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Conserved domains on  [gi|1039755807|ref|XP_017173358|]
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ankyrin repeat domain-containing protein 29 isoform X3 [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];
79-314 1.03e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGH 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 159 MPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 238
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755807 239 DAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPA 314
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-314 1.03e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGH 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 159 MPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 238
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755807 239 DAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPA 314
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-207 2.14e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 117 LFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 196
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1039755807 197 LLLSSGAKVNQ 207
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-326 3.67e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 161 VVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVMLL 233
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 234 RGADRDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVA 294
Cdd:PHA03100  130 NGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEFVK 209

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039755807 295 LLLEAGADPALRNKANELPAE---LTKNERILHLL 326
Cdd:PHA03100  210 YLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 115-249 1.87e-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: 58.87  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 115 TALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IHDQLYDGATALFLAAQ 188
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039755807 189 GGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRDAARNDGTTAL 249
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 100-254 5.07e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.15  E-value: 5.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 100 NSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH------ 173
Cdd:TIGR00870  39 EPKKLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpl 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 174 --------DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVM 231
Cdd:TIGR00870 115 elandqytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALL 194

                         170       180
                  ....*....|....*....|...
gi 1039755807 232 LLRGADRDAARNDGTTaLLKAAN 254
Cdd:TIGR00870 195 SEDPADILTADSLGNT-LLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 178-206 9.47e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 9.47e-05
                           10        20
                   ....*....|....*....|....*....
gi 1039755807  178 DGATALFLAAQGGYLDVIRLLLSSGAKVN 206
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-314 1.03e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGH 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 159 MPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 238
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755807 239 DAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPA 314
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-343 6.69e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 6.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGH 158
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 159 MPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 238
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 239 DAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPAELT 317
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                         250       260
                  ....*....|....*....|....*.
gi 1039755807 318 KNERILHLLRQKEGPGKNELGSILDR 343
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-329 4.34e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 4.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 105 DVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALF 184
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 185 LAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEEL 264
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755807 265 LKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELP---AELTKNERILHLLRQK 329
Cdd:COG0666   173 LEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAldlAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-207 2.14e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 117 LFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 196
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1039755807 197 LLLSSGAKVNQ 207
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-307 2.93e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 2.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 216 LWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNVKTVAL 295
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1039755807 296 LLEAGADPALRN 307
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
150-237 4.40e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 4.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 150 LLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPrqDGTAPLWIASQMGHSEVVR 229
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1039755807 230 VMLLRGAD 237
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-326 3.67e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 161 VVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVMLL 233
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 234 RGADRDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVA 294
Cdd:PHA03100  130 NGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEFVK 209

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039755807 295 LLLEAGADPALRNKANELPAE---LTKNERILHLL 326
Cdd:PHA03100  210 YLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 105-244 8.78e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.29  E-value: 8.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 105 DVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVEtLLKHGANIHDQlYDGATALF 184
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDP-HAAGDLLC 627

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 185 LAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARND 244
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-175 1.24e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  84 FWAAKRGNLALLKLLLNSGrVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 163
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039755807 164 TLLKHGANIHDQ 175
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-323 5.01e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 105 DVDCRDSSGTTALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGTALLA--ASQYGHMPVVETLLKHGANIHDQLYDGAT 181
Cdd:PHA03095   75 DVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 182 AL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHS--EVVRVMLLRGADRDAARNDGTTALLKAANKGY 257
Cdd:PHA03095  155 PLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSS 234

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755807 258 --NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPAELT---KNERIL 323
Cdd:PHA03095  235 ckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMvrnNNGRAV 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 124-303 1.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 124 GHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGA 203
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 204 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 281
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|..
gi 1039755807 282 HAAVLSGNVKTVALLLEAGADP 303
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANI 194
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-313 1.52e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.47  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 102 GRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQlydgAT 181
Cdd:PHA02876  167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN----DL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 182 ALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGH-SEVVRVMLLRGADRDAARNDGTTALLKAANKGYNdv 260
Cdd:PHA02876  243 SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYD-- 320

