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Conserved domains on  [gi|1034589512|ref|XP_016877347|]
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POTE ankyrin domain family member B isoform X3 [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];
100-331 4.42e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 4.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 100 REDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQC 179
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 180 QEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKA 259
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034589512 260 NLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 331
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-331 4.42e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 4.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 100 REDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQC 179
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 180 QEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKA 259
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034589512 260 NLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 331
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-232 8.86e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 140 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHgADGNIQDeYGNTALHYAIYNEDKLMAK 219
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1034589512 220 ALLLYGADIESKN 232
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 185-312 1.16e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 185 VLMLLEHGADGNIQDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKCGLTPL-LLGVHEQKQEVVKFLIKKKAN 260
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 261 LNALDRYGRTalILAVCCGSASI----VNLLLEQNVDVSSQDLSGQTAREYAVSSH 312
Cdd:PHA03095  110 VNAKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 161-325 9.50e-11

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: 62.79  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 161 QLNVLDNKKRTALIKAVQCQE-DECVLMLLEHGADGNIqdeyGNTALHyAIYNEDKLMAKALLLYGADIESKNKC----- 234
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelan 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 235 ---------GLTPLLLGVHEQKQEVVKFLIKKKANLNA--------------LDRYGRTALILAVCCGSASIVNLLLEQN 291
Cdd:TIGR00870 119 dqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDP 198

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034589512 292 VDVSSQDLSGQTAREYAVsshhhVICELLSDYKE 325
Cdd:TIGR00870 199 ADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 126-303 1.62e-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: 61.95  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 126 DTDMNKRDKQKRTALHLASANGNSEVVQLLLDrrcQLNVLDNKKRTAlikavqcqedecvlmllehgadgniqDEY-GNT 204
Cdd:cd22192    41 SCDLFQRGALGETALHVAALYDNLEAAVVLME---AAPELVNEPMTS--------------------------DLYqGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 205 ALHYAIYNEDKLMAKALLLYGADIESKNKCGLtplllgvheqkqevvkFLIKKKANLNaldRYGRTALILAVCCGSASIV 284
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAACVGNEEIV 152

                         170
                  ....*....|....*....
gi 1034589512 285 NLLLEQNVDVSSQDLSGQT 303
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNT 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-229 5.87e-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: 5.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 1034589512  201 YGNTALHYAIYNEDKLMAKALLLYGADIE 229
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-331 4.42e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 4.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 100 REDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQC 179
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 180 QEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKA 259
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034589512 260 NLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 331
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-337 3.82e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.98  E-value: 3.82e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 102 DLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQE 181
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 182 DECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANL 261
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 262 NALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKISSENSN 337
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-304 1.69e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 106 LHRAAWWGkvpRKDLIVML--RDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDE 183
Cdd:COG0666    91 LHAAARNG---DLEIVKLLleAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 184 CVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNA 263
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034589512 264 LDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTA 304
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
120-320 6.34e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 6.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 120 LIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQD 199
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 200 EYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCG 279
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034589512 280 SASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 320
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-272 4.26e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 4.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 106 LHRAAWWGKVprkDLIVML--RDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDE 183
Cdd:COG0666   124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 184 CVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNA 263
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                  ....*....
gi 1034589512 264 LDRYGRTAL 272
Cdd:COG0666   281 ALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-232 8.86e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 140 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHgADGNIQDeYGNTALHYAIYNEDKLMAK 219
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1034589512 220 ALLLYGADIESKN 232
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 185-312 1.16e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 185 VLMLLEHGADGNIQDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKCGLTPL-LLGVHEQKQEVVKFLIKKKAN 260
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 261 LNALDRYGRTalILAVCCGSASI----VNLLLEQNVDVSSQDLSGQTAREYAVSSH 312
Cdd:PHA03095  110 VNAKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 117-295 1.78e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.65  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 117 RKDLIVMLRDT--DMNKRDKQKRTALHLAS-----ANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQC--QEDECVLM 187
Cdd:PHA03100   47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 188 LLEHGADGNIQDEYGNTALH-YAIYNEDKL-MAKALLL----------------YGADIESKNKCGLTPLLLGVHEQKQE 249
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034589512 250 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVS 295
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 181-297 3.58e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 91.09  E-value: 3.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 181 EDECVLMLLEHGADGNIQDEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKA 259
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034589512 260 NLNALDRYGRTALILAVC-CGSASIVNLLLEQNVDVSSQ 297
Cdd:PHA02878  226 STDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAK 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 121-309 1.68e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.57  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 121 IVMLrDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-----IKAVQCQEDECVLMLLEHGADG 195
Cdd:PHA03100   21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 196 NIQDEYGNTALHYAIYN--EDKLMAKALLLYGADIESKNKCGLTPL--LLGVHEQKQEVVKFLIKKKANLNALDRygrta 271
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNR----- 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034589512 272 lilavccgsasiVNLLLEQNVDVSSQDLSGQTAREYAV 309
Cdd:PHA03100  175 ------------VNYLLSYGVPINIKDVYGFTPLHYAV 200
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-314 2.16e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.54  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 150 EVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDEC---VLMLLEHGADGNIQDEYGNTALHYAIYNEDKL-MAKALLLYG 225
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 226 ADIESKNKCGLTPL--LLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASI--VNLLLEQNVDVSSQDLSG 301
Cdd:PHA03095  108 ADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRF 187

