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Conserved domains on  [gi|268607514|ref|NP_001161330|]
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protein phosphatase 1 regulatory subunit 12B isoform f [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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-308 5.48e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 5.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  62 FLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 142 YFINHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666  171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 222 HVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGLVEHLELL 301
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                 ....*..
gi 268607514 302 QKKQNVL 308
Cdd:COG0666  271 LLLALLL 277
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 169-257 7.81e-04

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 7.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 169 MKDLLLEQVKKQGVDLEQ---SRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192 494 LKNFLQHHKELHDLNVGDllgDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                         90       100
                 ....*....|....*....|....*
gi 268607514 233 LRLLIQAGYELNVQDYDGWTPLHAA 257
Cdd:PLN03192 574 VLVLLKHACNVHIRDANGNTALWNA 598
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-308 5.48e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 5.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  62 FLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 142 YFINHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666  171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 222 HVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGLVEHLELL 301
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                 ....*..
gi 268607514 302 QKKQNVL 308
Cdd:COG0666  271 LLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 6.86e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 6.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514   65 ACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENrANVNQQDNeGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 268607514  145 NHGASVGIVN 154
Cdd:pfam12796  82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-290 9.87e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 96.25  E-value: 9.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  61 VFLAACSSGDTDEVRKLLARGADINTVNVDGLTALH-QACIDENLDMVKFLVENRANVNQQDNEGWTPLHAaascgYL-- 137
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 138 -----NIAEYFINHGASVGIVNSEGEVPSDLAeepamkdllleqVKKQGVDLEQSRkeeeqqMLQDArqwlnsgkIEDVR 212
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 213 QARS-GATALHVAA--AKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSI--LAEALCDMDIRNKLGQTPF 287
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL 261


                 ...
gi 268607514 288 DVA 290
Cdd:PHA03095 262 HYA 264
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 55-305 1.75e-08

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: 56.17  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  55 RFEDGAVFLAAcSSGDTDEVRKLL-ARGADINTVNVDGLTALHQACIDENLDMVKFLVEN-RANVNQ----QDNEGWTPL 128
Cdd:cd22192   15 RISESPLLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNEpmtsDLYQGETAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 129 HAAASCGYLNIAEYFINHGASVGIVNSEGEVPSdlaeePAMKDLLLeqvkkqgvdleqsrkeeeqqmlqdarqwlnsgki 208
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGADVVSPRATGTFFR-----PGPKNLIY---------------------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 209 edvrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKE-ACSILaEALCDMD---------- 277
Cdd:cd22192  135 -------YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldl 206

                        250       260
                 ....*....|....*....|....*....
gi 268607514 278 IRNKLGQTPFDVA-DEGLVEHLELLQKKQ 305
Cdd:cd22192  207 VPNNQGLTPFKLAaKEGNIVMFQHLVQKR 235
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-150 2.17e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 2.17e-05
                           10        20
                   ....*....|....*....|....*...
gi 268607514   123 EGWTPLHAAASCGYLNIAEYFINHGASV 150
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-260 4.11e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514   91 GLTALHQACIDENLDMVKFLVENRANVNQQDN--------------EGWTPLHAAASCGYLNIAEYFINHGASVGIVNSE 156
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  157 G-EVPSDLAEEPAMKDLLLEqvkkqgvdLEQSRKEEEQQMLQDARqwlNSGKIEDVRQaRSGATALHVAAAKGYSEVLRL 235
Cdd:TIGR00870 208 GnTLLHLLVMENEFKAEYEE--------LSCQMYNFALSLLDKLR---DSKELEVILN-HQGLTPLKLAAKEGRIVLFRL 275

