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Conserved domains on  [gi|1310163689|ref|NP_001345862|]
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protein phosphatase 1 regulatory subunit 16A [Mus musculus]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-327 5.05e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 5.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLV 153
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 154 ELLISRGADLLAVNSDGNMPydlcedaqtldcLETAMANQgitqegieEARAVPELcmlndlqnrLQAGANLSDPLDHGA 233
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTP------------LHLAAANG--------NLEIVKLL---------LEAGADVNARDNDGE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 234 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD---VCGDEEV 310
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALI 267

                         250
                  ....*....|....*..
gi 1310163689 311 RAKLLELKHKQDALLRA 327
Cdd:COG0666   268 VKLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-327 5.05e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 5.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLV 153
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 154 ELLISRGADLLAVNSDGNMPydlcedaqtldcLETAMANQgitqegieEARAVPELcmlndlqnrLQAGANLSDPLDHGA 233
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTP------------LHLAAANG--------NLEIVKLL---------LEAGADVNARDNDGE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 234 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD---VCGDEEV 310
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALI 267

                         250
                  ....*....|....*..
gi 1310163689 311 RAKLLELKHKQDALLRA 327
Cdd:COG0666   268 VKLLLLALLLLAAALLD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-167 2.00e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  75 LLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDaGADVNARDSEcWTPLHAAATCGHLHLVE 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1310163689 155 LLISRGADLLAVN 167
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 119-302 5.06e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 5.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 119 MAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNMPYDLCEDAQTLDCLETAMANQG-ITQ 197
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 198 EGIEEARAVPElcmlNDLQNRL---QAGANLSDPLDHGATLLHIAA-ANGFSEVATLLLEQGASLSAKDHDGWEPLHAAA 273
Cdd:PHA02876  240 NDLSLLKAIRN----EDLETSLllyDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190
                  ....*....|....*....|....*....|
gi 1310163689 274 YWG-QVHLVELLVAHGADLNGKSLVDETPL 302
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAADRLYITPL 345
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 76-196 8.18e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  76 LEAAARNDLEEVRQFLTSGVsPNLANE-------DGLTALHQCCIDDFQEMAQQLLDAGADV-NAR----------DSEC 137
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAA-PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVvSPRatgtffrpgpKNLI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 138 W---TPLHAAATCGHLHLVELLISRGADLLAVNSDGNMP----------------YDLC---EDAQTLDCLETAMANQGI 195
Cdd:cd22192   134 YygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhilvlqpnktfacqmYDLIlsyDKEDDLQPLDLVPNNQGL 213


                  .
gi 1310163689 196 T 196
Cdd:cd22192   214 T 214
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 264-292 5.02e-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: 40.26  E-value: 5.02e-05
                           10        20
                   ....*....|....*....|....*....
gi 1310163689  264 DGWEPLHAAAYWGQVHLVELLVAHGADLN 292
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 231-292 5.81e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 5.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310163689 231 HGATLLHIAAANGFSEVATLLLEQGASLSAK----------DHD----GWEPLHAAAYWGQVHLVELLVAHGADLN 292
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqGVDsfyhGESPLNAAACLGSPSIVALLSEDPADIL 202
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-327 5.05e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 5.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLV 153
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 154 ELLISRGADLLAVNSDGNMPydlcedaqtldcLETAMANQgitqegieEARAVPELcmlndlqnrLQAGANLSDPLDHGA 233
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTP------------LHLAAANG--------NLEIVKLL---------LEAGADVNARDNDGE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 234 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD---VCGDEEV 310
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALI 267

                         250
                  ....*....|....*..
gi 1310163689 311 RAKLLELKHKQDALLRA 327
Cdd:COG0666   268 VKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-302 2.47e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 2.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLV 153
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 154 ELLISRGADLLAVNSDGNMPYDLCEDAQTLDCLEtamanqgitqegieearavpelcMLndlqnrLQAGANLSDPLDHGA 233
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVK-----------------------LL------LEAGADVNAKDNDGK 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310163689 234 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 302
Cdd:COG0666   221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-327 3.96e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 3.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLV 153
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 154 ELLISRGADLLAVNSDGNMPYDLCEDAQTLDCLEtamanqgitqegieearavpelcMLndlqnrLQAGANLSDPLDHGA 233
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK-----------------------LL------LEAGADVNAQDNDGN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 234 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV---CGDEEV 310
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEI 234

