NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19353050|gb|AAH24900|]
View 

Ankyrin repeat domain 32 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-315 1.63e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 162 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 241
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19353050 242 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 315
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-315 1.63e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 162 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 241
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19353050 242 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 315
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-261 3.05e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   174 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 19353050   254 GKLLLQRG 261
Cdd:pfam12796  77 VKLLLEKG 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-262 6.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  161 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 222
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19353050  223 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 262
Cdd:PHA03100 211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 180-262 9.61e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 9.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 180 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 253
Cdd:cd22192  27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                ....*....
gi 19353050 254 GKLLLQRGG 262
Cdd:cd22192 105 VRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 204-232 4.76e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 4.76e-04
                           10        20
                   ....*....|....*....|....*....
gi 19353050    204 GWTPLHEACNYGNTECVQEILQRCPEVDL 232
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 160-388 6.75e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   160 KMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAgwtpLHEACN--YGNTE-CVQEILQRCPEVDLLTQV 236
Cdd:TIGR00870  42 KLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL----LHAISLeyVDAVEaILLHLLAAFRKSGPLELA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   237 D---------GVTPLHDALSNGHVEIGKLLLQRGGpellqqrnskgelpldyvlspkdkeelfaitniddtvdNFHAKTQ 307
Cdd:TIGR00870 118 NdqytseftpGITALHLAAHRQNYEIVKLLLERGA--------------------------------------SVPARAC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   308 KHFYHQQLEFGSFLLSRMLINF--C----SIFDLSSEF---ILAFKGLGhlNELLMACNSDTEASNAHT-------DWLL 371
Cdd:TIGR00870 160 GDFFVKSQGVDSFYHGESPLNAaaClgspSIVALLSEDpadILTADSLG--NTLLHLLVMENEFKAEYEelscqmyNFAL 237

                         250
                  ....*....|....*..
gi 19353050   372 DVYARnIKTLKKLPSVL 388
Cdd:TIGR00870 238 SLLDK-LRDSKELEVIL 253
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-315 1.63e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 162 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 241
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19353050 242 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 315
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
164-279 1.90e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 1.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 164 HKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLH 243
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLH 158

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19353050 244 DALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 279
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGAD--VNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-306 5.24e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 5.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 162 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 241
Cdd:COG0666 145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTA 222

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19353050 242 LHDALSNGHVEIGKLLLQRGGPELLQQRNSKGELPLDYVLSPKDKEELFAITNIDDTVDNFHAKT 306
Cdd:COG0666 223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-261 3.05e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   174 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 19353050   254 GKLLLQRG 261
Cdd:pfam12796  77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-279 1.74e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 157 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcpEVDLLTQ- 235
Cdd:COG0666  40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARd 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19353050 236 VDGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 279
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGAD--VNAQDNDGNTPLHL 159
Ank_2 pfam12796
Ankyrin repeats (3 copies);
162-232 5.35e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 5.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19353050   162 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpgIDINVKDNaGWTPLHEACNYGNTECVQEILQRCPEVDL 232
Cdd:pfam12796  22 DANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-262 6.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  161 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 222
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19353050  223 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 262
Cdd:PHA03100 211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 180-262 9.61e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 9.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 180 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 253
Cdd:cd22192  27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                ....*....
gi 19353050 254 GKLLLQRGG 262
Cdd:cd22192 105 VRELIARGA 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-258 1.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19353050   204 GWTPLHEACNYGNTECVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 258
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 166-260 5.53e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  166 TNLKGETALHRV-----CIKNQVEKLIIllslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVT 240
Cdd:PHA03095 218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                         90       100
                 ....*....|....*....|
gi 19353050  241 PLHDALSNGHVEIGKLLLQR 260
Cdd:PHA03095 293 PLSLMVRNNNGRAVRAALAK 312
Ank_4 pfam13637
Ankyrin repeats (many copies);
172-221 6.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 19353050   172 TALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQ 221
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLK 51
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 177-283 8.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  177 VCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKL 256
Cdd:PHA02874 163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHNRSAIELL 241

                         90       100
                 ....*....|....*....|....*..
gi 19353050  257 LLQRGgpelLQQRNSKGELPLDYVLSP 283
Cdd:PHA02874 242 INNAS----INDQDIDGSTPLHHAINP 264
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 178-279 4.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  178 CIKNQVEKLIILlslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 257
Cdd:PHA02874 101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176

