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Conserved domains on  [gi|2462582474|ref|XP_054180434|]
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POTE ankyrin domain family member D isoform X1 [Homo sapiens]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-368 1.82e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.60  E-value: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 134 HIRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 214 IQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582474 294 KKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 368
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-368 1.82e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.60  E-value: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 134 HIRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 214 IQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582474 294 KKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 368
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 2.09e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 177 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHgADRNIPDeYGNTALHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462582474 257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-349 7.99e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 7.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 200 NVLDNKKRTALIKAIQCQEDECVL---MLLEHGADRNIPDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKCGL 273
Cdd:PHA03095    5 ESVDIIMEAALYDYLLNASNVTVEevrRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 274 TPL-LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTalILAVCCGSASI----VNLLLEQNVDVSSQDLSGQTAREYAVSS 348
Cdd:PHA03095   85 TPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKS 162


                  .
gi 2462582474 349 H 349
Cdd:PHA03095  163 R 163
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 163-340 1.68e-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: 62.34  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 163 DTDMNKRDKEKRTALHLASANGNSEVVQLLLdrrcqlnvldnkkrtalikaiqcqedECVLMLLehgadrNIP---DEY- 238
Cdd:cd22192    41 SCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------EAAPELV------NEPmtsDLYq 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLtplllgvheqkqqvvkFLIKKKANLNVldrYGRTALILAVCCGSA 318
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLIY---YGEHPLSFAACVGNE 149

                         170       180
                  ....*....|....*....|..
gi 2462582474 319 SIVNLLLEQNVDVSSQDLSGQT 340
Cdd:cd22192   150 EIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 174-362 5.93e-09

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: 57.78  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 174 RTAL-HLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIP-------DEY--GNTAL 243
Cdd:TIGR00870  53 RSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLElandqytSEFtpGITAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 244 HYAIYNEDKLMAKALLLYGADIESKNKCgltplllgvheqkqqvVKFLIKKKANLNvldRYGRTALILAVCCGSASIVNL 323
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGASVPARACG----------------DFFVKSQGVDSF---YHGESPLNAAACLGSPSIVAL 193

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462582474 324 LLEQNVDVSSQDLSGQTAREYAVsshhhVICELLSDYKE 362
Cdd:TIGR00870 194 LSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 6.63e-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: 36.80  E-value: 6.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462582474  238 YGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-368 1.82e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.60  E-value: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 134 HIRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 214 IQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582474 294 KKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 368
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
135-374 2.44e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 2.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 135 IRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAI 214
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 215 QCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 295 KANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKISSENSN 374
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-341 4.84e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 4.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 143 LHRAAWWGkvpRKDLIVML--RDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDE 220
Cdd:COG0666    91 LHAAARNG---DLEIVKLLleAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 221 CVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNV 300
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462582474 301 LDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTA 341
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-357 3.92e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 3.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 157 LIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPD 236
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 237 EYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCG 316
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462582474 317 SASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-309 9.25e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 9.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 143 LHRAAWWGKVprkDLIVML--RDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDE 220
Cdd:COG0666   124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 221 CVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNV 300
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                  ....*....
gi 2462582474 301 LDRYGRTAL 309
Cdd:COG0666   281 ALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 2.09e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 177 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHgADRNIPDeYGNTALHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462582474 257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-349 7.99e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 7.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 200 NVLDNKKRTALIKAIQCQEDECVL---MLLEHGADRNIPDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKCGL 273
Cdd:PHA03095    5 ESVDIIMEAALYDYLLNASNVTVEevrRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 274 TPL-LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTalILAVCCGSASI----VNLLLEQNVDVSSQDLSGQTAREYAVSS 348
Cdd:PHA03095   85 TPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKS 162


                  .
gi 2462582474 349 H 349
Cdd:PHA03095  163 R 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-332 2.11e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.95  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 154 RKDLIVMLRDT--DMNKRDKEKRTALHLAS-----ANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQC--QEDECVLM 224
Cdd:PHA03100   47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 225 LLEHGADRNIPDEYGNTALH-YAIYNEDKL-MAKALLL----------------YGADIESKNKCGLTPLLLGVHEQKQQ 286
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462582474 287 VVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVS 332
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 218-334 3.40e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 88.78  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 218 EDECVLMLLEHGADRNIPDEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKA 296
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462582474 297 NLNVLDRYGRTALILAVC-CGSASIVNLLLEQNVDVSSQ 334
Cdd:PHA02878  226 STDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAK 264
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 155-370 4.13e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 155 KDLIVMLRDT--DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADR 232
Cdd:PHA02874  104 KDMIKTILDCgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 233 NIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKqQVVKFLIkKKANLNVLDRYGRTALILA 312
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHA 261