                         170
                  ....*....|...
gi 1034589512 302 QTAReyavssHHH 314
Cdd:PHA03095  188 RSLL------HHH 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 118-333 1.05e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 118 KDLIVMLRDT--DMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADG 195
Cdd:PHA02874  104 KDMIKTILDCgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 196 NIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQeVVKFLIkKKANLNALDRYGRTALILA 275
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI-NNASINDQDIDGSTPLHHA 261

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 276 V---CcgSASIVNLLLEQNVDVSSQDLSGQTAREYAVS--SHHHVICELLSD---YKEKQMLKISS 333
Cdd:PHA02874  262 InppC--DIDIIDILLYHKADISIKDNKGENPIDTAFKyiNKDPVIKDIIANavlIKEADKLKDSD 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-298 1.41e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 206 LHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIkKKANLNALDrYGRTALILAVCCGSASIVN 285
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1034589512 286 LLLEQNVDVSSQD 298
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 121-267 1.69e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 121 IVMLRDTDMNKRDKQKRTALHLASAN--GNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDEC-------------- 184
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdin 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 185 ----VLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKAN 260
Cdd:PHA03100  171 aknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                  ....*..
gi 1034589512 261 LNALDRY 267
Cdd:PHA03100  251 IKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 128-320 4.28e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 4.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 128 DMNKRDKQKRTALHLASANGNS---EVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVL-MLLEHGADGNIQDEYGN 203
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 204 TALHyaIY----NEDKLMAKALLLYGADIESKNKCGLTPL--LLGVHEQKQEVVKFLIKKKANLNALDRYGRTAL----- 272
Cdd:PHA03095  119 TPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhlq 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 273 ------------ILAVCCGSA--------------------SIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 320
Cdd:PHA03095  197 sfkprarivrelIRAGCDPAAtdmlgntplhsmatgssckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-199 1.41e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 106 LHRAAWWGKVprkDLIVML--RDTDMNKRDKQKRTALHLASANGNSEVVQLLLDrRCQLNVlDNKKRTALIKAVQCQEDE 183
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1034589512 184 CVLMLLEHGADGNIQD 199
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 128-323 2.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.11  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 128 DMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLD-----------------------------NKKRTALIKAVQ 178
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDLSLLKAIR 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 179 CQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNE--DKLMAKaLLLYGADIESKNKCGLTPL-LLGVHEQKQEVVKFLI 255
Cdd:PHA02876  250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034589512 256 KKKANLNALDRYGRTALILAVCCG-SASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDY 323
Cdd:PHA02876  329 MLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 138-320 2.80e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 138 TALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQ-----------------------CQEDECVLMLLEHGAD 194
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpipCIEKDMIKTILDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 195 GNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALIL 274
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034589512 275 AVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVIcELL 320
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELL 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 128-291 8.25e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 8.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 128 DMNKRDKQKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAVQCQEDECVL-MLLEHGADGNIQDEYGN 203
Cdd:PHA03095  144 DVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDMLGN 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 204 TALHY-AIYNEDK--LMAKaLLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGS 280
Cdd:PHA03095  224 TPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                         170
                  ....*....|.
gi 1034589512 281 ASIVNLLLEQN 291
Cdd:PHA03095  303 GRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
 128-316 3.09e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 128 DMNKRDKQKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRT---ALIKAVQCqEDECVLMLLEHGADGNIQDEYG 202
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDDRF 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 203 NTALHY-AIY---NEDKLmaKALLLYGADIESKNKCGLTPL--LLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAV 276
Cdd:PHA03095  188 RSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034589512 277 CCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVI 316
Cdd:PHA03095  266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 106-323 1.64e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.25  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 106 LHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANG-NSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQED-E 183
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 184 CVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNK----------CGLTPLLlgvheqkqeVVKF 253
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQkigtalhfalCGTNPYM---------SVKT 427