                         170       180
                  ....*....|....*....|....*..
gi 268607514  236 LIQAGYElnVQDYDGWT--PLHAAAHW 260
Cdd:TIGR00870 276 KLAIKYK--QKKFVAWPngQQLLSLYW 300
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-257 7.81e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 7.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 169 MKDLLLEQVKKQGVDLEQ---SRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192 494 LKNFLQHHKELHDLNVGDllgDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                         90       100
                 ....*....|....*....|....*
gi 268607514 233 LRLLIQAGYELNVQDYDGWTPLHAA 257
Cdd:PLN03192 574 VLVLLKHACNVHIRDANGNTALWNA 598
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-308 5.48e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 5.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  62 FLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 142 YFINHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666  171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 222 HVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGLVEHLELL 301
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                 ....*..
gi 268607514 302 QKKQNVL 308
Cdd:COG0666  271 LLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-327 5.56e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 5.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  62 FLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 142 YFINHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666  138 LLLEAGADVNAQDNDGN------------------------------------------------------------TPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 222 HVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA----DEGLVEH 297
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengNLEIVKL 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 268607514 298 LELLQKKQNVLRSEKETRNKLIESDLNSKI 327
Cdd:COG0666  238 LLEAGADLNAKDKDGLTALLLAAAAGAALI 267
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 6.86e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 6.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514   65 ACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENrANVNQQDNeGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 268607514  145 NHGASVGIVN 154
Cdd:pfam12796  82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-290 9.87e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 96.25  E-value: 9.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  61 VFLAACSSGDTDEVRKLLARGADINTVNVDGLTALH-QACIDENLDMVKFLVENRANVNQQDNEGWTPLHAaascgYL-- 137
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 138 -----NIAEYFINHGASVGIVNSEGEVPSDLAeepamkdllleqVKKQGVDLEQSRkeeeqqMLQDArqwlnsgkIEDVR 212
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 213 QARS-GATALHVAA--AKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSI--LAEALCDMDIRNKLGQTPF 287
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL 261


                 ...
gi 268607514 288 DVA 290
Cdd:PHA03095 262 HYA 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-258 6.06e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.80  E-value: 6.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  72 DEVRKLLARGADINTVNVDGLTALH-----QACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASC--GYLNIAEYFI 144
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 145 NHGASVGIVNSEGEVPSDLAEEPAMKDL-LLEQVKKQGVDLEQSRKEEeqqMLqdarqwLNSGKIEDVRQARsGATALHV 223
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKGVDINAKNRVN---YL------LSYGVPINIKDVY-GFTPLHY 198

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 268607514 224 AAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAA 258
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-247 3.30e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514   95 LHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGasvgivnsegevpsdlaeepamkdlll 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268607514  175 eqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkieDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQD 247
Cdd:pfam12796  54 -----------------------------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-164 1.21e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  62 FLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQA--CIDENLDMVKFLVENRANVNQQ----------------DNE 123
Cdd:PHA03100 112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVY 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 268607514 124 GWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLA 164
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-144 2.30e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.61  E-value: 2.30e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 268607514   91 GLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-301 8.36e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 8.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  221 LHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 299
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 268607514  300 LL 301
Cdd:pfam12796  79 LL 80
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-290 2.55e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  70 DTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGAS 149
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 150 VGIVNSEGEVPSDLAEE---PAMKDLLLEqvkkqgvdleqsrkeeeqqmlqdarqwlNSGKIEDvrQARSGATALHVAAA 226
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEygdYACIKLLID----------------------------HGNHIMN--KCKNGFTPLHNAII 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268607514 227 KGYSeVLRLLIQaGYELNVQDYDGWTPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02874 233 HNRS-AIELLIN-NASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-290 5.90e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  65 ACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDnegwTPLHAAASCGYLNIAEYFI 144
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 145 NHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDleqsrkeeeqqmlqdarqwLNSGKIEdvrqarsGATALHVA 224
Cdd:PHA02876 261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGAD-------------------VNAKNIK-------GETPLYLM 314

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607514 225 AAKGY-SEVLRLLIQAGYELNVQDYDGWTPLHAAAHWG-VKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02876 315 AKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA 382
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-290 7.30e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.52  E-value: 7.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  85 NTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLA 164
Cdd:PHA02878  31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 165 EEPA--MKDLLLEQVKK-QGVDLEQSRKEEEQQMLQDA--RQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQA 239
Cdd:PHA02878 111 NRNVeiFKIILTNRYKNiQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 268607514 240 GYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-155 3.44e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  72 DEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVG 151
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....
gi 268607514 152 IVNS 155
Cdd:PHA03100 253 TIIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 70-283 1.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  70 DTDEVRKLLARGADINTVNVDGL-TALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGA 148
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 149 SVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLeqsrkeeeqqmlqdarqwlnsgkieDVRQARSGATALHVAAAKg 228
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDV-------------------------NAKSYILGLTALHSSIKS- 279

