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Conserved domains on  [gi|1907129472|ref|XP_036016982|]
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ankyrin repeat domain-containing protein 29 isoform X6 [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];
74-305 5.89e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  74 KHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYG 153
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 154 HMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 233
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129472 234 RDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-305 5.89e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  74 KHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYG 153
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 154 HMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 233
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129472 234 RDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-171 2.45e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  80 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 159
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1907129472 160 TLLKHGANIHDQ 171
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 76-201 3.89e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 84.92  E-value: 3.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  76 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTkdGGTALLAASQYGHM 155
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDL 635

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129472 156 PVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 201
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 96-245 6.52e-10

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: 59.64  E-value: 6.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  96 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IH 169
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 170 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRD 235
Cdd:cd22192    84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                         170
                  ....*....|
gi 1907129472 236 AARNDGTTAL 245
Cdd:cd22192   164 AQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.03e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.03e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907129472  174 DGATALFLAAQGGYLDVIRLLLSSGAKVN 202
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-250 1.88e-04

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: 42.76  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 101 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH----------- 169
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 170 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 232
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1907129472 233 DRDAARNDGTTaLLKAAN 250
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-305 5.89e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  74 KHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYG 153
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 154 HMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 233
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129472 234 RDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-262 2.36e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 2.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  71 MSFKHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAAS 150
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 151 QYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLR 230
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907129472 231 GADRDAARNDGTTALLKAANKGYNDVIEELLK 262
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-305 7.31e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 7.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  77 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMP 156
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 157 VVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDA 236
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 237 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-245 3.65e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 3.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  74 KHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYG 153
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 154 HMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 233
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277

                         170
                  ....*....|..
gi 1907129472 234 RDAARNDGTTAL 245
Cdd:COG0666   278 LAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-305 8.55e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 8.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  92 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQ 171
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 172 LYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANK 251
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907129472 252 GYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-171 2.45e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  80 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 159
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1907129472 160 TLLKHGANIHDQ 171
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-203 2.43e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 113 LFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 192
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1907129472 193 LLLSSGAKVNQ 203
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
212-303 3.45e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 3.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 212 LWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNVKTVAL 291
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1907129472 292 LLEAGADPALRN 303
Cdd:pfam12796  80 LLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 76-201 3.89e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 84.92  E-value: 3.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  76 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTkdGGTALLAASQYGHM 155
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDL 635

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129472 156 PVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 201
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
146-233 5.15e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 146 LLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPrqDGTAPLWIASQMGHSEVVR 225
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1907129472 226 VMLLRGAD 233
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 67-298 9.18e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 9.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  67 DMCRMSFKHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHN-----DVVRFLFGFGASTECRTKD 141
Cdd:PHA03100   26 DLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 142 GGTALLAASQY--GHMPVVETLLKHGANIHDQLYDGATALFLAAQGGY--LDVIRLLLSSGAKVNQprqdgtaplwiasq 217
Cdd:PHA03100  106 GITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA-------------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 218 mghSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAG 296
Cdd:PHA03100  172 ---KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNG 248


                  ..
gi 1907129472 297 AD 298
Cdd:PHA03100  249 PS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 157-305 1.15e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 157 VVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVMLL 229
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 230 RGADRDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVA 290
Cdd:PHA03100  130 NGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEFVK 209

                         170
                  ....*....|....*
gi 1907129472 291 LLLEAGADPALRNKN 305
Cdd:PHA03100  210 YLLDLGANPNLVNKY 224
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 79-240 2.01e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 73.75  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  79 LLMVASyAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVV 158
Cdd:PLN03192  529 LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 159 EtLLKHGANIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAAR 238
Cdd:PLN03192  608 R-ILYHFASISDP-HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685