                         250
                  ....*....|....*..
gi 1310163689 311 RAKLLELKHKQDALLRA 327
Cdd:COG0666   235 VKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-322 7.76e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 7.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 150 LHLVELLISRGADLLAVNSDGNMPYDLCEDAQTLDCLETAMANQGITQEGIEEARAVPELCMLNDLQNRLQAGANLSDPL 229
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 230 DHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV---CG 306
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNG 164

                         170
                  ....*....|....*.
gi 1310163689 307 DEEVrAKLLeLKHKQD 322
Cdd:COG0666   165 NLEI-VKLL-LEAGAD 178
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-167 2.00e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  75 LLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDaGADVNARDSEcWTPLHAAATCGHLHLVE 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1310163689 155 LLISRGADLLAVN 167
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 119-302 5.06e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 5.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 119 MAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNMPYDLCEDAQTLDCLETAMANQG-ITQ 197
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 198 EGIEEARAVPElcmlNDLQNRL---QAGANLSDPLDHGATLLHIAA-ANGFSEVATLLLEQGASLSAKDHDGWEPLHAAA 273
Cdd:PHA02876  240 NDLSLLKAIRN----EDLETSLllyDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190
                  ....*....|....*....|....*....|
gi 1310163689 274 YWG-QVHLVELLVAHGADLNGKSLVDETPL 302
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAADRLYITPL 345
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-302 1.75e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  76 LEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCC---IDDFQEMAQQLLDAGADVNARDSECWTPLH---------- 142
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHlylynattld 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 143 -------------AAATCG----HLHL---------VELLISRGADLLAVNSDGNMPydlcedaqtLDCLetaMANQGIT 196
Cdd:PHA03095   99 vikllikagadvnAKDKVGrtplHVYLsgfninpkvIRLLLRKGADVNALDLYGMTP---------LAVL---LKSRNAN 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 197 QE-------GIEEARAVpELCMLNDLQNRLQ--------------AGANLSDPLDHGATLLHIAAAnGFSEVATL---LL 252
Cdd:PHA03095  167 VEllrllidAGADVYAV-DDRFRSLLHHHLQsfkprarivrelirAGCDPAATDMLGNTPLHSMAT-GSSCKRSLvlpLL 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1310163689 253 EQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 302
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
236-322 4.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 236 LHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHgADLNGKSLvDETPLDVC---GDEEVrA 312
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEI-V 77

                          90
                  ....*....|
gi 1310163689 313 KLLeLKHKQD 322
Cdd:pfam12796  78 KLL-LEKGAD 86
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 73-302 8.99e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  73 VALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCC-IDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGH-L 150
Cdd:PHA02876  242 LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdT 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 151 HLVELLISRGADLLAVNSDGNMPYdlcEDAQTLD--------CLETAM---ANQGITQEGIEEARAVPELCMLNDLqnrL 219
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPL---HQASTLDrnkdivitLLELGAnvnARDYCDKTPIHYAAVRNNVVIINTL---L 395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 220 QAGANLSDPLDHGATLLHIA--AANGFSEVATLLlEQGASLSAKDHDGWEPLHAAAYWG-QVHLVELLVAHGADLNGKSL 296
Cdd:PHA02876  396 DYGADIEALSQKIGTALHFAlcGTNPYMSVKTLI-DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474


                  ....*.
gi 1310163689 297 VDETPL 302
Cdd:PHA02876  475 QNQYPL 480
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-262 4.40e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 4.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 108 LHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISrgadllavNSDGNMPydlcedaqtldcle 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--------HADVNLK-------------- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310163689 188 tamanqgitqegieearavpelcmlndlqnrlqaganlsdplDHGATLLHIAAANGFSEVATLLLEQGASLSAKD 262
Cdd:pfam12796  59 ------------------------------------------DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-292 5.34e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.34e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310163689 219 LQAGANLSDPLDHGATLLHIAAANGFSEVATLLLEQGASlsAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLN 292
Cdd:pfam12796  17 LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-302 3.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  83 DLEEVRQFL-TSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGA 161
Cdd:PHA02874   13 DIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 162 DLLAVnsdgnmpydlcedaqTLDCLETAMANQgITQEGIEEARAVPELCML-------NDLQN---RLQAGANLSDPLDH 231
Cdd:PHA02874   93 DTSIL---------------PIPCIEKDMIKT-ILDCGIDVNIKDAELKTFlhyaikkGDLESikmLFEYGADVNIEDDN 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310163689 232 GATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 302
Cdd:PHA02874  157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-304 4.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  85 EEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLL 164
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 165 AVNSDGNMPYDLCEDAQTLDCLETAMANqgitqegieearavpelcmlndlqnrlqaGANLSDPLDHGATLLHIAAANGF 244
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDH-----------------------------GNHIMNKCKNGFTPLHNAIIHNR 235