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607514 229 ySEVLRLLIQAGYELNVQDYDGWTPLHAAA--HWGVkEACSILAEALC-----DMDIRNKLG 283
Cdd:PHA02878 280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCI-NIGRILISNICllkriKPDIKNSEG 339
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-269 6.52e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 6.52e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 268607514  219 TALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSIL 269
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-290 2.48e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 103 NLDMVKFLVENRAN-VNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEgeVPSDLAEE--------------- 166
Cdd:PHA02874  13 DIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK--IPHPLLTAikigahdiikllidn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 167 ---------PAMKDLLLEQVKKQGVDLEQSRKE--------------EEQQMLQDARQWLNsgkIEDVrqarSGATALHV 223
Cdd:PHA02874  91 gvdtsilpiPCIEKDMIKTILDCGIDVNIKDAElktflhyaikkgdlESIKMLFEYGADVN---IEDD----NGCYPIHI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607514 224 AAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 63-169 3.39e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  63 LAAcsSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEY 142
Cdd:PTZ00322  89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                         90       100       110
                 ....*....|....*....|....*....|...
gi 268607514 143 FINH------GASVGIVNSEGEVPSDLAEEPAM 169
Cdd:PTZ00322 167 LSRHsqchfeLGANAKPDSFTGKPPSLEDSPIS 199
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-348 5.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 5.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  65 ACSSGDTDEVRKLLARGADINTVNV-DGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYF 143
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 144 INHGASVGIVNSEGEVPsdlaeepamkdlLLEQVKKQGVDLeqsrkeeeqqmlqdARQWLNSGKIEDVRQARSGATALHV 223
Cdd:PHA02875 155 IDHKACLDIEDCCGCTP------------LIIAMAKGDIAI--------------CKMLLDSGANIDYFGKNGCVAALCY 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 224 AAAKGYSEVLRLLIQAGYELNVqdydgwtplhaaAHWGVKEACSILaEALCDMDIrnklgqTPFDVADEGLVEHLELLQK 303
Cdd:PHA02875 209 AIENNKIDIVRLFIKRGADCNI------------MFMIEGEECTIL-DMICNMCT------NLESEAIDALIADIAIRIH 269

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 268607514 304 KQNVLRSEKETRNKlieSDLNSKiqSGFFKNKEKMLYEEETPKSQ 348
Cdd:PHA02875 270 KKTIRRDEGFKNNM---STIEDK--EEFKDVFEKCIIELRRIKSE 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-121 5.99e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 5.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 268607514   64 AACSSGDTDEVrKLLARGADINtVNVDGLTALHQACIDENLDMVKFLVENRANVNQQD 121
Cdd:pfam12796  36 LAAKNGHLEIV-KLLLEHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
61-111 7.71e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 7.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 268607514   61 VFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLV 111
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-159 7.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 7.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  54 VRFEDGAVFL-AACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAA 132
Cdd:PHA02875  97 VFYKDGMTPLhLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                         90       100
                 ....*....|....*....|....*..
gi 268607514 133 SCGYLNIAEYFINHGASVGIVNSEGEV 159
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCV 203
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 1.08e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.08e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 268607514   77 LLARG-ADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAA 131
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-150 1.39e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  61 VFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQA-CIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNI 139
Cdd:PHA02876 311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                         90
                 ....*....|.
gi 268607514 140 AEYFINHGASV 150
Cdd:PHA02876 391 INTLLDYGADI 401
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 3.51e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 3.51e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 268607514  110 LVENR-ANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLA 164
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 69-183 8.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 8.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  69 GDTDEVRKLLARGADINTVNVDGLTALHQACIdENLDMVKFLVENRAnVNQQDNEGWTPLHAAAS--CGyLNIAEYFINH 146
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLINNAS-INDQDIDGSTPLHHAINppCD-IDIIDILLYH 277

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 268607514 147 GASVGIVNSEGEVPSDLA-----EEPAMKDLLLEQVKKQGVD 183
Cdd:PHA02874 278 KADISIKDNKGENPIDTAfkyinKDPVIKDIIANAVLIKEAD 319
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 55-305 1.75e-08

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: 56.17  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  55 RFEDGAVFLAAcSSGDTDEVRKLL-ARGADINTVNVDGLTALHQACIDENLDMVKFLVEN-RANVNQ----QDNEGWTPL 128
Cdd:cd22192   15 RISESPLLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNEpmtsDLYQGETAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 129 HAAASCGYLNIAEYFINHGASVGIVNSEGEVPSdlaeePAMKDLLLeqvkkqgvdleqsrkeeeqqmlqdarqwlnsgki 208
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGADVVSPRATGTFFR-----PGPKNLIY---------------------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 209 edvrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKE-ACSILaEALCDMD---------- 277
Cdd:cd22192  135 -------YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldl 206