                  ..
gi 1907129472 239 ND 240
Cdd:PLN03192  686 TD 687
PHA03095 PHA03095
ankyrin-like protein; Provisional
 90-302 6.48e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  90 DCVRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGTALLA--ASQYGHMPVVETLLKHGA 166
Cdd:PHA03095   64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 167 NIHDQLYDGATAL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHS--EVVRVMLLRGADRDAARNDGT 242
Cdd:PHA03095  144 DVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGN 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129472 243 TALLKAANKGY--NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALR 302
Cdd:PHA03095  224 TPLHSMATGSSckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-305 7.31e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 7.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  89 IDCVRELVLQGADINLQRESGTTALffaAQQGHN------DVVRFLFGFGASTECRTKDGGTALLAASQYGH-MPVVETL 161
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 162 LKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPL--WIASQMGHSEVVRVMLLRGADRDAA 237
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAV 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129472 238 RNDGTTALLKAAN--KGYNDVIEELLKFS-PTLGILKNGTSALHAAVLSGNVKT--VALLLEAGADPALRNKN 305
Cdd:PHA03095  184 DDRFRSLLHHHLQsfKPRARIVRELIRAGcDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRY 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 71-293 8.54e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 8.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  71 MSFKHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTE-----CRTKDggta 145
Cdd:PHA02874   30 ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipCIEKD---- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 146 llaasqyghmpVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVR 225
Cdd:PHA02874  106 -----------MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129472 226 VMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGI-LKNGTSALHAAVLSgNVKTVALLL 293
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKNGFTPLHNAIIH-NRSAIELLI 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 120-305 4.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 4.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 120 GHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGA 199
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 200 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 277
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|....*...
gi 1907129472 278 HAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKN 200
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 92-298 1.25e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  92 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHD 170
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 171 Q------------------LYDGA-----------TALFLAAQGGYLD-VIRLLLSSGAKVNQPRQDGTAPLWIASQMGH 220
Cdd:PHA02876  240 NdlsllkairnedletsllLYDAGfsvnsiddcknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 221 -SEVVRVMLLRGADRDAARNDGTTALLKAAN-KGYNDVIEELLKfsptLGILKNG-----TSALHAAVLSGNVKTVALLL 293
Cdd:PHA02876  320 dTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLE----LGANVNArdycdKTPIHYAAVRNNVVIINTLL 395


                  ....*
gi 1907129472 294 EAGAD 298
Cdd:PHA02876  396 DYGAD 400
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 181-264 5.48e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 181 LAAQGGYLDvIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEEL 260
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1907129472 261 LKFS 264
Cdd:PTZ00322  168 SRHS 171
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-253 5.66e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 5.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  92 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHD 170
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 171 QLYDGATALFLAAqgGYL---DVIRLLLSSGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGADRDAARNDGTTAL 245
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                  ....*...
gi 1907129472 246 LKAANKGY 253
Cdd:PHA02878  305 SSAVKQYL 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-134 7.19e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 7.19e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129472  76 GTTLLMVASYAGHIDCVRELvLQGADINLQrESGTTALFFAAQQGHNDVVRFLFGFGAS 134
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 157-299 8.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 8.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 157 VVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 234
Cdd:PHA02878  149 ITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907129472 235 DAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGNVktVALLLEAGADP 299
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSERK--LKLLLEYGADI 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 90-236 1.70e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  90 DCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAAsQYGHMPV--VETLLKHGAN 167
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGAN 434

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907129472 168 IHDQLYDGATALFLAAQGG-YLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAD-RDA 236
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 87-233 1.92e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  87 GHIDCVRELVLQGADIN-LQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHG 165
Cdd:PHA02875   79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907129472 166 A--NIHDQLydGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAD 233
Cdd:PHA02875  159 AclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-128 3.62e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907129472  76 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 128
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 57-267 4.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  57 ERGpagggtADMCRMSFKHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGAST 135
Cdd:PHA02876  295 ERG------ADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANV 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 136 ECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGG--YLDViRLLLSSGAKVNQPRQDGTAPLW 213
Cdd:PHA02876  369 NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTnpYMSV-KTLIDRGANVNSKNKDLSTPLH 447