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034589512 254 LIKKKANLNALDRYGRTALILAvCCGSA--SIVNLLLEQNVDVSSQDLSGQTAREYAVSshHHVICELLSDY 323
Cdd:PHA02876  428 LIDRGANVNSKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 148-309 1.87e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 148 NSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGAD 227
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 228 IESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVcCGSASIVNLLLeQNVDVSSQDLSGQTAREY 307
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHH 260


                  ..
gi 1034589512 308 AV 309
Cdd:PHA02874  261 AI 262
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 143-306 2.29e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 143 ASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAVQCQEDeCVLMLLEHGADGNIQDEYGNTAL-------HYAIYNed 214
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLhIAASKGYED-CVLVLLKHACNVHIRDANGNTALwnaisakHHKIFR-- 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 215 klmakalLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDV 294
Cdd:PLN03192  609 -------ILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                         170
                  ....*....|....*.
gi 1034589512 295 SS----QDLSGQTARE 306
Cdd:PLN03192  682 DKantdDDFSPTELRE 697
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 106-262 2.86e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 106 LHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECV 185
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034589512 186 LMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIE--SKNKCgLTPLLLGVHEQKQEVVKFLIKKKANLN 262
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyfGKNGC-VAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 128-243 6.83e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 128 DMNKRDKQK-RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTAL 206
Cdd:PHA02878  159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034589512 207 HYA-----------------------------------IYNEDKLmaKALLLYGADIESKNKCGLTPLLLGV 243
Cdd:PHA02878  239 HISvgyckdydilklllehgvdvnaksyilgltalhssIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
185-320 9.31e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 9.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 185 VLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNAL 264
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 265 DRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 320
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 137-293 2.05e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.71  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 137 RTALHLASANGNSEVVQLLLDRRCQLN-VLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDK 215
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034589512 216 LMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGR-TALILAVCCGSASIVNLLLEQNVD 293
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 119-267 2.31e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 119 DLIVMLRDTDMNkrDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDEcVLMLLEHGAdgNIQ 198
Cdd:PLN03192  543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYHFA--SIS 617

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 199 DEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRY 267
Cdd:PLN03192  618 DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
249-330 5.25e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 5.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 249 EVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEqNVDVSSQDlSGQTAREYAVSSHHHVICELLSDYKEKQM 328
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88


                  ..
gi 1034589512 329 LK 330
Cdd:pfam12796  89 VK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 138-294 8.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 138 TALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGN-IQDEYGNTALHYAIYNEDKL 216
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589512 217 MAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDV 294
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 161-325 9.50e-11

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: 62.79  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 161 QLNVLDNKKRTALIKAVQCQE-DECVLMLLEHGADGNIqdeyGNTALHyAIYNEDKLMAKALLLYGADIESKNKC----- 234
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelan 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 235 ---------GLTPLLLGVHEQKQEVVKFLIKKKANLNA--------------LDRYGRTALILAVCCGSASIVNLLLEQN 291
Cdd:TIGR00870 119 dqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDP 198

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034589512 292 VDVSSQDLSGQTAREYAVsshhhVICELLSDYKE 325
Cdd:TIGR00870 199 ADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 126-303 1.62e-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: 61.95  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 126 DTDMNKRDKQKRTALHLASANGNSEVVQLLLDrrcQLNVLDNKKRTAlikavqcqedecvlmllehgadgniqDEY-GNT 204
Cdd:cd22192    41 SCDLFQRGALGETALHVAALYDNLEAAVVLME---AAPELVNEPMTS--------------------------DLYqGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 205 ALHYAIYNEDKLMAKALLLYGADIESKNKCGLtplllgvheqkqevvkFLIKKKANLNaldRYGRTALILAVCCGSASIV 284
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAACVGNEEIV 152

