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Conserved domains on  [gi|313851097|ref|NP_001186499|]
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CAP-Gly domain-containing linker protein 3 [Homo sapiens]

Protein Classification

CAP-Gly domain-containing linker protein; CAP-Gly domain-containing protein( domain architecture ID 12790878)

CAP-Gly domain-containing linker protein functions as a cytoplasmic linker protein; CAP-Gly domain-containing protein similar to human dynactin-1 and Saccharomyces cerevisiae nuclear fusion protein BIK1; CAP-Gly domains serve as recognition domains for EEY/F-COO(-) motifs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 418-482 1.14e-33

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 122.13  E-value: 1.14e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313851097  418 VGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVFAPASRI 482
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 296-360 1.03e-31

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 116.73  E-value: 1.03e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313851097  296 LGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKI 360
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-235 1.04e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 101 NEILRRGCHVNDRDGLtDMTLLHYACKAGAhgvgdpAAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYFDVPDLVRVL 180
Cdd:COG0666  104 KLLLEAGADVNARDKD-GETPLHLAAYNGN------LEIVKL---LLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLL 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313851097 181 LK-GARPRVVNStcsdfNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPA 235
Cdd:COG0666  173 LEaGADVNARDN-----DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 418-482 1.14e-33

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 122.13  E-value: 1.14e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313851097  418 VGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVFAPASRI 482
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 296-360 1.03e-31

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 116.73  E-value: 1.03e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313851097  296 LGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKI 360
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 418-483 2.19e-27

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 104.59  E-value: 2.19e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313851097   418 VGDQVLVAG-QKQGIVRFYGKTDFAPGYWYGIELDQPT-GKHDGSVFGVRYFTCPPRHGVFAPASRIQ 483
Cdd:smart01052   1 VGDRVEVGGgGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 296-361 7.79e-27

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 103.05  E-value: 7.79e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313851097   296 LGDRVLL-DGQKTGTLRFCGTTEFASGQWVGVELDEPE-GKNDGSVGGVRYFICPPKQGLFASVSKIS 361
Cdd:smart01052   1 VGDRVEVgGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 418-476 6.31e-19

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 90.51  E-value: 6.31e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 313851097 418 VGDQVLVAGQKqGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVF 476
Cdd:COG5244    6 VNDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-235 1.04e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 101 NEILRRGCHVNDRDGLtDMTLLHYACKAGAhgvgdpAAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYFDVPDLVRVL 180
Cdd:COG0666  104 KLLLEAGADVNARDKD-GETPLHLAAYNGN------LEIVKL---LLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLL 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313851097 181 LK-GARPRVVNStcsdfNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPA 235
Cdd:COG0666  173 LEaGADVNARDN-----DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 294-354 1.27e-17

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 86.28  E-value: 1.27e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313851097 294 LRLGDRVLLDGQKtGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLF 354
Cdd:COG5244    4 LSVNDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-228 3.57e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097  122 LHYACKAGAHgvgdpaAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYFDVPDLVRVLLKGARPRVVNstcsdfNHGSA 201
Cdd:pfam12796   1 LHLAAKNGNL------ELVKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD------NGRTA 64

                          90       100
                  ....*....|....*....|....*..
gi 313851097  202 LHIAASSLCLGAAKCLLEHGANPALRN 228
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 95-237 8.89e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 8.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097  95 KIDVIgNEILRRGCHVNDRDGLtDMTLLHYAckaGAHGVGDPAAAVRLsqqLLALGADVTLRSRwTNMNALHYAAYFD-V 173
Cdd:PHA03095  26 TVEEV-RRLLAAGADVNFRGEY-GKTPLHLY---LHYSSEKVKDIVRL---LLEAGADVNAPER-CGFTPLHLYLYNAtT 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313851097 174 PDLVRVLLK-GARprvVNStcSDFNHGSALHIAASSLCL--GAAKCLLEHGANPALRNRKGQVPAEV 237
Cdd:PHA03095  97 LDVIKLLIKaGAD---VNA--KDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAV 158
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 164-222 9.66e-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: 38.84  E-value: 9.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313851097 164 ALHYAAYFDVPDLVRVLLKGArPRVVNSTC-SDFNHG-SALHIAASSLCLGAAKCLLEHGA 222
Cdd:cd22192   54 ALHVAALYDNLEAAVVLMEAA-PELVNEPMtSDLYQGeTALHIAVVNQNLNLVRELIARGA 113
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 418-482 1.14e-33