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907129472 214 IASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAAnkGYNDVIEELLKFSPTL 267
Cdd:PHA02876  448 YACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 73-202 5.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  73 FKHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQY 152
Cdd:PHA02875   99 YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907129472 153 GHMPVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLSSGAKVN 202
Cdd:PHA02875  179 GDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-195 5.90e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 5.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907129472 142 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 96-245 6.52e-10

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: 59.64  E-value: 6.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  96 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IH 169
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 170 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRD 235
Cdd:cd22192    84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                         170
                  ....*....|
gi 1907129472 236 AARNDGTTAL 245
Cdd:cd22192   164 AQDSLGNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-261 2.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  78 TLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPV 157
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 158 VETLLKHGANIHDQLYDGATALFLAAQGGYlDVIRLLLSSgAKVNQPRQDGTAPLWIASQMGHS-EVVRVMLLRGADRDA 236
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISI 283

                         170       180
                  ....*....|....*....|....*...
gi 1907129472 237 ARNDGTTAL---LKAANKgyNDVIEELL 261
Cdd:PHA02874  284 KDNKGENPIdtaFKYINK--DPVIKDII 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 142-279 2.61e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 142 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSgAKVNQPRQDGTApLWIASQMGHS 221
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907129472 222 EVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKNGTSALHA 279
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMNGADVDKA 684
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-162 1.49e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907129472 109 GTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLL 162
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 90-272 1.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  90 DCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIH 169
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 170 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGADRDAARNDGTTALLKAA 249
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAI 262

                         170       180
                  ....*....|....*....|....
gi 1907129472 250 NKGYN-DVIEELLKFSPTLGILKN 272
Cdd:PHA02874  263 NPPCDiDIIDILLYHKADISIKDN 286
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 66-215 2.66e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  66 ADMCRMSFKHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTA 145
Cdd:PHA02878  158 ADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907129472 146 L-LAASQYGHMPVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLSSGAKVNQPRQDGTAPLWIA 215
Cdd:PHA02878  238 LhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 140-262 2.79e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 140 KDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMG 219
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907129472 220 HSEVVRVMLLRGADRD-AARNDGTTALLKAANKGYNDVIEELLK 262
Cdd:PHA02875  180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
188-305 4.29e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 4.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 188 LDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFS-PT 266
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGaDI 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907129472 267 LGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 144-305 1.60e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 144 TALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLL-----------------------LSSGAK 200
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 201 VNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHA 279
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnNGESPLHN 196

                         170       180
                  ....*....|....*....|....*.
gi 1907129472 280 AVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKN 222
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 125-196 2.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907129472 125 VRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLS 196
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 147-228 4.37e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 147 LAASqyGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRV 226
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1907129472 227 ML 228
Cdd:PTZ00322  167 LS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 78-304 4.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  78 TLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR-----------------------------FL 128
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 129 FGFGASTECRTKDGGTALLAASQYGHMP-VVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLSSGAKVNQPRQ 206
Cdd:PHA02876  260 YDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADR 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 207 DGTAPLWIASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL--KNGTsALHAAVLS 283
Cdd:PHA02876  340 LYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-ALHFALCG 418

                         250       260
                  ....*....|....*....|..
gi 1907129472 284 GN-VKTVALLLEAGADPALRNK 304
Cdd:PHA02876  419 TNpYMSVKTLIDRGANVNSKNK 440
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 92-181 4.91e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 4.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  92 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKH------- 164
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 1907129472 165 GANIHDQLYDGATALFL 181
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-228 2.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907129472 177 TALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 228
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-300 3.05e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  77 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTAL--FFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL--LAASQY 152
Cdd:PHA03095   85 TPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRN 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 153 GHMPVVETLLKHGANIH----------DQLYD-------------------------GATALFLAAQGGYLD--VIRLLL 195
Cdd:PHA03095  165 ANVELLRLLIDAGADVYavddrfrsllHHHLQsfkprarivreliragcdpaatdmlGNTPLHSMATGSSCKrsLVLPLL 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 196 SSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTL----GILK 271
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAetvaATLN 324