                        250       260
                 ....*....|....*....|....*....
gi 268607514 278 IRNKLGQTPFDVA-DEGLVEHLELLQKKQ 305
Cdd:cd22192  207 VPNNQGLTPFKLAaKEGNIVMFQHLVQKR 235
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-152 4.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  65 ACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLH-AAASCGYLNIAEYF 143
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLL 254


                 ....*....
gi 268607514 144 INHGASVGI 152
Cdd:PHA02878 255 LEHGVDVNA 263
PHA02798 PHA02798
ankyrin-like protein; Provisional
 71-333 4.62e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.84  E-value: 4.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  71 TDEVRKLLARGADINTVNVDGLTALhqaC------IDEN--LDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE- 141
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 142 --YFINHGASVGIVNSEG------EVPSDLAEEPAMKDLLLEqvkkQGVDLEQSRKEEEQQMLQ-------------DAR 200
Cdd:PHA02798 128 llFMIENGADTTLLDKDGftmlqvYLQSNHHIDIEIIKLLLE----KGVDINTHNNKEKYDTLHcyfkynidridadILK 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 201 QWLNSGKI--EDVRQARSG----ATALHVAAAKGYSEVLRLLIQAgyeLNVQDYD--GWTPLHAAAHWGVKEACSILAEA 272
Cdd:PHA02798 204 LFVDNGFIinKENKSHKKKfmeyLNSLLYDNKRFKKNILDFIFSY---IDINQVDelGFNPLYYSVSHNNRKIFEYLLQL 280

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607514 273 LCDMDIRNKLGQTPFDVADEglvehlellqkkqnvlRSEKETRNKLIESDLNSK-IQSGFFK 333
Cdd:PHA02798 281 GGDINIITELGNTCLFTAFE----------------NESKFIFNSILNKKPNKNtISYTYYK 326
Ank_5 pfam13857
Ankyrin repeats (many copies);
203-257 2.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 2.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 268607514  203 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAA 257
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 63-254 3.15e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  63 LAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEy 142
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR- 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 143 FINHGASVGIVNSEGEVPSDLAEE---PAMKDLLleqvkKQGVDLEQsrkeeeqqmlqdarqwlnsgkiEDvrqaRSGAT 219
Cdd:PLN03192 609 ILYHFASISDPHAAGDLLCTAAKRndlTAMKELL-----KQGLNVDS----------------------ED----HQGAT 657

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 268607514 220 ALHVAAAKGYSEVLRLLIQAGYELN-VQDYDGWTPL 254
Cdd:PLN03192 658 ALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPT 693
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 225-301 5.22e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 5.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607514 225 AAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE-GLVEHLELL 301
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEnGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 90-122 1.15e-06

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: 44.59  E-value: 1.15e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 268607514   90 DGLTALHQACIDE-NLDMVKFLVENRANVNQQDN 122
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-118 3.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 3.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 268607514  65 ACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVN 118
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-150 5.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  60 AVFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDE-NLDMVKFLVENRANVNQQDNEGWTPLHAAasCGYLN 138
Cdd:PHA02876 411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                         90
                 ....*....|..
gi 268607514 139 IAEYFINHGASV 150
Cdd:PHA02876 489 IVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-117 1.14e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 1.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 268607514  59 GAVFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANV 117
Cdd:PLN03192 623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-154 1.19e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.19e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 268607514  123 EGWTPLHAAA-SCGYLNIAEYFINHGASVGIVN 154
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 90-118 1.84e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 1.84e-05
                          10        20
                  ....*....|....*....|....*....
gi 268607514   90 DGLTALHQACIDENLDMVKFLVENRANVN 118
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-150 2.17e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 2.17e-05
                           10        20
                   ....*....|....*....|....*...
gi 268607514   123 EGWTPLHAAASCGYLNIAEYFINHGASV 150
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 107-172 2.43e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 2.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268607514 107 VKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLAEEPAMKDL 172
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 90-118 8.48e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 8.48e-05
                           10        20
                   ....*....|....*....|....*....
gi 268607514    90 DGLTALHQACIDENLDMVKFLVENRANVN 118
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-247 1.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 268607514  217 GATALHVAAAK-GYSEVLRLLIQAGYELNVQD 247
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-290 1.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 102 ENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEG----EVPSDLAEEPAMKDLL--LE 175
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDlsvlECAVDSKNIDTIKAIIdnRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 176 QVKKQGVDLEQSRKEEEQQ---MLQDARQWLNSgkIEDVRQarsgaTALHVAA-AKGYSEVLRLLIQAGYELNVQDYDGW 251
Cdd:PHA02876 236 NINKNDLSLLKAIRNEDLEtslLLYDAGFSVNS--IDDCKN-----TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGE 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 268607514 252 TPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02876 309 TPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQA 348
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 91-257 2.18e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  91 GLTALHQACIDENLDMVKFLVENRANVNQQDNE-------------GWTPLHAAASCGYLNIAEYFINHGASvgivnseg 157
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ-------- 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 158 evPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQ---QMLQDARQWLNSGKIEDVRQaRSGATALHVAAAKGYSEVLR 234
Cdd:cd21882  145 --PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQmynLLLSYGAHLDPTQQLEEIPN-HQGLTPLKLAAVEGKIVMFQ 221