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 122.13  E-value: 1.14e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313851097  418 VGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVFAPASRI 482
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 296-360 1.03e-31

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 116.73  E-value: 1.03e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313851097  296 LGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKI 360
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 418-483 2.19e-27

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 104.59  E-value: 2.19e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313851097   418 VGDQVLVAG-QKQGIVRFYGKTDFAPGYWYGIELDQPT-GKHDGSVFGVRYFTCPPRHGVFAPASRIQ 483
Cdd:smart01052   1 VGDRVEVGGgGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 296-361 7.79e-27

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 103.05  E-value: 7.79e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313851097   296 LGDRVLL-DGQKTGTLRFCGTTEFASGQWVGVELDEPE-GKNDGSVGGVRYFICPPKQGLFASVSKIS 361
Cdd:smart01052   1 VGDRVEVgGGGRRGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 418-476 6.31e-19

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 90.51  E-value: 6.31e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 313851097 418 VGDQVLVAGQKqGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVF 476
Cdd:COG5244    6 VNDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-235 1.04e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 101 NEILRRGCHVNDRDGLtDMTLLHYACKAGAhgvgdpAAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYFDVPDLVRVL 180
Cdd:COG0666  104 KLLLEAGADVNARDKD-GETPLHLAAYNGN------LEIVKL---LLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLL 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313851097 181 LK-GARPRVVNStcsdfNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPA 235
Cdd:COG0666  173 LEaGADVNARDN-----DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 294-354 1.27e-17

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 86.28  E-value: 1.27e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313851097 294 LRLGDRVLLDGQKtGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLF 354
Cdd:COG5244    4 LSVNDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-234 3.13e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097  92 VQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAhgvgdpAAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYF 171
Cdd:COG0666   61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD------LEIVKL---LLEAGADVNARDKD-GETPLHLAAYN 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313851097 172 DVPDLVRVLL-KGARprvVNSTcsDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVP 234
Cdd:COG0666  131 GNLEIVKLLLeAGAD---VNAQ--DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
104-256 8.69e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 8.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 104 LRRGCHVNDRDGlTDMTLLHYACKAGAhgvgdpAAAVRLsqqLLALGADVTLRSRwTNMNALHYAAYFDVPDLVRVLL-K 182
Cdd:COG0666  140 LEAGADVNAQDN-DGNTPLHLAAANGN------LEIVKL---LLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLeA 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313851097 183 GARPRVVNStcsdfNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAK 256
Cdd:COG0666  209 GADVNAKDN-----DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-228 3.57e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097  122 LHYACKAGAHgvgdpaAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYFDVPDLVRVLLKGARPRVVNstcsdfNHGSA 201
Cdd:pfam12796   1 LHLAAKNGNL------ELVKL---LLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD------NGRTA 64