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907129472 272 NGTSALHAAVLSGN---VKTVALLLEAGADPA 300
Cdd:PHA03095  325 TASVAGGDIPSDATrlcVAKVVLRGAFSLLPE 356
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 153-305 3.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 153 GHMPVVETLLKHGAN-IHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRG 231
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129472 232 ADrdaarndgtTALLKAANKGyNDVIEELLKFSPTLGIlKNGTSA--LHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:PHA02874   92 VD---------TSILPIPCIE-KDMIKTILDCGIDVNI-KDAELKtfLHYAIKKGDLESIKMLFEYGADVNIEDDN 156
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 87-202 5.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  87 GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLFGFGA--STECR------------TKD--GGTALLA 148
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVdiNAKNRvnyllsygvpinIKDvyGFTPLHY 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907129472 149 ASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN 202
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-116 7.07e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907129472  74 KHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFA 116
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 187-305 8.32e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 187 YLDVIRLLLSSGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGADRDAARNDGTTALLKAAnkgYNDVIEEL 260
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907129472 261 LKFSPTLG--IL---KNGTSALHA--AVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:PHA03095  100 IKLLIKAGadVNakdKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLY 151
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-146 1.39e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907129472 100 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 146
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 144-299 1.73e-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: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 144 TALLAASQYGHMPVVETLLK-HGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAK-VNQPRQ----DGTAPLWIASQ 217
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 218 MGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDviEELLKFsptlgilkngtsalhaAVLSGNVKTVALLLEAGA 297
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNLIYYG--EHPLSF----------------AACVGNEEIVRLLIEHGA 160


                  ..
gi 1907129472 298 DP 299
Cdd:cd22192   161 DI 162
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 76-141 2.14e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129472  76 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKD 141
Cdd:PLN03192  622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 241-302 5.21e-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: 5.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907129472 241 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGADPALR 302
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-105 6.99e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 6.99e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907129472  75 HGTTLLMVASYAGHIDCVRELVLQGADINLQ 105
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02798 PHA02798
ankyrin-like protein; Provisional
 157-262 8.12e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 157 VVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLSSGAKVNQPRQDGTAPLWIA---SQMGHSEVVRVML 228
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMI 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907129472 229 LRGADRDAARNDGTTAL---LKAANKGYNDVIEELLK 262
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.03e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.03e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907129472  174 DGATALFLAAQGGYLDVIRLLLSSGAKVN 202
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 76-223 1.05e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  76 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGT------TALF--------FAAQQGHNDVVRFLFGFGASTECRTKD 141
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIyygehplsFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 142 GGTALlaasqygHMPVvetlLKHGANIHDQLYDgatalFLAAQGGYLDVIRLLLssgakvnQPRQDGTAPLWIASQMGHS 221
Cdd:cd22192   169 GNTVL-------HILV----LQPNKTFACQMYD-----LILSYDKEDDLQPLDL-------VPNNQGLTPFKLAAKEGNI 225


                  ..
gi 1907129472 222 EV 223
Cdd:cd22192   226 VM 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-304 1.19e-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: 38.81  E-value: 1.19e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907129472 272 NGTSALHAAVLS-GNVKTVALLLEAGADPALRNK 304
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 142-294 1.23e-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: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 142 GGTALLAASQYGH-------MPVVETLLKHG-------ANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVnQPRQD 207
Cdd:cd21882    26 GKTCLHKAALNLNdgvneaiMLLLEAAPDSGnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 208 GTA--------------PLWIASQMGHSEVVRVMLLRGAD------RDAARNDGTTALLKAANKG----------YNDVI 257
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907129472 258 EELLKFSPT--LGILKN--GTSALHAAVLSGNVKTVALLLE 294
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
PHA02798 PHA02798
ankyrin-like protein; Provisional
 89-203 1.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  89 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGT---ALLAASQYGHMPVVET 160
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129472 161 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLSSGAKVNQ 203
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-250 1.88e-04