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 313 V---CcgSASIVNLLLEQNVDVSSQDLSGQTAREYAVS--SHHHVICELLSD---YKEKQMLKISS 370
Cdd:PHA02874  262 InppC--DIDIIDILLYHKADISIKDNKGENPIDTAFKyiNKDPVIKDIIANavlIKEADKLKDSD 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-335 2.29e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 243 LHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIkKKANLNVLDrYGRTALILAVCCGSASIVN 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462582474 323 LLLEQNVDVSSQD 335
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-346 5.63e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 5.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 158 IVMLrDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-----IKAIQCQEDECVLMLLEHGADR 232
Cdd:PHA03100   21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 233 NIPDEYGNTALHYAIYN--EDKLMAKALLLYGADIESKNKCGLTPL--LLGVHEQKQQVVKFLIKKKANLNVLDRygrta 308
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNR----- 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462582474 309 lilavccgsasiVNLLLEQNVDVSSQDLSGQTAREYAV 346
Cdd:PHA03100  175 ------------VNYLLSYGVPINIKDVYGFTPLHYAV 200
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-304 1.06e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 158 IVMLRDTDMNKRDKEKRTALHLASAN--GNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDEC-------------- 221
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdin 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 222 ----VLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:PHA03100  171 aknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                  ....*..
gi 2462582474 298 LNVLDRY 304
Cdd:PHA03100  251 IKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 2.53e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 143 LHRAAWWGKVprkDLIVML--RDTDMNKRDKEKRTALHLASANGNSEVVQLLLDrRCQLNVlDNKKRTALIKAIQCQEDE 220
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 2462582474 221 CVLMLLEHGADRNIPD 236
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-357 9.76e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 9.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 158 IVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQ---------------------- 215
Cdd:PHA02874   20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpi 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 216 -CQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02874  100 pCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582474 295 KANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVIcELL 357
Cdd:PHA02874  180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELL 241
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 165-360 2.40e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLD-----------------------------NKKRTALIKAIQ 215
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDLSLLKAIR 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 216 CQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNE--DKLMAKaLLLYGADIESKNKCGLTPL-LLGVHEQKQQVVKFLI 292
Cdd:PHA02876  250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462582474 293 KKKANLNVLDRYGRTALILAVCCG-SASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDY 360
Cdd:PHA02876  329 MLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-357 2.68e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKRTALHLASANGNS---EVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVL-MLLEHGADRNIPDEYGN 240
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 241 TALHyaIY----NEDKLMAKALLLYGADIESKNKCGLTPL--LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTAL----- 309
Cdd:PHA03095  119 TPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhlq 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 310 ------------ILAVCCGSA--------------------SIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:PHA03095  197 sfkprarivrelIRAGCDPAAtdmlgntplhsmatgssckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-328 1.05e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAIQCQEDECVL-MLLEHGADRNIPDEYGN 240
Cdd:PHA03095  144 DVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDMLGN 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 241 TALHY-AIYNEDK--LMAKaLLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGS 317
Cdd:PHA03095  224 TPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                         170
                  ....*....|.
gi 2462582474 318 ASIVNLLLEQN 328
Cdd:PHA03095  303 GRAVRAALAKN 313
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-346 1.63e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 185 NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGAD 264
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 265 IESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVcCGSASIVNLLLeQNVDVSSQDLSGQTAREY 344
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHH 260


                  ..
gi 2462582474 345 AV 346
Cdd:PHA02874  261 AI 262
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-353 6.94e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 6.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRT---ALIKAIQCqEDECVLMLLEHGADRNIPDEYG 239
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDDRF 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 240 NTALHY-AIY---NEDKLmaKALLLYGADIESKNKCGLTPL--LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAV 313
Cdd:PHA03095  188 RSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462582474 314 CCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVI 353
Cdd:PHA03095  266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
222-357 7.50e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 7.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 222 VLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVL 301
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 302 DRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 143-301 1.03e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 143 LHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECV 222
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 223 LMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIE--SKNKCgLTPLLLGVHEQKQQVVKFLIKKKANLNV 300
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyfGKNGC-VAALCYAIENNKIDIVRLFIKRGADCNI 230


                  .
gi 2462582474 301 L 301
Cdd:PHA02875  231 M 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-330 1.25e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 174 RTALHLASANGNSEVVQLLLDRRCQLN-VLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDK 252
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462582474 253 LMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGR-TALILAVCCGSASIVNLLLEQNVD 330
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 143-360 1.87e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.55  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 143 LHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANG-NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQED-E 220
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 221 CVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNK----------CGLTPLLlgvheqkqqVVKF 290
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQkigtalhfalCGTNPYM---------SVKT 427