                        170       180
                 ....*....|....*....|....*....
gi 268607514 235 LLIQ----AGYELNVQDYDGWT--PLHAA 257
Cdd:cd21882  222 HILQrefsGPYQPLSRKFTEWTygPVTSS 250
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 215-304 2.22e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.40  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 215 RSGATALHVAAAKGYS---EVLRLLIQAGYELNVQD-YDGWTPLHAAAHWGVKEacsiLAEALC-----DMDIRNKLGQT 285
Cdd:PHA02736  53 RHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYE----LATWLCnqpgvNMEILNYAFKT 128

                         90       100
                 ....*....|....*....|
gi 268607514 286 PFDVA-DEGLVEHLELLQKK 304
Cdd:PHA02736 129 PYYVAcERHDAKMMNILRAK 148
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-160 2.90e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 2.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268607514 101 DENLDMVKFLVENRANVNQQDNEGWTPLHAAASC-----GYLNIAEYFINHGASVGIVNSEGEVP 160
Cdd:PHA02798  48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETP 112
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 3.10e-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: 37.62  E-value: 3.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 268607514  123 EGWTPLHAAASCGYLNIAEYFINHGASVGI 152
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-290 3.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 268607514  250 GWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 217-245 4.00e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 4.00e-04
                           10        20
                   ....*....|....*....|....*....
gi 268607514   217 GATALHVAAAKGYSEVLRLLIQAGYELNV 245
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-260 4.11e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514   91 GLTALHQACIDENLDMVKFLVENRANVNQQDN--------------EGWTPLHAAASCGYLNIAEYFINHGASVGIVNSE 156
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  157 G-EVPSDLAEEPAMKDLLLEqvkkqgvdLEQSRKEEEQQMLQDARqwlNSGKIEDVRQaRSGATALHVAAAKGYSEVLRL 235
Cdd:TIGR00870 208 GnTLLHLLVMENEFKAEYEE--------LSCQMYNFALSLLDKLR---DSKELEVILN-HQGLTPLKLAAKEGRIVLFRL 275

                         170       180
                  ....*....|....*....|....*..
gi 268607514  236 LIQAGYElnVQDYDGWT--PLHAAAHW 260
Cdd:TIGR00870 276 KLAIKYK--QKKFVAWPngQQLLSLYW 300
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-290 4.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  94 ALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGAsvgivnsegeVPSdlAEEPAMKDLL 173
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA----------IPD--VKYPDIESEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 174 LEQVKKQGVdleqsRKEEEqqmlqdarqWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTP 253
Cdd:PHA02875  73 HDAVEEGDV-----KAVEE---------LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 268607514 254 LHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 186-285 6.63e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 6.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 186 QSRKEEEQQMLQDARQW---LNSGKIEDVRQARSG-------ATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLH 255
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHhkeLHDLNVGDLLGDNGGehddpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                         90       100       110
                 ....*....|....*....|....*....|
gi 268607514 256 AAAHWGVKEACSILAEALCDMDIRNKLGQT 285
Cdd:PLN03192 564 IAASKGYEDCVLVLLKHACNVHIRDANGNT 593
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-257 7.81e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 7.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 169 MKDLLLEQVKKQGVDLEQ---SRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192 494 LKNFLQHHKELHDLNVGDllgDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                         90       100
                 ....*....|....*....|....*
gi 268607514 233 LRLLIQAGYELNVQDYDGWTPLHAA 257
Cdd:PLN03192 574 VLVLLKHACNVHIRDANGNTALWNA 598
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 73-163 1.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  73 EVRKLLAR-GADINTVNVDGLTALHQAC--IDENLDMVKFLVENRANVNQQDNEGWTPLHAaascgYL------NIAEYF 143
Cdd:PHA02859 104 EILKILIDsGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                         90       100
                 ....*....|....*....|
gi 268607514 144 INHGASVGIVNSEGEVPSDL 163
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDL 198
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 70-254 1.35e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  70 DTDEVRKLLARGADINTVNVDGLTALHQACIDENL--DMVKFLVENRANVNQQDNEGWTPLHAAASCG------------ 135
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 136 --YLNIAEYFINHGASVGIVNSEGEVP-------------SDLAeEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQ--- 197
Cdd:PHA02716 376 diRLDVIQCLISLGADITAVNCLGYTPltsyictaqnymyYDII-DCLISDKVLNMVKHRILQDLLIRVDDTPCIIHhii 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 198 -----------DARQWLNSGKIEDVRQAR------------SGATALHVAA-----AKGYSEVLRLLIQAGYELNVQDYD 249
Cdd:PHA02716 455 akyniptdlytDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKN 534


