASIH 207
Cdd:cd22194 220 SRGNTVLHALVTvaedSKTqndfvKRMYDMILlkSENKNLETiRNNEGLTPLQLAAKMGKaeilKYILSREIKEKPNRS 298
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-213 3.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   54 AASVGDVAKVQhILILGKSGVNDRDKKDRTALHLACAYGHPEVVTLLVerkceIDARDSEsstalIKAVQCQEEECAAIL 133
Cdd:PHA02874  42 AIRSGDAKIVE-LFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNGVDTS-----ILPIPCIEKDMIKTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  134 LDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVDQLG 213
Cdd:PHA02874 111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 95-206 4.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 4.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335   95 EVVTLLVERKCEIDARDSESSTALIKAVQCQEEECAAILLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIE 174
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110
                 ....*....|....*....|....*....|..
gi 26351335  175 AKNKDDLTPMLLAVKENKQHIVEFLVKKKASI 206
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 5.65e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 5.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 26351335    51 IHKAASVGDVAKVQHILILGKSgVNDRDKKDRTALHLACAYGHPEVVTLLV 101
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-111 2.07e-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: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 26351335    82 RTALHLACA-YGHPEVVTLLVERKCEIDARD 111
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-109 7.58e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 7.58e-05
                          10        20
                  ....*....|....*....|....*...
gi 26351335    82 RTALHLACAYGHPEVVTLLVERKCEIDA 109
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 147-178 9.56e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 9.56e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 26351335   147 GNTALHYAVYSE-NTSMAAKLLAHNANIEAKNK 178
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 83-207 1.64e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  83 TALHLACAYGHPEVVTLLVE---RKCEIDARDSESSTALIKAVQCQEeecaailldhgadpnvmDSSGNTALHYAVYSEN 159
Cdd:cd22193 125 LPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVTVAD-----------------NTKENTKFVTRMYDMI 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 26351335 160 TSMAAKLLAHNANIEAKNKDDLTPMLLAVKENK----QHIVEFLVKKKASIH 207
Cdd:cd22193 188 LIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKieilKYILQREIKEPELRH 239
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-109 1.64e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.64e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 26351335     80 KDRTALHLACAYGHPEVVTLLVERKCEIDA 109
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 121-213 3.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  121 AVQCQEEECAAILLDHGADPNV------------------------MDSS----------GNTALHYAVYSENTSMAAKL 166
Cdd:PHA02875  42 AMKFRDSEAIKLLMKHGAIPDVkypdieselhdaveegdvkaveelLDLGkfaddvfykdGMTPLHLATILKKLDIMKLL 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 26351335  167 LAHNANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKASIHAVDQLG 213
Cdd:PHA02875 122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 132-204 5.34e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 5.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26351335  132 ILLDHGADPNVMDS-SGNTALHYAVYSENTSMAAKLLAH-NANIEAKNKDDLTPMLLAVKENKQHIVEFLVKKKA 204
Cdd:PHA02736  76 LLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 147-175 1.15e-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: 36.03  E-value: 1.15e-03
                           10        20
                   ....*....|....*....|....*....
gi 26351335    147 GNTALHYAVYSENTSMAAKLLAHNANIEA 175
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 133-213 1.44e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  133 LLDHGADPNVMDSSGNTALHYAVYSENTSMAAKLLAHNANIEAKNKDDLTPMLLAVKENKQHI--VEFLVKKKASI-HAV 209
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKInNSV 137


                 ....
gi 26351335  210 DQLG 213
Cdd:PHA02946 138 DEEG 141
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 99-215 1.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  99 LLVERKCEIDARDSESSTA---LIKAV---QCQEEECAAILLDHGADPNVMDS-----------SGNTALHYAVYSENTS 161
Cdd:cd22193  11 LCRRRKDLTDSEFTESSTGktcLMKALlnlNPGTNDTIRILLDIAEKTDNLKRfinaeytdeyyEGQTALHIAIERRQGD 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26351335 162 MAAKLLAHNANIEAKNKDDL--------------TPMLLAVKENKQHIVEFLVK---KKASIHAVDQLGSN 215
Cdd:cd22193  91 IVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
PHA02741 PHA02741
hypothetical protein; Provisional
 121-205 2.96e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  121 AVQCQEEECAAILLDH----GADPNVMDS-SGNTALHYAVYSENTSMAAKLLAH-NANIEAKNKDDLTPMLLAVKENKQH 194
Cdd:PHA02741  67 AAEKHEAQLAAEIIDHlielGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVA 146

                         90
                 ....*....|.
gi 26351335  195 IVEFLVKKKAS 205
Cdd:PHA02741 147 MMQILREIVAT 157
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 110-214 4.73e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 38.71  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 110 RDSESSTALIKAV---QCQEEECAAILLDhgADPNVMDSS-------------GNTALHYAVYSENTSMAAKLLAHNANI 173
Cdd:cd21882  22 RGATGKTCLHKAAlnlNDGVNEAIMLLLE--AAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADV 99

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26351335 174 EAKNKDDL-------------TPMLLAVKENKQHIVEFLVK---KKASIHAVDQLGS 214
Cdd:cd21882 100 SARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGN 156
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 80-207 9.01e-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: 37.91  E-value: 9.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335  80 KDRTALHLACAYGHPEVVTLLVERKCEIDA---------RDSES-----STALIKAVQCQEEECAAILLDHG---ADPNV 142
Cdd:cd22195 136 RGQTALHIAIERRCKHYVELLVEKGADVHAqargrffqpKDEGGyfyfgELPLSLAACTNQPDIVHYLTENAhkkADLRR 215

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26351335 143 MDSSGNTALHYAVY-----SENTSMAAKL----------LAHNANIEA-KNKDDLTPMLLAVKENK----QHIVEFLVKK 202
Cdd:cd22195 216 QDSRGNTVLHALVAiadntRENTKFVTKMydlllikcakLYPDCNLEAiLNNDGMSPLMMAAKLGKigifQHIIRREIKD 295


                ....*
gi 26351335 203 KASIH 207
Cdd:cd22195 296 EEARH 300
 
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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