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462582474 291 LIKKKANLNVLDRYGRTALILAvCCGSA--SIVNLLLEQNVDVSSQDLSGQTAREYAVSshHHVICELLSDY 360
Cdd:PHA02876  428 LIDRGANVNSKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 165-280 2.92e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEK-RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTAL 243
Cdd:PHA02878  159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462582474 244 HYA-----------------------------------IYNEDKLmaKALLLYGADIESKNKCGLTPLLLGV 280
Cdd:PHA02878  239 HISvgyckdydilklllehgvdvnaksyilgltalhssIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 180-343 5.53e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 5.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 180 ASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAIQCQEDeCVLMLLEHGADRNIPDEYGNTAL-------HYAIYNed 251
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLhIAASKGYED-CVLVLLKHACNVHIRDANGNTALwnaisakHHKIFR-- 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 252 klmakalLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDV 331
Cdd:PLN03192  609 -------ILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                         170
                  ....*....|....*.
gi 2462582474 332 SS----QDLSGQTARE 343
Cdd:PLN03192  682 DKantdDDFSPTELRE 697
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 156-298 3.67e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 156 DLIVMLRDTDMNkrDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDEcVLMLLEHGADRNIP 235
Cdd:PLN03192  543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYHFASISDP 619

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582474 236 DEYGNTaLHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANL 298
Cdd:PLN03192  620 HAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-367 5.22e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 287 VVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEqNVDVSSQDlSGQTAREYAVSSHHHVICELLSDYKEKQML 366
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINV 89


                  .
gi 2462582474 367 K 367
Cdd:pfam12796  90 K 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 177-331 1.38e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 177 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRN-IPDEYGNTALHYAIYNEDKLMA 255
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIM 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 256 KALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDV 331
Cdd:PHA02875  119 KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 163-340 1.68e-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: 62.34  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 163 DTDMNKRDKEKRTALHLASANGNSEVVQLLLdrrcqlnvldnkkrtalikaiqcqedECVLMLLehgadrNIP---DEY- 238
Cdd:cd22192    41 SCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------EAAPELV------NEPmtsDLYq 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLtplllgvheqkqqvvkFLIKKKANLNVldrYGRTALILAVCCGSA 318
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLIY---YGEHPLSFAACVGNE 149

                         170       180
                  ....*....|....*....|..
gi 2462582474 319 SIVNLLLEQNVDVSSQDLSGQT 340
Cdd:cd22192   150 EIVRLLIEHGADIRAQDSLGNT 171
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-359 6.79e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 6.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 174 RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGA--DRNIPDEygNTALHYAIYNED 251
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 252 KLMAKALLLYGADIESK-NKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVD 330
Cdd:PHA02875   81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180
                  ....*....|....*....|....*....
gi 2462582474 331 VSSQDLSGQTAREYAVSSHHHVICELLSD 359
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 174-362 5.93e-09

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: 57.78  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 174 RTAL-HLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIP-------DEY--GNTAL 243
Cdd:TIGR00870  53 RSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLElandqytSEFtpGITAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 244 HYAIYNEDKLMAKALLLYGADIESKNKCgltplllgvheqkqqvVKFLIKKKANLNvldRYGRTALILAVCCGSASIVNL 323
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGASVPARACG----------------DFFVKSQGVDSF---YHGESPLNAAACLGSPSIVAL 193

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462582474 324 LLEQNVDVSSQDLSGQTAREYAVsshhhVICELLSDYKE 362
Cdd:TIGR00870 194 LSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 217-340 9.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 9.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 217 QEDECVL--MLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02876  154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 295 KANL-----------------------------NVLDRYGRTALILAVCCGSAS-IVNLLLEQNVDVSSQDLSGQT 340
Cdd:PHA02876  234 RSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 1.58e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 1.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 192 LLDRR-CQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-303 2.64e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLM--LLEHGADRNIPDEYGN 240
Cdd:PHA03095  179 DVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462582474 241 TALHYA-IYNEDKLMAKaLLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDR 303
Cdd:PHA03095  259 TPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 1.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462582474 207 RTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALL 259
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 157-330 2.18e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.53  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 157 LIVMLRDTDMNKRDKEKRTALHLASANG---NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQ--CQED-ECVLMLLEHGA 230
Cdd:PHA02798   93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 231 DRN-IPDEYGNTALH-YAIYN---------------------EDKLMAKALLLY---------------------GADIE 266
Cdd:PHA02798  173 DINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462582474 267 SKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVD 330
Cdd:PHA02798  253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-295 2.21e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 175 TALHLASANGNSEVVQLLLDRRCQLN------VLDNKKRTALI---------KAIQCQEdECVLMLLEHGADRNIPDEYG 239
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIyygehplsfAACVGNE-EIVRLLIEHGADIRAQDSLG 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 240 NTALHYAIYNEDKLMAKAL--LLYGADIES--------KNKCGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd22192   170 NTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-276 2.79e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 2.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462582474 225 LLEHG-ADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPL 276
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
165-213 3.40e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 3.40e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462582474 165 DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
296-345 9.61e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 9.61e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462582474 296 ANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYA 345
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-378 1.02e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.02e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462582474 309 LILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQM-------LKISSENSNPENV 378
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLkdngrtaLHYAARSGHLEIV 77
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-292 2.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462582474 239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLI 292
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-193 2.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 2.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462582474 143 LHRAAWWGKVprkDLIVMLRDT--DMNKRDKEKRTALHLASANGNSEVVQLLL 193
Cdd:pfam13637   5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 207-340 3.28e-06