                          90       100
                  ....*....|....*....|....*..
gi 313851097  202 LHIAASSLCLGAAKCLLEHGANPALRN 228
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
104-231 4.33e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 104 LRRGCHVNDRDGLtDMTLLHYACKAGAhgvgdpAAAVRLsqqLLALGADVTLRSRWtNMNALHYAAYFDVPDLVRVLLKG 183
Cdd:COG0666  173 LEAGADVNARDND-GETPLHLAAENGH------LEIVKL---LLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEA 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 313851097 184 ARPRVVNstcsDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKG 231
Cdd:COG0666  242 GADLNAK----DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 95-237 8.89e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 8.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097  95 KIDVIgNEILRRGCHVNDRDGLtDMTLLHYAckaGAHGVGDPAAAVRLsqqLLALGADVTLRSRwTNMNALHYAAYFD-V 173
Cdd:PHA03095  26 TVEEV-RRLLAAGADVNFRGEY-GKTPLHLY---LHYSSEKVKDIVRL---LLEAGADVNAPER-CGFTPLHLYLYNAtT 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313851097 174 PDLVRVLLK-GARprvVNStcSDFNHGSALHIAASSLCL--GAAKCLLEHGANPALRNRKGQVPAEV 237
Cdd:PHA03095  97 LDVIKLLIKaGAD---VNA--KDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 146-234 2.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 146 LLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLL-KGARPRVVNSTcsdfnHGSALHIAASSLCLGAAKCLLEHGANP 224
Cdd:PHA02878 153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLsYGANVNIPDKT-----NNSPLHHAVKHYNKPIVHILLENGAST 227

                         90
                 ....*....|
gi 313851097 225 ALRNRKGQVP 234
Cdd:PHA02878 228 DARDKCGNTP 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-190 5.95e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 5.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097  101 NEILRRGCHVNDRDGlTDMTLLHYACKAGAHgvgdpaAAVRLsqqLLALgadVTLRSRWTNMNALHYAAYFDVPDLVRVL 180
Cdd:pfam12796  14 KLLLENGADANLQDK-NGRTALHLAAKNGHL------EIVKL---LLEH---ADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 313851097  181 L-KGARPRVVN 190
Cdd:pfam12796  81 LeKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 177-237 2.50e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 2.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313851097 177 VRVLLKGArprvVNSTCSDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPAEV 237
Cdd:PTZ00322  98 ARILLTGG----ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 101-234 2.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 101 NEILRRGCHVNDRDGLTDmTLLHYACKAGAhgvgdpaaaVRLSQQLLALGADVTLRSRWTNMnALHYAAYFDVPDLVRVL 180
Cdd:PHA02874 108 KTILDCGIDVNIKDAELK-TFLHYAIKKGD---------LESIKMLFEYGADVNIEDDNGCY-PIHIAIKHNFFDIIKLL 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 313851097 181 L-KGARPRVvnstcSDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVP 234
Cdd:PHA02874 177 LeKGAYANV-----KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-192 2.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 102 EILRRGCHVNDRDGLtDMTLLHYA-----CKAGahgvgdpaaavrLSQQLLALGADVTLRSRWtNMNALHYAAYFDVPDL 176
Cdd:PHA03095 207 ELIRAGCDPAATDML-GNTPLHSMatgssCKRS------------LVLPLLIAGISINARNRY-GQTPLHYAAVFNNPRA 272

                         90
                 ....*....|....*..
gi 313851097 177 VRVLLK-GARPRVVNST 192
Cdd:PHA03095 273 CRRLIAlGADINAVSSD 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
161-218 2.71e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 313851097  161 NMNALHYAAYFDVPDLVRVLL-KGARPRVVNStcsdfNHGSALHIAASSLCLGAAKCLL 218
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLeKGADINAVDG-----NGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-234 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851097 146 LLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGArprvVNSTCSDFNHGSALHIAASSLCLGAAKCLLEHGANPA 225
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114


                 ....*....
gi 313851097 226 LRNRKGQVP 234
Cdd:COG0666  115 ARDKDGETP 123
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 164-222 9.66e-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: 38.84  E-value: 9.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313851097 164 ALHYAAYFDVPDLVRVLLKGArPRVVNSTC-SDFNHG-SALHIAASSLCLGAAKCLLEHGA 222
Cdd:cd22192   54 ALHVAALYDNLEAAVVLMEAA-PELVNEPMtSDLYQGeTALHIAVVNQNLNLVRELIARGA 113
 
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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