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755807 261 iEELLKFSPTLGILKNGTSALH------AAVLSGNVKTVALLLEAGADPALRNKANELP 313
Cdd:PHA02876  321 -TENIRTLIMLGADVNAADRLYitplhqASTLDRNKDIVITLLELGANVNARDYCDKTP 378
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 161-313 3.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 161 VVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 238
Cdd:PHA02878  149 ITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755807 239 DAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGNVktVALLLEAGADPALRNKANELP 313
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTP 303
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 185-268 6.72e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 6.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 185 LAAQGGYLDvIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEEL 264
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1039755807 265 LKFS 268
Cdd:PTZ00322  168 SRHS 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-199 3.98e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 3.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755807 146 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 199
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-270 4.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 104 VDVDCRDSSGTTALFFAAQQ--GHNDVVRFLFGFGASTECRTKDGGTALLAASQYGH--MPVVETLLKHGANIHDqlydg 179
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA----- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 180 atalflaaqggyLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYND 259
Cdd:PHA03100  172 ------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239

                         170
                  ....*....|.
gi 1039755807 260 VIEELLKFSPT 270
Cdd:PHA03100  240 IFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 126-313 5.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 5.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 126 NDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 205
Cdd:PHA02874  104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 206 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANkgYNDVIEELLKFSPTLGILK-NGTSALHAA 284
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDiDGSTPLHHA 261

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039755807 285 V-LSGNVKTVALLLEAGADPALRNKANELP 313
Cdd:PHA02874  262 InPPCDIDIIDILLYHKADISIKDNKGENP 291
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 105-240 7.25e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 105 DVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAAsQYGHMPV--VETLLKHGANIHDQLYDGATA 182
Cdd:PHA02876  367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKNKDLSTP 445

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 183 LFLAAQGG-YLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAD-RDA 240
Cdd:PHA02876  446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-237 1.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  86 AAKRGNLALLKLLLNSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETL 165
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039755807 166 LKHGA--NIHDQLydGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAD 237
Cdd:PHA02875  155 IDHKAclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 115-249 1.87e-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: 58.87  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 115 TALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IHDQLYDGATALFLAAQ 188
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039755807 189 GGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRDAARNDGTTAL 249
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 127-304 2.89e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 127 DVVRFLFGFGASTECRTKDGGTALLAASQYGHMP---VVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLSSG 202
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 203 AKVNQPRQDGTAPLWI--ASQMGHSEVVRVMLLRGADRDAARNDGTTALlkaankgynDVieeLLKFsptlgilkngtsa 280
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPL---------AV---LLKS------------- 162

                         170       180
                  ....*....|....*....|....
gi 1039755807 281 lHAAvlsgNVKTVALLLEAGADPA 304
Cdd:PHA03095  163 -RNA----NVELLRLLIDAGADVY 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 146-283 3.74e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 146 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSgAKVNQPRQDGTApLWIASQMGHS 225
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755807 226 EVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKNGTSALHA 283
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMNGADVDKA 684
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-166 1.05e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755807 113 GTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLL 166
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-185 2.84e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 101 SGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKH-------GANIH 173
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANAK 182

                          90
                  ....*....|..
gi 1039755807 174 DQLYDGATALFL 185
Cdd:PTZ00322  183 PDSFTGKPPSLE 194
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 144-266 3.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 144 KDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMG 223
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039755807 224 HSEVVRVMLLRGADRD-AARNDGTTALLKAANKGYNDVIEELLK 266
Cdd:PHA02875  180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 105-257 7.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 105 DVDCRD-SSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATAL 183
Cdd:PHA02878  159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755807 184 FLAAqgGYL---DVIRLLLSSGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGADRDAARNDGTTALLKAANKGY 257
Cdd:PHA02878  239 HISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 129-200 2.35e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755807 129 VRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLS 200
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 148-310 3.59e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 148 TALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLL-----------------------LSSGAK 204
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 205 VNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHA 283
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnNGESPLHN 196

                         170       180
                  ....*....|....*....|....*..
gi 1039755807 284 AVLSGNVKTVALLLEAGADpaLRNKAN 310
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNH--IMNKCK 221
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 151-232 5.12e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 151 LAASqyGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRV 230
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1039755807 231 ML 232
Cdd:PTZ00322  167 LS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-232 2.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039755807 181 TALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 232
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 157-313 3.51e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 157 GHMPVVETLLKHGAN-IHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRG 235
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 236 AD--------------------------RDAarnDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSG 288
Cdd:PHA02874   92 VDtsilpipciekdmiktildcgidvniKDA---ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHN 168