                 ....*
gi 268607514 250 GWTPL 254
Cdd:PHA02716 535 GVTPL 539
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-98 1.63e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 268607514   65 ACSSGDTDEVRKLLARGADINTVNVDGLTALHQA 98
Cdd:pfam13857  23 AAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 77-171 1.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  77 LLARGADINTVNVDGLTALHQA----CideNLDMVKFLVENRANVNQQDNEGWTPLHAAAScgYLNIAEYFINHGASVGI 152
Cdd:PHA02874 240 LLINNASINDQDIDGSTPLHHAinppC---DIDIIDILLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIANAVL 314

                         90       100
                 ....*....|....*....|
gi 268607514 153 VNSEGEVP-SDLAEEPAMKD 171
Cdd:PHA02874 315 IKEADKLKdSDFLEHIEIKD 334
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 74-149 2.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  74 VRKLLARGADIN-TVNVDGLTALHQ-ACIDENL--DMVKFLVENRANVNQQDNEGWTPLHA-AASCGY-LNIAEYFINHG 147
Cdd:PHA02859  69 LKFLIENGADVNfKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMyMCNFNVrINVIKLLIDSG 148


                 ..
gi 268607514 148 AS 149
Cdd:PHA02859 149 VS 150
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-245 2.05e-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: 2.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 268607514  217 GATALHVAAAKGYSEVLRLLIQAGYELNV 245
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 199-269 3.00e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 3.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607514 199 ARQWLNSGKIEDVRQaRSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSIL 269
Cdd:PTZ00322  98 ARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 249-281 3.48e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 3.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 268607514  249 DGWTPLHAAA-HWGVKEACSILAEALCDMDIRNK 281
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-290 4.77e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 4.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 268607514  236 LIQAGYE-LNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 68-160 4.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  68 SGDTDEVRKLLARGADINTVNVdglTALHqACIDE---NLDMVKFLVENRANVN-QQDNEGWTPLHAaascgYLN----- 138
Cdd:PHA02859  31 KDDIEGVKKWIKFVNDCNDLYE---TPIF-SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHH-----YLSfnknv 101

                         90       100
                 ....*....|....*....|....*
gi 268607514 139 ---IAEYFINHGASVGIVNSEGEVP 160
Cdd:PHA02859 102 epeILKILIDSGSSITEEDEDGKNL 126
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 91-238 7.11e-03

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: 38.30  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  91 GLTALHQACIDENLDMVKFLVENRANVNQ-------QDNEGWT------PLHAAASCGYLNIAEYFINHG---ASVGIVN 154
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrffQKKQGTCfyfgelPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514 155 SEGE--------VPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQdarqwlnsgkiedvrqarsGATALHVAAA 226
Cdd:cd22197  174 SLGNtvlhalvmIADNSPENSALVIKMYDGLLQAGARLCPTVQLEEISNHE-------------------GLTPLKLAAK 234

                        170
                 ....*....|..
gi 268607514 227 KGYSEVLRLLIQ 238
Cdd:cd22197  235 EGKIEIFRHILQ 246
PHA02795 PHA02795
ankyrin-like protein; Provisional
 83-155 8.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.05  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607514  83 DINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCG--------YLNIAEYFINHGASVGIVN 154
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLREPLSIDCIK 292


                 .
gi 268607514 155 S 155
Cdd:PHA02795 293 L 293
 
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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