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310163689 245 SEVAtlLLEQGASLSAKDHDGWEPLH-AAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV 304
Cdd:PHA02874  236 SAIE--LLINNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDT 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-157 1.41e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.41e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1310163689 104 GLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLI 157
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 91-302 1.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.15  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  91 LTSGVSPNLANEDGLTALHQCC-----IDDFQEMAQQLLDAGADVNARDSECWTPLHAAATC--GHLHLVELLISRGADL 163
Cdd:PHA03100   55 LDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 164 LAVNSDGNMPYdlcedAQTLDCLEtamanqgitqegieearavPELCMLNDLqnrlqaganlsdpLDHGAtllHIAAANg 243
Cdd:PHA03100  135 NIKNSDGENLL-----HLYLESNK-------------------IDLKILKLL-------------IDKGV---DINAKN- 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1310163689 244 fseVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 302
Cdd:PHA03100  174 ---RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-208 1.89e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 120 AQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNMPYDLCEDAQTLDCLETAMANQGITQEG 199
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                  ....*....
gi 1310163689 200 ieEARAVPE 208
Cdd:PTZ00322  178 --GANAKPD 184
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 121-364 2.36e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.35  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 121 QQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNmpydlcedaqtldcleTAMANQGITQEgi 200
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN----------------TALWNAISAKH-- 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 201 eearavpelcmlNDLQNRLQAGANLSDPlDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHL 280
Cdd:PLN03192  604 ------------HKIFRILYHFASISDP-HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 281 VELLVAHGADLNGKSLVDE-TPLDVcgdEEVRAKlLELKHK------QDALLRAQGRQRSLLRRRTSSAGSRGKVVRRVS 353
Cdd:PLN03192  671 VRLLIMNGADVDKANTDDDfSPTEL---RELLQK-RELGHSitivdsVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVS 746

                         250
                  ....*....|.
gi 1310163689 354 LTHRTNLYRKE 364
Cdd:PLN03192  747 IYKGHPLLRNE 757
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 78-295 8.85e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 8.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  78 AAARNDLEEVRQFLTSGVSPNLANEDGLTALhQCCIDDFQ------------------------------EMAQQLLDAG 127
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVL-ECAVDSKNidtikaiidnrsninkndlsllkairnedlETSLLLYDAG 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 128 ADVNARDSECWTPLHAAATCGHL-HLVELLISRGADLLAVNSDGNMPYDLcedaqtldcletaMANQGITQEGIEearav 206
Cdd:PHA02876  264 FSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL-------------MAKNGYDTENIR----- 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 207 pELCMLNdlqnrlqAGANLSDPLDHgaTLLHIAAA-NGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLV 285
Cdd:PHA02876  326 -TLIMLG-------ADVNAADRLYI--TPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                         250
                  ....*....|
gi 1310163689 286 AHGADLNGKS 295
Cdd:PHA02876  396 DYGADIEALS 405
Ank_4 pfam13637
Ankyrin repeats (many copies);
234-285 9.19e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 9.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1310163689 234 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLV 285
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-304 2.00e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 118 EMAQQLLDAGADVNARDSECW-TPLHAAATCGHLHLVELLISRGADLLAVNSDGNMPydlcedaqtldcletamanqgiT 196
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP----------------------L 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 197 QEGIEEARAvPELCMLndlqnrLQAGANLSDPLDHGATLLHIAAANGFS-EVATLLLEQGASLSAKDH-DGWEPLHAAAY 274
Cdd:PHA02878  206 HHAVKHYNK-PIVHIL------LENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                         170       180       190
                  ....*....|....*....|....*....|
gi 1310163689 275 WGQVhlVELLVAHGADLNGKSLVDETPLDV 304
Cdd:PHA02878  279 SERK--LKLLLEYGADINSLNSYKLTPLSS 306
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-327 2.28e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 212 LNDLQNRLQAGANLSDPLDHGATLLHIAAANGFS---EVATLLLEQGASLSAKDHDGWEPLHAAAYWGQV-HLVELLVAH 287
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1310163689 288 GADLNGKSLVDETPLDVC-GDEEVRAKLLELkhkqdaLLRA 327
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYlSGFNINPKVIRL------LLRK 141
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 73-292 2.81e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  73 VALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHL 152
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 153 VELLISRGADLLAV-NSDGNMPYDLCEDAQTLDCLETAMANQGITQEGIEEARAVPELC-MLNDLQN-----RLQAGANL 225
Cdd:PHA02875   84 VEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAvMMGDIKGielliDHKACLDI 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310163689 226 SDplDHGATLLHIAAANGFSEVATLLLEQGASLsakDHDGWEPLHAAAYWG----QVHLVELLVAHGADLN 292
Cdd:PHA02875  164 ED--CCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKNGCVAALCYAiennKIDIVRLFIKRGADCN 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-177 1.43e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1310163689 123 LLDAG-ADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNMPYDLC 177
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 72-158 1.77e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  72 SVALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLH 151
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162