                         170       180
                  ....*....|....*....|....*
gi 1039755807 289 NVKTVALLLEAGADPALRNKANELP 313
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESP 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 191-322 3.75e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 191 YLDVIRLLLSSGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGADRDAARNDGTTALLKAAnkgYNDVIEEL 264
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755807 265 LKFSPTLG--IL---KNGTSALHA--AVLSGNVKTVALLLEAGADPALRNKANELP-AELTKNERI 322
Cdd:PHA03095  100 IKLLIKAGadVNakdKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPlAVLLKSRNA 165
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 85-313 4.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807  85 WAAKRGNLALLKLLLNSGrVDVDCRDSSGTTALFFAAQQGHNDVVR-----------------------------FLFGF 135
Cdd:PHA02876  184 YAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDA 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 136 GASTECRTKDGGTALLAASQYGHMP-VVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLSSGAKVNQPRQDGT 213
Cdd:PHA02876  263 GFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 214 APLWIASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL--KNGTsALHAAVLSGN- 289
Cdd:PHA02876  343 TPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-ALHFALCGTNp 421

                         250       260
                  ....*....|....*....|....
gi 1039755807 290 VKTVALLLEAGADPALRNKANELP 313
Cdd:PHA02876  422 YMSVKTLIDRGANVNSKNKDLSTP 445
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 104-265 4.65e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 104 VDVDCRDSSGTTALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGTALLAASQYG-HMPVVETLLKHGANIHDQLYDGAT 181
Cdd:PHA02876  298 ADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKT 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 182 ALFLAAQGGYLDVIRLLLSSGAKVNQPRQD-GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYN-D 259
Cdd:PHA02876  378 PIHYAAVRNNVVIINTLLDYGADIEALSQKiGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlD 457


                  ....*.
gi 1039755807 260 VIEELL 265
Cdd:PHA02876  458 VIEMLL 463
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 100-254 5.07e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.15  E-value: 5.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 100 NSGRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH------ 173
Cdd:TIGR00870  39 EPKKLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpl 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 174 --------DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVM 231
Cdd:TIGR00870 115 elandqytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALL 194

                         170       180
                  ....*....|....*....|...
gi 1039755807 232 LLRGADRDAARNDGTTaLLKAAN 254
Cdd:TIGR00870 195 SEDPADILTADSLGNT-LLHLLV 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 105-206 1.84e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 105 DVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDG-ATAL 183
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAAL 206

                          90       100
                  ....*....|....*....|...
gi 1039755807 184 FLAAQGGYLDVIRLLLSSGAKVN 206
Cdd:PHA02875  207 CYAIENNKIDIVRLFIKRGADCN 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-150 2.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039755807 102 GRVDVDCRDSSGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 150
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 148-303 2.23e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 148 TALLAASQYGHMPVVETLLK-HGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAK-VNQPRQ----DGTAPLWIASQ 221
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 222 MGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDviEELLKFsptlgilkngtsalhaAVLSGNVKTVALLLEAGA 301
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNLIYYG--EHPLSF----------------AACVGNEEIVRLLIEHGA 160


