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Conserved domains on  [gi|166795254|ref|NP_110443|]
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ankyrin repeat domain-containing protein 13C [Homo sapiens]

Protein Classification

GPCR_chapero_1 domain-containing protein( domain architecture ID 12790908)

GPCR_chapero_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 259-532 3.71e-79

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


:

Pssm-ID: 463391  Cd Length: 298  Bit Score: 250.25  E-value: 3.71e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  259 RLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDIYSATLSTKSIS 336
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  337 FTRAQTGWlFREDKTERVGNFLADFYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGNIMEQNFEPIR-------- 408
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  409 -RQSLTPPPQN--TITWEEYISAEngkaphlgRELvcKESKKTFKATIAMSQEFPLGIELLLNVLEVVA-PFKHFNKLRE 484
Cdd:pfam11904 160 tREESEAPPTNptALTPEEYFDPP--------KEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166795254  485 FVQMKLPPGFPVKLDIPVFPTITATVTFQEF---------------------RYDEFDGSIFTIPDDYK 532
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFeeldpveefstpikspergspSSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-199 4.90e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 4.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  94 LLAGTNPVAVVADGGScpahyPVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKV 172
Cdd:COG0666  107 LEAGADVNARDKDGET-----PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         90       100
                 ....*....|....*....|....*..
gi 166795254 173 KNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 259-532 3.71e-79

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 250.25  E-value: 3.71e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  259 RLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDIYSATLSTKSIS 336
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  337 FTRAQTGWlFREDKTERVGNFLADFYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGNIMEQNFEPIR-------- 408
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  409 -RQSLTPPPQN--TITWEEYISAEngkaphlgRELvcKESKKTFKATIAMSQEFPLGIELLLNVLEVVA-PFKHFNKLRE 484
Cdd:pfam11904 160 tREESEAPPTNptALTPEEYFDPP--------KEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166795254  485 FVQMKLPPGFPVKLDIPVFPTITATVTFQEF---------------------RYDEFDGSIFTIPDDYK 532
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFeeldpveefstpikspergspSSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-199 4.90e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 4.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  94 LLAGTNPVAVVADGGScpahyPVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKV 172
Cdd:COG0666  107 LEAGADVNARDKDGET-----PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         90       100
                 ....*....|....*....|....*..
gi 166795254 173 KNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-199 4.86e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  117 HECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 195
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 166795254  196 LLRK 199
Cdd:pfam12796  80 LLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-198 2.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 115 PVHECVFKGDVRRLSSLIRT----HNIGQKDnhGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDR 190
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                 ....*...
gi 166795254 191 QMITALLR 198
Cdd:PHA02875 149 KGIELLID 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-168 5.13e-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: 5.13e-05
                           10        20
                   ....*....|....*....|....*.
gi 166795254   143 HGNTPLHLAVMLGNKECAHLLLAHNA 168
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 122-199 6.42e-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: 42.31  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 122 KGDVRRLSSLIRTH--NIGQKDNHGNTPLHLAVMLGNKECAhLLLAHNAPVKVKNA------QGWSPLAEAISYGDRQMI 193
Cdd:cd22192   27 ENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGETALHIAVVNQNLNLV 105


                 ....*.
gi 166795254 194 TALLRK 199
Cdd:cd22192  106 RELIAR 111
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 259-532 3.71e-79

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 250.25  E-value: 3.71e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  259 RLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDIYSATLSTKSIS 336
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  337 FTRAQTGWlFREDKTERVGNFLADFYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGNIMEQNFEPIR-------- 408
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  409 -RQSLTPPPQN--TITWEEYISAEngkaphlgRELvcKESKKTFKATIAMSQEFPLGIELLLNVLEVVA-PFKHFNKLRE 484
Cdd:pfam11904 160 tREESEAPPTNptALTPEEYFDPP--------KEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166795254  485 FVQMKLPPGFPVKLDIPVFPTITATVTFQEF---------------------RYDEFDGSIFTIPDDYK 532
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFeeldpveefstpikspergspSSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-199 4.90e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 4.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  94 LLAGTNPVAVVADGGScpahyPVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKV 172
Cdd:COG0666  107 LEAGADVNARDKDGET-----PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         90       100
                 ....*....|....*....|....*..
gi 166795254 173 KNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-229 1.48e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  94 LLAGTNPVAVVADGGScpahyPVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKV 172
Cdd:COG0666  140 LEAGADVNAQDNDGNT-----PLHLAAANGNLEIVKLLLEAGaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 166795254 173 KNAQGWSPLAEAISYGDRQMITALLRKLKQQSRESVEEKRPRLLKALKELGDFYLEL 229
Cdd:COG0666  215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-199 4.86e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  117 HECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 195
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 166795254  196 LLRK 199
Cdd:pfam12796  80 LLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
131-199 6.59e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 6.59e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166795254 131 LIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666   74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
144-197 9.77e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 9.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166795254  144 GNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 197
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-223 1.22e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  148 LHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRKLKQQSRES--------VEEKRPRLLKAL 219
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgrtalhyaARSGHLEIVKLL 80


                  ....
gi 166795254  220 KELG 223
Cdd:pfam12796  81 LEKG 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-198 2.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 115 PVHECVFKGDVRRLSSLIRT----HNIGQKDnhGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDR 190
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                 ....*...
gi 166795254 191 QMITALLR 198
Cdd:PHA02875 149 KGIELLID 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-174 4.08e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 4.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  115 PVHECVFKGDVRRLSSLIRtHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKN 174
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-201 7.86e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  93 ALL-AGTNPVAVVADGGScpahyPVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPV 170
Cdd:COG0666  171 LLLeAGADVNARDNDGET-----PLHLAAENGHLEIVKLLLEAGaDVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                         90       100       110
                 ....*....|....*....|....*....|.
gi 166795254 171 KVKNAQGWSPLAEAISYGDRQMITALLRKLK 201
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-174 7.49e-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: 42.66  E-value: 7.49e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 166795254  143 HGNTPLHLAV-MLGNKECAHLLLAHNAPVKVKN 174
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 146-197 1.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 1.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166795254 146 TPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 197
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 140-197 2.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 2.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 166795254 140 KDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYgDRQMITALL 197
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI 242
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-184 3.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 166795254  136 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEA 184
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-197 4.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 116 VHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMIT 194
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGaDVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207


                 ...
gi 166795254 195 ALL 197
Cdd:PHA02874 208 LLI 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-168 5.13e-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: 5.13e-05
                           10        20
                   ....*....|....*....|....*.
gi 166795254   143 HGNTPLHLAVMLGNKECAHLLLAHNA 168
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-170 1.51e-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: 39.16  E-value: 1.51e-04
                          10        20
                  ....*....|....*....|....*...
gi 166795254  143 HGNTPLHLAVMLGNKECAHLLLAHNAPV 170
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 141-188 2.40e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 2.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 166795254 141 DNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYG 188
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-164 3.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166795254  115 PVHECVFKGDVRRLSSLI-RTHNIGQKDNHGNTPLHLAVMLGNKECAHLLL 164
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 79-228 4.46e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  79 PLHNSSVTANSQS-PALLAGTNPVAVVADGGSCPAHYPVhecVFKGDVRRLssLIRTHNIGQKDNHGNTPLHLAVMLG-N 156
Cdd:PHA02874 193 PLHNAAEYGDYACiKLLIDHGNHIMNKCKNGFTPLHNAI---IHNRSAIEL--LINNASINDQDIDGSTPLHHAINPPcD 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 157 KECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI------TALLRKLKQQSRES--VEEKRprlLKALKELGDFYLE 228
Cdd:PHA02874 268 IDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikdiiaNAVLIKEADKLKDSdfLEHIE---IKDNKEFSDFIKE 344
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 122-199 6.42e-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: 42.31  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 122 KGDVRRLSSLIRTH--NIGQKDNHGNTPLHLAVMLGNKECAhLLLAHNAPVKVKNA------QGWSPLAEAISYGDRQMI 193
Cdd:cd22192   27 ENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGETALHIAVVNQNLNLV 105


                 ....*.
gi 166795254 194 TALLRK 199
Cdd:cd22192  106 RELIAR 111
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-198 1.20e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 166795254 140 KDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 198
Cdd:PTZ00322 111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
131-199 1.99e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166795254 131 LIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-199 3.89e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254  96 AGTNPVAVVAdGGSCPAHYPVHECVFK-GDVRRLssLIRTHNIGQKDNHGNTPLHLAVMLGNKE-CAHLLLAhNAPVKVK 173
Cdd:PHA03095 211 AGCDPAATDM-LGNTPLHSMATGSSCKrSLVLPL--LIAGISINARNRYGQTPLHYAAVFNNPRaCRRLIAL-GADINAV 286

                         90       100
                 ....*....|....*....|....*.
gi 166795254 174 NAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:PHA03095 287 SSDGNTPLSLMVRNNNGRAVRAALAK 312
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 119-201 6.14e-03

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: 39.23  E-value: 6.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795254 119 CVFKGDVRRLssLIRTH-NIGQKDNHGNTPLHLAVMLGNKECA----HLLLAHNAPVK------VKNAQGWSPLAEAISY 187
Cdd:cd22192  145 CVGNEEIVRL--LIEHGaDIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKE 222

                         90
                 ....*....|....
gi 166795254 188 GDRQMITALLRKLK 201
Cdd:cd22192  223 GNIVMFQHLVQKRR 236
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 136-198 9.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 9.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166795254 136 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 198
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
 
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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