                  ....*..
gi 1310163689 152 LVELLIS 158
Cdd:PTZ00322  163 VVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 219-287 3.02e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 3.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310163689 219 LQAGANLSDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAH 287
Cdd:PTZ00322  102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 76-196 8.18e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  76 LEAAARNDLEEVRQFLTSGVsPNLANE-------DGLTALHQCCIDDFQEMAQQLLDAGADV-NAR----------DSEC 137
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAA-PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVvSPRatgtffrpgpKNLI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 138 W---TPLHAAATCGHLHLVELLISRGADLLAVNSDGNMP----------------YDLC---EDAQTLDCLETAMANQGI 195
Cdd:cd22192   134 YygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhilvlqpnktfacqmYDLIlsyDKEDDLQPLDLVPNNQGL 213


                  .
gi 1310163689 196 T 196
Cdd:cd22192   214 T 214
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 75-162 1.68e-06

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: 50.78  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  75 LLEAAARNDLEEVRQFLTS-GVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGAD-VN-ARDSECW---TPLHAAATCG 148
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQ 100

                          90
                  ....*....|....
gi 1310163689 149 HLHLVELLISRGAD 162
Cdd:cd22192   101 NLNLVRELIARGAD 114
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 81-173 2.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  81 RNDLEEVRQFLTSGVSPNLANEDGLTALHQ---CCIDDFqEMAQQLLDAGADVNARDS---------------EC-WTPL 141
Cdd:PHA03100  118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLyleSNKIDL-KILKLLIDKGVDINAKNRvnyllsygvpinikdVYgFTPL 196

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1310163689 142 HAAATCGHLHLVELLISRGADLLAVNSDGNMP 173
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 208-311 2.26e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 208 ELCMLNDLQNRLQAGANLSDPLDHGAT--------LLHIA-------AANGFSEVATLLLEQGASLSAKDHDGWEPLHAA 272
Cdd:PTZ00322   43 EIARIDTHLEALEATENKDATPDHNLTteevidpvVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIA 122

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1310163689 273 AYWGQVHLVELLVAHGADLNGKSLVDETPLDVCGDEEVR 311
Cdd:PTZ00322  123 CANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-162 2.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  82 NDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGA 161
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  .
gi 1310163689 162 D 162
Cdd:PHA03100  250 S 250
PHA02946 PHA02946
ankyin-like protein; Provisional
 87-302 5.86e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  87 VRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAAATCGH--LHLVELLISRGADL- 163
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIn 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 164 LAVNSDGNMPYDLCEDAqtldcleTAMANQGITQEGIEearavpelcmlndlqnrlqagANLSDPLDHGATLLHIAAANG 243
Cdd:PHA02946  135 NSVDEEGCGPLLACTDP-------SERVFKKIMSIGFE---------------------ARIVDKFGKNHIHRHLMSDNP 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310163689 244 FSEVATLLLEQGASLSAKDHDGWEPLH--AAAYWGQVHLVELLVAhGADLNGKSLVDETPL 302
Cdd:PHA02946  187 KASTISWMMKLGISPSKPDHDGNTPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-167 1.35e-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: 1.35e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1310163689 138 WTPLHAAAT-CGHLHLVELLISRGADLLAVN 167
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 134-298 2.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 134 DSECW---TPLHAAATCGHLHLVELLISRGADLLAVNSDGNMPYDLcedaqtldcLETAMANqgitqegieeARAVPEL- 209
Cdd:PHA03100   29 DYSYKkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHY---------LSNIKYN----------LTDVKEIv 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 210 CMLndlqnrLQAGANLSDPLDHGATLLHIAAAN--GFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHL--VELLV 285
Cdd:PHA03100   90 KLL------LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLI 163