                         170
                  ....*....|....*....
gi 1034589512 285 NLLLEQNVDVSSQDLSGQT 303
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNT 171
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 137-322 3.28e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 137 RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKL 216
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 217 MAKALLLYGADIESK-NKCGLTPLLLGVHEQKQEVVKFLIKKKA--NLNALDRYgrTALILAVCCGSASIVNLLLEQNVD 293
Cdd:PHA02875   83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180
                  ....*....|....*....|....*....
gi 1034589512 294 VSSQDLSGQTAREYAVSSHHHVICELLSD 322
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 180-303 1.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 180 QEDECVL--MLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKK 257
Cdd:PHA02876  154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 258 KANL-----------------------------NALDRYGRTALILAVCCGSAS-IVNLLLEQNVDVSSQDLSGQT 303
Cdd:PHA02876  234 RSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 135-258 5.25e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.33  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 135 QKRTALHLASANGNSEVVQLLLDRRCQLN------VLDNKKRTALIK--------AVQCQEDECVLMLLEHGADGNIQDE 200
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDS 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589512 201 YGNTALHYAIYNEDKLMAKAL--LLYGADIES--------KNKCGLTPLLLGVHEQKQEVVKFLIKKK 258
Cdd:cd22192   168 LGNTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
154-209 2.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 2.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 154 LLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYA 209
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
170-222 2.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 2.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034589512 170 RTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALL 222
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 128-266 3.15e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 128 DMNKRDKQKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLM--LLEHGADGNIQDEYGN 203
Cdd:PHA03095  179 DVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034589512 204 TALHYA-IYNEDKLMAKaLLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDR 266
Cdd:PHA03095  259 TPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 188-324 1.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 188 LLEHGADGNIQDEYGNTALHYAI--YNEDKLmaKALLLYGADIESKNKCGLTPLLLGVHEQK-----QEVVKFLIKKKAN 260
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKeaRNIDVV--KILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGAN 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589512 261 LNALDRYGRTALILAVCC--GSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHV--ICELLSDYK 324
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKG 166
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 135-258 1.22e-07

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 53.35  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 135 QKRTALHLASANGNSEVVQLLLDRRCQLNVLDNK---KRTA----------LIKAVQCQEDECVLMLLEHGAD---GNIQ 198
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffRKSPgnlfyfgelpLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589512 199 DEYGNTALHYAIYNEDKL---------MAKALLLYGADI-------ESKNKCGLTPLLLGVHEQKQEVVKFLIKKK 258
Cdd:cd21882   152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
PHA02798 PHA02798
ankyrin-like protein; Provisional
 120-293 1.68e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.53  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 120 LIVMLRDTDMNKRDKQKRTALHLASANG---NSEVVQLLLDRRCQLNVLDNKKRTALIKAVQ--CQED-ECVLMLLEHGA 193
Cdd:PHA02798   93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 194 DGN-IQDEYGNTALH-YAIYN---------------------EDKLMAKALLLY---------------------GADIE 229
Cdd:PHA02798  173 DINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034589512 230 SKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVD 293
Cdd:PHA02798  253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
Ank_5 pfam13857
Ankyrin repeats (many copies);
188-239 1.82e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034589512 188 LLEHG-ADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPL 239
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
259-308 7.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 7.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034589512 259 ANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYA 308
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
235-288 8.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 8.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034589512 235 GLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLL 288
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
128-176 1.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.01e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034589512 128 DMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 176
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
202-255 1.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034589512 202 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLI 255
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
272-328 2.71e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 2.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034589512 272 LILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQM 328
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL 57
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-156 2.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 2.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034589512 106 LHRAAWWGKVprkDLIVMLRDT--DMNKRDKQKRTALHLASANGNSEVVQLLL 156
Cdd:pfam13637   5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 187-256 5.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 5.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 187 MLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIK 256
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 170-303 8.01e-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: 47.57  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 170 RTALIKAV---QCQEDECVLMLLEHGADGNIQ---------DEY--GNTALHYAIYNEDKLMAKALLLYGADIESKnKCG 235
Cdd:cd21882    27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALHIAIENRNLNLVRLLVENGADVSAR-ATG 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034589512 236 ltplllgvheqkqevvKFLIKKKANLNaldRYGRTALILAVCCGSASIVNLLLE---QNVDVSSQDLSGQT 303
Cdd:cd21882   106 ----------------RFFRKSPGNLF---YFGELPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 138-258 1.41e-05

