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Conserved domains on  [gi|1678759271|ref|XP_029284867|]
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ankyrin repeat domain-containing protein 13C-like [Cottoperca gobio]

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 ...
 243-516 2.49e-78

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: 247.55  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 243 RLDTTLIDFTDMKCQRGDLSFIFNGNAIPAESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDVYSATLSTKSIT 320
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 321 FSRAQTGWlFREDKTERVGNFLADFYSVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGNLIEQNFEPAR-------- 392
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 393 -RQSLTAP--SPNTISWEEYitadngkaPHLGRELvcKESKKNFKATIAMSQEFPLGIESLLNVLEVIA-PFKHFNKLRE 468
Cdd:pfam11904 160 tREESEAPptNPTALTPEEY--------FDPPKEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678759271 469 FVQMKLPPGFPVKLDIPVFPTITATVTFQEF---------------------RYDEFDQSIFTIPNDYK 516
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFeeldpveefstpikspergspSSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-183 4.83e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  83 IDDNNKNPIIRTgqdfPVHECVFKGDVRRLSSLIRTQ-NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQG 161
Cdd:COG0666   111 ADVNARDKDGET----PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100
                  ....*....|....*....|..
gi 1678759271 162 WSPLAEAISYGDRQMITALLRK 183
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 243-516 2.49e-78

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: 247.55  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 243 RLDTTLIDFTDMKCQRGDLSFIFNGNAIPAESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDVYSATLSTKSIT 320
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 321 FSRAQTGWlFREDKTERVGNFLADFYSVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGNLIEQNFEPAR-------- 392
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 393 -RQSLTAP--SPNTISWEEYitadngkaPHLGRELvcKESKKNFKATIAMSQEFPLGIESLLNVLEVIA-PFKHFNKLRE 468
Cdd:pfam11904 160 tREESEAPptNPTALTPEEY--------FDPPKEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678759271 469 FVQMKLPPGFPVKLDIPVFPTITATVTFQEF---------------------RYDEFDQSIFTIPNDYK 516
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFeeldpveefstpikspergspSSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-183 4.83e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  83 IDDNNKNPIIRTgqdfPVHECVFKGDVRRLSSLIRTQ-NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQG 161
Cdd:COG0666   111 ADVNARDKDGET----PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100
                  ....*....|....*....|..
gi 1678759271 162 WSPLAEAISYGDRQMITALLRK 183
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-183 1.50e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 101 HECVFKGDVRRLSSLIRT-QNISQKDVHGNTPLHLAVMMGHKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 179
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENgADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 1678759271 180 LLRK 183
Cdd:pfam12796  80 LLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-182 5.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  86 NNKNPIIRTgqdfPVHECVFKGDVRRLSSLIRTqNISQKDV---HGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGW 162
Cdd:PHA02875   62 DVKYPDIES----ELHDAVEEGDVKAVEELLDL-GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136

                          90       100
                  ....*....|....*....|
gi 1678759271 163 SPLAEAISYGDRQMITALLR 182
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLID 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 127-152 9.77e-06

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: 42.19  E-value: 9.77e-06
                           10        20
                   ....*....|....*....|....*.
gi 1678759271  127 HGNTPLHLAVMMGHKECAHLLLAHNA 152
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-183 4.43e-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: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  92 IRTGQDFPVHECVFKGDVRRLSSLIRTQ--NISQKDVHGNTPLHLAVMMGHKECAhLLLAHNAPVKVKNA------QGWS 163
Cdd:cd22192    13 QKRISESPLLLAAKENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGET 91

                          90       100
                  ....*....|....*....|
gi 1678759271 164 PLAEAISYGDRQMITALLRK 183
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIAR 111
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 243-516 2.49e-78