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: 42.76  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 101 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH----------- 169
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 170 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 232
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1907129472 233 DRDAARNDGTTaLLKAAN 250
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
241-293 2.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907129472 241 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLL 293
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 75-104 2.28e-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: 37.95  E-value: 2.28e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907129472   75 HGTTLLMVASYAGHIDCVRELVLQGADINL 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-171 2.74e-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: 37.65  E-value: 2.74e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907129472 141 DGGTAL-LAASQYGHMPVVETLLKHGANIHDQ 171
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 157-292 3.52e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 157 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLSSGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGADRDA 236
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907129472 237 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNVKTVALL 292
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 241-298 4.73e-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: 4.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129472 241 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGAD 298
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 241-304 4.85e-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: 41.70  E-value: 4.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129472 241 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNVKTVALLLEAGADPALRNK 304
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAK 107
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 75-150 5.52e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  75 HGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL-------FGFGASTECRTKDGGTALL 147
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLsrhsqchFELGANAKPDSFTGKPPSL 193


                  ...
gi 1907129472 148 AAS 150
Cdd:PTZ00322  194 EDS 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
208-261 6.18e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907129472 208 GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELL 261
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 272-299 8.08e-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: 8.08e-04
                           10        20
                   ....*....|....*....|....*...
gi 1907129472  272 NGTSALHAAVLSGNVKTVALLLEAGADP 299
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 151-303 1.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 151 QYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 230
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129472 231 gaDRDAARNDGTTALLKAANKgyNDVIEELLKFSP-----TLGILKNgtSALHAAVLSGNV-KTVALLLEAGADPALRN 303
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAIRN--EDLETSLLLYDAgfsvnSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKN 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 75-105 1.90e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907129472  75 HGTTLLMVASY-AGHIDCVRELVLQGADINLQ 105
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-170 2.43e-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: 34.87  E-value: 2.43e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907129472  141 DGGTALLAASQYGHMPVVETLLKHGANIHD 170
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 123-263 2.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.34  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 123 DVVRFLF--GFGASTECRtkdGGTALLaasQYGHMPVVET-----LLKHGANI-HDQLYDGATALFLA----AQGGYLDV 190
Cdd:PHA02989   17 NALEFLLrtGFDVNEEYR---GNSILL---LYLKRKDVKIkivklLIDNGADVnYKGYIETPLCAVLRnreiTSNKIKKI 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129472 191 IRLLLSSGAKVNQPRQDGTAPLWI---ASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYN---DVIEELLKF 263
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPIVCfiyNSNINNCDMLRFLLSKGINVNDVKNSRGYNLLHMYLESFSvkkDVIKILLSF 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
273-305 3.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907129472 273 GTSALHAAVLSGNVKTVALLLEAGADPALRNKN 305
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-136 4.74e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 4.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907129472  76 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTE 136
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-169 7.77e-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: 33.38  E-value: 7.77e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907129472 141 DGGTALLAASQYGHMPVVETLLKHGANIH 169
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 77-169 9.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  77 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH---NDVVRFLFGFGASTECRTKDGGTALLAASQYG 153
Cdd:PHA02798   77 TILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSN 156

                          90
                  ....*....|....*....
gi 1907129472 154 H---MPVVETLLKHGANIH 169
Cdd:PHA02798  157 HhidIEIIKLLLEKGVDIN 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 221-304 9.64e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.55  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 221 SEVVRVMLLRGADRDAA-RNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGAD 298
Cdd:PHA02878  147 AEITKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPdKTNNSPLHHAVKHYNKPIVHILLENGAS 226


                  ....*.
gi 1907129472 299 PALRNK 304
Cdd:PHA02878  227 TDARDK 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-195 9.78e-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: 37.37  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472  67 DMCRMSFKHGTTLLMVASYAGHIDCVRELVLQGADINL-------QRESGTTALF-------FAAQQGHNDVVRFLFGFG 132
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDP 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129472 133 AStecrtkdggtaLLAASQYG----HMPVVET----------------LLKHGANIHDQL-------YDGATALFLAAQG 185
Cdd:TIGR00870 199 AD-----------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKE 267

                         170
                  ....*....|
gi 1907129472 186 GYLDVIRLLL 195
Cdd:TIGR00870 268 GRIVLFRLKL 277
 
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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