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: 46.61  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 138 TALHLASANGNSEVVQLLLDR------RCQLNVLDNKKRTAL-------IKAVQC--QEDeCVLMLLEHGADGNIQDEYG 202
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSfyhgespLNAAAClgSPS-IVALLSEDPADILTADSLG 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034589512 203 NTALHYAIYNED------KL---MAKALLLYGADIESK-------NKCGLTPLLLGVHEQKQEVVKFLIKKK 258
Cdd:TIGR00870 209 NTLLHLLVMENEfkaeyeELscqMYNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
PHA02946 PHA02946
ankyin-like protein; Provisional
 148-317 2.92e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 148 NSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLL--YG 225
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 226 ADI-ESKNKCGLTPlLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGS--ASIVNLLLEQNVDVSSQDLSGQ 302
Cdd:PHA02946  131 AKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGN 209

                         170
                  ....*....|....*
gi 1034589512 303 TAReyavsshhHVIC 317
Cdd:PHA02946  210 TPL--------HIVC 216
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 243-313 4.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 4.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034589512 243 VHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHH 313
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 251-323 8.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 8.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034589512 251 VKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDY 323
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 201-233 8.64e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 8.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034589512 201 YGNTALHYAIYNEDKL-MAKALLLYGADIESKNK 233
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 128-191 1.04e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034589512 128 DMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEH 191
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 170-303 1.14e-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: 44.02  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 170 RTALIKAV---QCQEDECVLMLLEHGADGNIQDEY-----------GNTALHYAIYNEDKLMAKALLLYGADIESKnKCG 235
Cdd:cd22193    30 KTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAH-AKG 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034589512 236 ltplllgvheqkqevvKFLIKKKANLNALdrYGRTALILAVCCGSASIVNLLLE---QNVDVSSQDLSGQT 303
Cdd:cd22193   109 ----------------RFFQPKYQGEGFY--FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
PHA02798 PHA02798
ankyrin-like protein; Provisional
 141-262 1.61e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 141 HLASANGNSEVVQLLLDRRCQLNVLDNKKRTAL------IKAVQCQEDeCVLMLLEHGADGNIQDEYGNTALhYAIYNED 214
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsnIKDYKHMLD-IVKILIENGADINKKNSDGETPL-YCLLSNG 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034589512 215 KLMAKALLLY----GADIESKNKCGLTPLLLGV---HEQKQEVVKFLIKKKANLN 262
Cdd:PHA02798  121 YINNLEILLFmienGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDIN 175
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 223-303 1.92e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 223 LYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDR--------------YGRTALILAVCCGSASIVNLLL 288
Cdd:cd22194   129 FINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLM 208

                          90
                  ....*....|....*.
gi 1034589512 289 EQ-NVDVSSQDLSGQT 303
Cdd:cd22194   209 EKeSTDITSQDSRGNT 224
PHA02791 PHA02791
ankyrin-like protein; Provisional
 118-210 2.94e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 118 KDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKkrTALIKAVQCQEDECVLMLLEHGADGNI 197
Cdd:PHA02791   12 KQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQ 89

                          90
                  ....*....|...
gi 1034589512 198 QDEYGNTALHYAI 210
Cdd:PHA02791   90 FDDKGNTALYYAV 102
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 214-301 4.50e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 214 DKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVD 293
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                  ....*...
gi 1034589512 294 VSSQDLSG 301
Cdd:PTZ00322  174 HFELGANA 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-229 5.87e-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: 5.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 1034589512  201 YGNTALHYAIYNEDKLMAKALLLYGADIE 229
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 201-228 6.88e-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: 6.88e-04
                          10        20
                  ....*....|....*....|....*...
gi 1034589512 201 YGNTALHYAIYNEDKLMAKALLLYGADI 228
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-167 6.93e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 6.93e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1034589512 137 RTALHLASA-NGNSEVVQLLLDRRCQLNVLDN 167
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 137-272 9.59e-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: 40.99  E-value: 9.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 137 RTALHLASANGNSEVVQLLLD--RRCQLNVLDNK------KRTALIKAVQCQED---ECVLMLLEHGAD-GNIQ------ 198
Cdd:cd22197     7 RDRLFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAVLNLQDgvnACIMPLLEIDKDsGNPKplvnaq 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 199 --DEY--GNTALHYAIYNEDKLMAKALLLYGADIES--------KNK--C---GLTPLLLGVHEQKQEVVKFLIKKK--- 258
Cdd:cd22197    87 ctDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqKKQgtCfyfGELPLSLAACTKQWDVVNYLLENPhqp 166

                         170
                  ....*....|....
gi 1034589512 259 ANLNALDRYGRTAL 272
Cdd:cd22197   167 ASLQAQDSLGNTVL 180
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 106-197 1.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 106 LHRAAWWGKVPRKDLIVMLRDTdMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLN-VLDNKKRTALIKAVQCQEDEC 184
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDI 217