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: 247.55  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 243 RLDTTLIDFTDMKCQRGDLSFIFNGNAIPAESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDVYSATLSTKSIT 320
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 321 FSRAQTGWlFREDKTERVGNFLADFYSVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGNLIEQNFEPAR-------- 392
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 393 -RQSLTAP--SPNTISWEEYitadngkaPHLGRELvcKESKKNFKATIAMSQEFPLGIESLLNVLEVIA-PFKHFNKLRE 468
Cdd:pfam11904 160 tREESEAPptNPTALTPEEY--------FDPPKEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678759271 469 FVQMKLPPGFPVKLDIPVFPTITATVTFQEF---------------------RYDEFDQSIFTIPNDYK 516
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFeeldpveefstpikspergspSSCEIDDDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-183 4.83e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  83 IDDNNKNPIIRTgqdfPVHECVFKGDVRRLSSLIRTQ-NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQG 161
Cdd:COG0666   111 ADVNARDKDGET----PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100
                  ....*....|....*....|..
gi 1678759271 162 WSPLAEAISYGDRQMITALLRK 183
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-213 2.20e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  83 IDDNNKNPIIRTgqdfPVHECVFKGDVRRLSSLI-RTQNISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQG 161
Cdd:COG0666   144 ADVNAQDNDGNT----PLHLAAANGNLEIVKLLLeAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1678759271 162 WSPLAEAISYGDRQMITALLRKLKQQSRETVEDKRPKLLKALKELGDFYLEL 213
Cdd:COG0666   220 KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-183 1.50e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 101 HECVFKGDVRRLSSLIRT-QNISQKDVHGNTPLHLAVMMGHKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 179
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENgADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 1678759271 180 LLRK 183
Cdd:pfam12796  80 LLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
120-183 2.80e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 2.80e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678759271 120 NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 183
Cdd:COG0666    79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
128-181 1.61e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678759271 128 GNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 181
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
132-190 3.18e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 3.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678759271 132 LHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRKLKQQSRE 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD 59
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-182 5.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  86 NNKNPIIRTgqdfPVHECVFKGDVRRLSSLIRTqNISQKDV---HGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGW 162
Cdd:PHA02875   62 DVKYPDIES----ELHDAVEEGDVKAVEELLDL-GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136

                          90       100
                  ....*....|....*....|
gi 1678759271 163 SPLAEAISYGDRQMITALLR 182
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLID 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
99-158 5.40e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 5.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  99 PVHECVFKGDVRRLSSLIRTQNISQKDvHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKN 158
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 127-158 1.10e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 1.10e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1678759271 127 HGNTPLHLAV-MMGHKECAHLLLAHNAPVKVKN 158
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-185 4.35e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  84 DDNNKNPIIRTgqdfPVHECVFKGDVRRLSSLIRTQ-NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGW 162
Cdd:COG0666   178 DVNARDNDGET----PLHLAAENGHLEIVKLLLEAGaDVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                          90       100
                  ....*....|....*....|...
gi 1678759271 163 SPLAEAISYGDRQMITALLRKLK 185
Cdd:COG0666   254 TALLLAAAAGAALIVKLLLLALL 276
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 127-152 9.77e-06

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: 42.19  E-value: 9.77e-06
                           10        20
                   ....*....|....*....|....*.
gi 1678759271  127 HGNTPLHLAVMMGHKECAHLLLAHNA 152
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-181 1.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  83 IDDNNKNPIIRTGqdfpVHECVFKGDVRRLSSLIRTQ-NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQG 161
Cdd:PHA02874  115 IDVNIKDAELKTF----LHYAIKKGDLESIKMLFEYGaDVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                          90       100
                  ....*....|....*....|
gi 1678759271 162 WSPLAEAISYGDRQMITALL 181
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLI 210
Ank_4 pfam13637
Ankyrin repeats (many copies);
99-148 2.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1678759271  99 PVHECVFKGDVRRLSSLI-RTQNISQKDVHGNTPLHLAVMMGHKECAHLLL 148
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-172 3.13e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 3.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1678759271 125 DVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYG 172
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 124-182 5.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 5.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678759271 124 KDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 182
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 127-154 8.98e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 8.98e-05
                          10        20
                  ....*....|....*....|....*...
gi 1678759271 127 HGNTPLHLAVMMGHKECAHLLLAHNAPV 154
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-168 1.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1678759271 120 NISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEA 168
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 99-181 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  99 PVHECVFKGDVRRLSSLI-RTQNISQKDVHGNTPLHLAVMmgHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYG-DRQM 176
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIdHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDI 270


                  ....*
gi 1678759271 177 ITALL 181
Cdd:PHA02874  271 IDILL 275
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-183 4.43e-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: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271  92 IRTGQDFPVHECVFKGDVRRLSSLIRTQ--NISQKDVHGNTPLHLAVMMGHKECAhLLLAHNAPVKVKNA------QGWS 163
Cdd:cd22192    13 QKRISESPLLLAAKENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGET 91

                          90       100
                  ....*....|....*....|
gi 1678759271 164 PLAEAISYGDRQMITALLRK 183
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIAR 111
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 124-181 7.53e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 7.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1678759271 124 KDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYgDRQMITALL 181
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI 242
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 115-212 2.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678759271 115 LIRTQNISQKDVHGNTPLHLAVMMG-HKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI-------TALLRKLKQ 186
Cdd:PHA02874  241 LINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikdiianAVLIKEADK 320

                          90       100
                  ....*....|....*....|....*.
gi 1678759271 187 QSRETVEDKrpKLLKALKELGDFYLE 212
Cdd:PHA02874  321 LKDSDFLEH--IEIKDNKEFSDFIKE 344
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-183 4.84e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.17  E-value: 4.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678759271 115 LIRTQNISQKDVHGNTPLHLAVMMGHKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 183
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
 
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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