                  ..
gi 1039755807 302 DP 303
Cdd:cd22192   161 DI 162
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 245-306 6.61e-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: 44.49  E-value: 6.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755807 245 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGADPALR 306
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 178-206 9.47e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 9.47e-05
                           10        20
                   ....*....|....*....|....*....
gi 1039755807  178 DGATALFLAAQGGYLDVIRLLLSSGAKVN 206
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 276-308 9.64e-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: 9.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039755807 276 NGTSALHAAVLS-GNVKTVALLLEAGADPALRNK 308
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 161-266 1.02e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 161 VVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLSSGAKVNQPRQDGTAPLWIA---SQMGHSEVVRVML 232
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMI 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039755807 233 LRGADRDAARNDGTTAL---LKAANKGYNDVIEELLK 266
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 245-330 1.43e-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: 43.63  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 245 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNVKTVALLLEAGADPALRNKA 309
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAKG 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039755807 310 N--------------ELPAEL---TKNERILHLLRQKE 330
Cdd:cd22193   109 RffqpkyqgegfyfgELPLSLaacTNQPDIVQYLLENE 146
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 146-298 1.55e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 146 GGTALLAASQYGH-------MPVVETLLKHG-------ANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVnQPRQD 211
Cdd:cd21882    26 GKTCLHKAALNLNdgvneaiMLLLEAAPDSGnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 212 GTA--------------PLWIASQMGHSEVVRVMLLRGAD------RDAARNDGTTALLKAANKG----------YNDVI 261
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039755807 262 EELLKFSPT--LGILKN--GTSALHAAVLSGNVKTVALLLE 298
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
245-297 1.61e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 1.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755807 245 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLL 297
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 145-175 2.18e-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: 38.04  E-value: 2.18e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039755807 145 DGGTAL-LAASQYGHMPVVETLLKHGANIHDQ 175
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
 104-304 3.47e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 104 VDVDCRDSSGTTALFfAAQQGHN---DVVRFLFGFGASTecRTKD--GGTALLAASQYGH--MPVVETLLKHGANIHDQL 176
Cdd:PHA03095  143 ADVNALDLYGMTPLA-VLLKSRNanvELLRLLIDAGADV--YAVDdrFRSLLHHHLQSFKprARIVRELIRAGCDPAATD 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 177 YDGATALFLAAQGGYLD--VIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAAN 254
Cdd:PHA03095  220 MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755807 255 KGYNDVIEELLKFSPTL----GILKNGTSALHAAVLSGN---VKTVALLLEAGADPA 304
Cdd:PHA03095  300 NNNGRAVRAALAKNPSAetvaATLNTASVAGGDIPSDATrlcVAKVVLRGAFSLLPE 356
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 161-296 4.41e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 161 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLSSGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGADRDA 240
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755807 241 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNVKTVALL 296
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-265 4.89e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 4.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755807 212 GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELL 265
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-132 5.45e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 5.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039755807  81 NAAFWAAKRGNLALLKLLLNSGrVDVDCRDSSGTTALFFAAQQGHNDVVRFL 132
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 245-302 5.91e-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: 41.72  E-value: 5.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755807 245 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGAD 302
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
Ank_4 pfam13637
Ankyrin repeats (many copies);
277-326 6.51e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039755807 277 GTSALHAAVLSGNVKTVALLLEAGADPALRNKANELP---AELTKNERILHLL 326
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAlhfAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 276-303 7.67e-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: 36.41  E-value: 7.67e-04
                           10        20
                   ....*....|....*....|....*...
gi 1039755807  276 NGTSALHAAVLSGNVKTVALLLEAGADP 303
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-138 1.03e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755807  66 ADMCRMSFKKETPLanaaFWAAKRGNLALLKLLLNSGRVDVDCrdsSGTTALFFAAQQGHNDVVRFLFGFGAS 138
Cdd:pfam12796  21 ADANLQDKNGRTAL----HLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 127-206 1.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 127 DVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN 206
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02798 PHA02798
ankyrin-like protein; Provisional
 127-207 1.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 127 DVVRFLFGFGASTECRTKDGGT---ALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLS 200
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169


                  ....*..
gi 1039755807 201 SGAKVNQ 207
Cdd:PHA02798  170 KGVDINT 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 145-174 2.33e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755807  145 DGGTALLAASQYGHMPVVETLLKHGANIHD 174
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 276-316 2.94e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039755807 276 NGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPAEL 316
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 127-267 3.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.34  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 127 DVVRFLF--GFGASTECRtkdGGTALLaasQYGHMPVVET-----LLKHGANI-HDQLYDGATALFLA----AQGGYLDV 194
Cdd:PHA02989   17 NALEFLLrtGFDVNEEYR---GNSILL---LYLKRKDVKIkivklLIDNGADVnYKGYIETPLCAVLRnreiTSNKIKKI 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755807 195 IRLLLSSGAKVNQPRQDGTAPLWI---ASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYN---DVIEELLKF 267
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPIVCfiyNSNINNCDMLRFLLSKGINVNDVKNSRGYNLLHMYLESFSvkkDVIKILLSF 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 175-311 5.96e-03

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: 38.52  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755807 175 QLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQ--PRQDGTAPL-WIASQMGHSEVVRVMLLRGadRDAARNDgttALLK 251
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLNIncPDRLGRSALfVAAIENENLELTELLLNLS--CRGAVGD---TLLH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039755807 252 AANKGYNDVIEELLK---------------FSPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANE 311
Cdd:TIGR00870  88 AISLEYVDAVEAILLhllaafrksgplelaNDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDF 162
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 145-173 6.30e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 6.30e-03
                          10        20
                  ....*....|....*....|....*....
gi 1039755807 145 DGGTALLAASQYGHMPVVETLLKHGANIH 173
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
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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