                          90
                  ....*....|...
gi 1034589512 185 VLMLLEHGADGNI 197
Cdd:PHA02875  218 VRLFIKRGADCNI 230
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-164 2.15e-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: 2.15e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034589512 137 RTALHLASANGNSEVVQLLLDRRCQLNV 164
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 135-164 2.17e-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: 2.17e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034589512  135 QKRTALHLASANGNSEVVQLLLDRRCQLNV 164
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 196-324 2.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 196 NIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIkkkanLNALDrygrtALILA 275
Cdd:PHA02874   29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNGVD-----TSILP 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034589512 276 VCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYK 324
Cdd:PHA02874   99 IPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG 147
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 151-241 3.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.81  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 151 VVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGN-TALHYAIYNEDKLMAKALLLYGADIE 229
Cdd:PHA02884   52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADIN 131

                          90
                  ....*....|..
gi 1034589512 230 SKNKCGLTPLLL 241
Cdd:PHA02884  132 IQTNDMVTPIEL 143
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 254-320 3.45e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.08  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034589512 254 LIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 320
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 267-298 4.20e-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: 34.57  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034589512 267 YGRTALILAVC-CGSASIVNLLLEQNVDVSSQD 298
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 137-262 4.73e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.59  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 137 RTALHLASANGNSEVVQLLLDRRCQLN-----VLDNKK---------RTALIKAVQCQEDECVLMLLEHGAD-GNIQDEY 201
Cdd:cd22194   142 QTALNIAIERRQGDIVKLLIAKGADVNahakgVFFNPKykhegfyfgETPLALAACTNQPEIVQLLMEKESTdITSQDSR 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034589512 202 GNTALHYAIYNED---------KLMAKALLLY--GADIES-KNKCGLTPLLLGVHEQKQEVVKFL----IKKKANLN 262
Cdd:cd22194   222 GNTVLHALVTVAEdsktqndfvKRMYDMILLKseNKNLETiRNNEGLTPLQLAAKMGKAEILKYIlsreIKEKPNRS 298
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 146-238 5.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 146 NGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAVQCQED-ECVLMLLEHGADGNIQDEYGNTALH-YAIYNEDKLMAKALL 222
Cdd:PHA02859  100 NVEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNVRiNVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLT 179

                          90
                  ....*....|....*.
gi 1034589512 223 LYGADIESKNKCGLTP 238
Cdd:PHA02859  180 SLGIDINETNKSGYNC 195
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 133-300 5.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 133 DKQKRTALHLASANGNSEVVQLLLDRRCQLnVLDNKKRTALIKAVQCqeDECVLMLLEHGADGN-IQDEYGNTALHYA-- 209
Cdd:PHA02876   72 DHKCHSTLHTICIIPNVMDIVISLTLDCDI-ILDIKYASIILNKHKL--DEACIHILKEAISGNdIHYDKINESIEYMkl 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 210 ----IYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVN 285
Cdd:PHA02876  149 ikerIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                         170
                  ....*....|....*
gi 1034589512 286 LLLEQNVDVSSQDLS 300
Cdd:PHA02876  229 AIIDNRSNINKNDLS 243
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 170-272 5.93e-03

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: 38.63  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 170 RTALIKA---VQCQEDECVLMLLEHGADGN-----IQDEY------GNTALHYAIYNEDKLMAKALLLYGADIES----- 230
Cdd:cd22196    48 KTCLLKAmlnLHNGQNDTISLLLDIAEKTGnlkefVNAAYtdsyykGQTALHIAIERRNMHLVELLVQNGADVHArasge 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034589512 231 ---KNKC------GLTPLLLGVHEQKQEVVKFLIK---KKANLNALDRYGRTAL 272
Cdd:cd22196   128 ffkKKKGgpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVL 181
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 137-258 9.26e-03

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: 37.86  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589512 137 RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA-------------VQCQEDEC-VLMLLEH---GADGNIQD 199
Cdd:cd22196    95 QTALHIAIERRNMHLVELLVQNGADVHARASGEFFKKKKGgpgfyfgelplslAACTNQLDiVKFLLENphsPADISARD 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034589512 200 EYGNTALHYAIYNEDK---------LMAKALLLYGADI-------ESKNKCGLTPLLLGVHEQKQEVVKFLIKKK 258
Cdd:cd22196   175 SMGNTVLHALVEVADNtpentkfvtKMYNEILILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILGRE 249
 
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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