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: 49.11  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 207 RTALIKAI---QCQEDECVLMLLEHGADRNIP---------DEY--GNTALHYAIYNEDKLMAKALLLYGADIESKnKCG 272
Cdd:cd21882    27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALHIAIENRNLNLVRLLVENGADVSAR-ATG 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462582474 273 ltplllgvheqkqqvvKFLIKKKANLNVldrYGRTALILAVCCGSASIVNLLLE---QNVDVSSQDLSGQT 340
Cdd:cd21882   106 ----------------RFFRKSPGNLFY---FGELPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 243-361 3.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 243 LHYAI--YNEDKLmaKALLLYGADIESKNKCGLTPLLLGVHEQKQQ-----VVKFLIKKKANLNVLDRYGRTALILAVCC 315
Cdd:PHA03100   39 LYLAKeaRNIDVV--KILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462582474 316 --GSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHV--ICELLSDYK 361
Cdd:PHA03100  117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKG 166
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-325 3.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 3.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462582474 272 GLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLL 325
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 172-295 4.74e-06

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: 48.72  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 172 EKRTALHLASANGNSEVVQLLLDRRCQLNVLDNK---KRTA----------LIKAIQCQEDECVLMLLEHGAD-RNIP-- 235
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffRKSPgnlfyfgelpLSLAACTNQEEIVRLLLENGAQpAALEaq 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 236 DEYGNTALHYAIYNEDKL---------MAKALLLYGADI-------ESKNKCGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd21882   152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
PHA02946 PHA02946
ankyin-like protein; Provisional
 185-354 1.05e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 185 NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLL--YG 262
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 263 ADI-ESKNKCGLTPlLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGS--ASIVNLLLEQNVDVSSQDLSGQ 339
Cdd:PHA02946  131 AKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGN 209

                         170
                  ....*....|....*
gi 2462582474 340 TAReyavsshhHVIC 354
Cdd:PHA02946  210 TPL--------HIVC 216
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 207-340 1.07e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.48  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 207 RTALIKA---IQCQEDECVLMLLEHGADRNIPDEY-----------GNTALHYAIYNEDKLMAKALLLYGADIESKnKCG 272
Cdd:cd22193    30 KTCLMKAllnLNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAH-AKG 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462582474 273 ltplllgvheqkqqvvKFLIKKKANLNVLdrYGRTALILAVCCGSASIVNLLLE---QNVDVSSQDLSGQT 340
Cdd:cd22193   109 ----------------RFFQPKYQGEGFY--FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 224-293 4.47e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 4.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 224 MLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 6.72e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 6.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462582474 238 YGNTALHYAIYNEDKL-MAKALLLYGADIESKNK 270
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 164-384 7.47e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 164 TDMNKRDKEKRtaLHLASANGNSEVVQLL-----LDRRC-----------QLNVLDNKKrTALIKA---IQCQEDECVLM 224
Cdd:cd22194    39 AKEEQRDKKKR--LKKVSEAAVEELGELLkelkdLSRRRrktdvpdflmhKLTASDTGK-TCLMKAllnINENTKEIVRI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 225 LLEHGADRNIPD-----EY------GNTALHYAIYNEDKLMAKALLLYGADIESKNKcgltplllGVHEQ-KQQVVKFLi 292
Cdd:cd22194   116 LLAFAEENGILDrfinaEYteeayeGQTALNIAIERRQGDIVKLLIAKGADVNAHAK--------GVFFNpKYKHEGFY- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 293 kkkanlnvldrYGRTALILAVCCGSASIVNLLLEQ-NVDVSSQDLSGQTAReyavsshhHVICELLSDYKE-----KQML 366
Cdd:cd22194   187 -----------FGETPLALAACTNQPEIVQLLMEKeSTDITSQDSRGNTVL--------HALVTVAEDSKTqndfvKRMY 247