                         170
                  ....*....|...
gi 1310163689 286 AHGADLNGKSLVD 298
Cdd:PHA03100  164 DKGVDINAKNRVN 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 247-303 3.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1310163689 247 VATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD 303
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 264-292 5.02e-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: 40.26  E-value: 5.02e-05
                           10        20
                   ....*....|....*....|....*....
gi 1310163689  264 DGWEPLHAAAYWGQVHLVELLVAHGADLN 292
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 138-163 5.87e-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: 40.26  E-value: 5.87e-05
                           10        20
                   ....*....|....*....|....*.
gi 1310163689  138 WTPLHAAATCGHLHLVELLISRGADL 163
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 71-316 9.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  71 PSVALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLdagADVNARDseCWTPLHAAATCGHL 150
Cdd:PHA02878   37 PFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCS--VFYTLVAIKDAFNN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 151 HLVELLISrgadLLAVNSDGNmpydlcedaQTLDCLETamanQGITQEGIEEARAVPELcmlndlqnrLQAGA--NLSDP 228
Cdd:PHA02878  112 RNVEIFKI----ILTNRYKNI---------QTIDLVYI----DKKSKDDIIEAEITKLL---------LSYGAdiNMKDR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 229 lDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV---- 304
Cdd:PHA02878  166 -HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvgy 244

                         250
                  ....*....|..
gi 1310163689 305 CGDEEVRAKLLE 316
Cdd:PHA02878  245 CKDYDILKLLLE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
265-315 2.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1310163689 265 GWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDVC---GDEEVrAKLL 315
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEV-LKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-144 2.66e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1310163689  95 VSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLHAA 144
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-165 3.58e-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: 38.01  E-value: 3.58e-04
                          10        20
                  ....*....|....*....|....*...
gi 1310163689 138 WTPLHAAATCGHLHLVELLISRGADLLA 165
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
137-173 3.72e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1310163689 137 CWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNMP 173
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 103-134 4.03e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 4.03e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1310163689 103 DGLTALHQCCID-DFQEMAQQLLDAGADVNARD 134
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 231-290 4.05e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 4.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310163689 231 HGATLLHIAAANGFSEVATLLLEQGASL-----SAKDHDGWEPLHAAAYWGQVHLVELLVAHGAD 290
Cdd:cd22192    50 LGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 264-292 5.36e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 5.36e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1310163689 264 DGWEPLHAAAY-WGQVHLVELLVAHGADLN 292
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 75-132 6.66e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 6.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1310163689  75 LLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNA 132
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 264-292 7.26e-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: 36.85  E-value: 7.26e-04
                          10        20
                  ....*....|....*....|....*....
gi 1310163689 264 DGWEPLHAAAYWGQVHLVELLVAHGADLN 292
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 185-298 1.30e-03

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: 41.40  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689 185 CLETAMANqgiTQEGIEEArAVPELCMLNDLQNRLQ-AGANLSDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAKD- 262
Cdd:cd21882    29 CLHKAALN---LNDGVNEA-IMLLLEAAPDSGNPKElVNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARAt 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1310163689 263 ------------HDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVD 298
Cdd:cd21882   105 grffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD 152
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-263 1.61e-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: 36.11  E-value: 1.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1310163689 231 HGATLLHIAAA-NGFSEVATLLLEQGASLSAKDH 263
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-172 1.95e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1310163689 118 EMAQQLLDAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNSDGNM 172
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 82-163 3.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  82 NDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQ-EMAQQLLDAGADVNARDSECWTPLHAAatCGHLHLVELLISRG 160
Cdd:PHA02876  420 NPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYG 497


                  ...
gi 1310163689 161 ADL 163
Cdd:PHA02876  498 AEL 500
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-124 3.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLL 124
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-260 4.79e-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: 34.54  E-value: 4.79e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1310163689 231 HGATLLHIAAANGFSEVATLLLEQGASLSA 260
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 231-292 5.81e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 5.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310163689 231 HGATLLHIAAANGFSEVATLLLEQGASLSAK----------DHD----GWEPLHAAAYWGQVHLVELLVAHGADLN 292
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqGVDsfyhGESPLNAAACLGSPSIVALLSEDPADIL 202
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 74-132 6.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 6.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1310163689  74 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNA 132
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 72-163 7.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310163689  72 SVALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMAQQLLDAGADVNARDSECWTPLH-AAATCGHL 150
Cdd:PHA02878  169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDY 248

                          90
                  ....*....|...
gi 1310163689 151 HLVELLISRGADL 163
Cdd:PHA02878  249 DILKLLLEHGVDV 261
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 219-289 8.58e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.10  E-value: 8.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310163689 219 LQAGANL-SDPLDHGATLLHIAAANGFSEVATLLLEQ-GASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGA 289
Cdd:PHA02743   80 VNMGADInARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 103-132 8.81e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.81e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1310163689  103 DGLTALHQCCIDDFQEMAQQLLDAGADVNA 132
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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