                         250
                  ....*....|....*...
gi 2462582474 367 KISSENSNPENVSRTRNK 384
Cdd:cd22194   248 DMILLKSENKNLETIRNN 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-238 7.61e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEH------GADRNIPDEY 238
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfeLGANAKPDSF 186
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 280-350 1.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 1.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462582474 280 VHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHH 350
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 288-360 1.73e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582474 288 VKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDY 360
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 251-338 3.35e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 251 DKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVD 330
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                  ....*...
gi 2462582474 331 VSSQDLSG 338
Cdd:PTZ00322  174 HFELGANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-204 5.34e-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: 37.27  E-value: 5.34e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462582474 174 RTALHLASA-NGNSEVVQLLLDRRCQLNVLDN 204
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 6.63e-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: 36.80  E-value: 6.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462582474  238 YGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 155-247 6.66e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 155 KDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKkrTALIKAIQCQEDECVLMLLEHGADRNI 234
Cdd:PHA02791   12 KQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQ 89

                          90
                  ....*....|...
gi 2462582474 235 PDEYGNTALHYAI 247
Cdd:PHA02791   90 FDDKGNTALYYAV 102
PHA02798 PHA02798
ankyrin-like protein; Provisional
 178-309 7.14e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 178 HLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQED-----ECVLMLLEHGADRNIPDEYGNTALhYAIYNEDK 252
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPL-YCLLSNGY 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582474 253 LMAKALLLY----GADIESKNKCGLTPLLLGV---HEQKQQVVKFLIKKKANLNVL-DRYGRTAL 309
Cdd:PHA02798  122 INNLEILLFmienGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDINTHnNKEKYDTL 186
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-265 7.19e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 7.19e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462582474 238 YGNTALHYAIYNEDKLMAKALLLYGADI 265
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 165-340 9.13e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 165 DMNKRDKEKrtaLHLASANGNSEVVQLLLD--RRCQLNVLDNK------KRTALIKAIQCQED---ECVLMLLEHGADRN 233
Cdd:cd22197     1 DPNRFDRDR---LFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAVLNLQDgvnACIMPLLEIDKDSG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 234 IP---------DEY--GNTALHYAIYNEDKLMAKALLLYGADIESKNKcgltplllGVHEQKQQVVKFLikkkanlnvld 302
Cdd:cd22197    78 NPkplvnaqctDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARAC--------GRFFQKKQGTCFY----------- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462582474 303 rYGRTALILAVCCGSASIVNLLLEQNVDVSS---QDLSGQT 340
Cdd:cd22197   139 -FGELPLSLAACTKQWDVVNYLLENPHQPASlqaQDSLGNT 178
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 291-357 9.46e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 9.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462582474 291 LIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-201 2.31e-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: 35.31  E-value: 2.31e-03
                          10        20
                  ....*....|....*....|....*...
gi 2462582474 174 RTALHLASANGNSEVVQLLLDRRCQLNV 201
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 2.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 2.52e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462582474  172 EKRTALHLASANGNSEVVQLLLDRRCQLNV 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 304-335 3.33e-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: 34.96  E-value: 3.33e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462582474 304 YGRTALILAVC-CGSASIVNLLLEQNVDVSSQD 335
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 222-276 4.05e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.12  E-value: 4.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462582474 222 VLMLLEHGADRNIPDEYGNTALHY-------------AIYNEDKL-MAKALLLYGADIESKNKCGLTPL 276
Cdd:PHA02716  335 IKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildpETDNDIRLdVIQCLISLGADITAVNCLGYTPL 403
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 188-278 4.95e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 188 VVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGN-TALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:PHA02884   52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADIN 131

                          90
                  ....*....|..
gi 2462582474 267 SKNKCGLTPLLL 278
Cdd:PHA02884  132 IQTNDMVTPIEL 143
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 188-337 7.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582474 188 VVQLLLDrrCQLnVLDNKKRTALIKAIQCQEdECVLMLLEHGADRNIPDEYGNTALHYA------IYNEDKLMAKALLLY 261
Cdd:PHA02876   92 VISLTLD--CDI-ILDIKYASIILNKHKLDE-ACIHILKEAISGNDIHYDKINESIEYMklikerIQQDELLIAEMLLEG 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582474 262 GADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLS 337
Cdd:PHA02876  168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS 243
 
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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