                         90       100
                 ....*....|....*....|..
gi 19353050  258 LQRGGpeLLQQRNSKGELPLDY 279
Cdd:PHA02874 177 LEKGA--YANVKDNNGESPLHN 196
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 166-231 4.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 4.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19353050  166 TNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVD 231
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
223-280 5.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 5.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19353050   223 ILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRGGPELLqqRNSKGELPLDYV 280
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL--KDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 165-261 6.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  165 KTNLKGETALHRVCiKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVdGVTPLHD 244
Cdd:PHA02878 163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                         90
                 ....*....|....*...
gi 19353050  245 ALSN-GHVEIGKLLLQRG 261
Cdd:PHA02878 241 SVGYcKDYDILKLLLEHG 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-279 1.18e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050 157 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQv 236
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD- 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19353050 237 DGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 279
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKDGETPLHL 126
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 188-258 1.86e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19353050  188 ILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLL 258
Cdd:PTZ00322 100 ILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
161-211 1.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19353050   161 MNFHKTNLKGETALHRVCIKNQVEKLIILLsLPGIDINVKDNAGWTPLHEA 211
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
189-243 4.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 4.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19353050   189 LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcPEVDLLTQVDGVTPLH 243
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 182-297 4.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  182 QVEKLII--LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQ 259
Cdd:PHA02876 154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIID 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 19353050  260 RggpellQQRNSKGELPLDYVLSPKDKEEL-------FAITNIDD 297
Cdd:PHA02876 233 N------RSNINKNDLSLLKAIRNEDLETSlllydagFSVNSIDD 271
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 204-232 4.76e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 4.76e-04
                           10        20
                   ....*....|....*....|....*....
gi 19353050    204 GWTPLHEACNYGNTECVQEILQRCPEVDL 232
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 171-287 5.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  171 ETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGH 250
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGD 147

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19353050  251 VEIGKLLLQRGGpeLLQQRNSKGELPLDYVLSPKDKE 287
Cdd:PHA02875 148 IKGIELLIDHKA--CLDIEDCCGCTPLIIAMAKGDIA 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 194-259 7.63e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 7.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19353050  194 GIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLLLQ 259
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH-IRDANGNTALWNAISAKHHKIFRILYH 612
PHA03095 PHA03095
ankyrin-like protein; Provisional
 170-261 9.15e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 9.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  170 GETALHrVCIKNQVEKL--IILLSL-PGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCpEVDLLTQVD-GVTPLHDA 245
Cdd:PHA03095  47 GKTPLH-LYLHYSSEKVkdIVRLLLeAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA-GADVNAKDKvGRTPLHVY 124

                         90
                 ....*....|....*...
gi 19353050  246 LSNG--HVEIGKLLLQRG 261
Cdd:PHA03095 125 LSGFniNPKVIRLLLRKG 142
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 179-261 1.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  179 IKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNY--GNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHV--EIG 254
Cdd:PHA03100  81 NLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN-SDGENLLHLYLESNKIdlKIL 159


                 ....*..
gi 19353050  255 KLLLQRG 261
Cdd:PHA03100 160 KLLIDKG 166
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-231 2.32e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.32e-03
                          10        20
                  ....*....|....*....|....*...
gi 19353050   204 GWTPLHEACNYGNTECVQEILQRCPEVD 231
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 186-261 2.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 2.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19353050  186 LIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRG 261
Cdd:PHA02875  50 AIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG 125
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-234 2.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 2.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19353050   204 GWTPLHEAC-NYGNTECVQEILQRCPEVDLLT 234
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 172-261 3.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  172 TALHRVCIKNQVeKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHV 251
Cdd:PHA02875 137 SPLHLAVMMGDI-KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215

                         90
                 ....*....|
gi 19353050  252 EIGKLLLQRG 261
Cdd:PHA02875 216 DIVRLFIKRG 225
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 174-282 4.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  174 LHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYG-NTECVQEIlqrcpeVDLLTQ---------VDGVTPLH 243
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDN-GADINSSTKNNSTPLHYLSNIKyNLTDVKEI------VKLLLEyganvnapdNNGITPLL 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19353050  244 DALSN--GHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLS 282
Cdd:PHA03100 112 YAISKksNSYSIVEYLLDNGAN--VNIKNSDGENLLHLYLE 150
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 160-388 6.75e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   160 KMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAgwtpLHEACN--YGNTE-CVQEILQRCPEVDLLTQV 236
Cdd:TIGR00870  42 KLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL----LHAISLeyVDAVEaILLHLLAAFRKSGPLELA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   237 D---------GVTPLHDALSNGHVEIGKLLLQRGGpellqqrnskgelpldyvlspkdkeelfaitniddtvdNFHAKTQ 307
Cdd:TIGR00870 118 NdqytseftpGITALHLAAHRQNYEIVKLLLERGA--------------------------------------SVPARAC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050   308 KHFYHQQLEFGSFLLSRMLINF--C----SIFDLSSEF---ILAFKGLGhlNELLMACNSDTEASNAHT-------DWLL 371
Cdd:TIGR00870 160 GDFFVKSQGVDSFYHGESPLNAaaClgspSIVALLSEDpadILTADSLG--NTLLHLLVMENEFKAEYEelscqmyNFAL 237

                         250
                  ....*....|....*..
gi 19353050   372 DVYARnIKTLKKLPSVL 388
Cdd:TIGR00870 238 SLLDK-LRDSKELEVIL 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 170-261 7.29e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19353050  170 GETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNT-ECVQEILQRcPEVDL-LTQVDGVTPLHDALS 247
Cdd:PHA03095  83 GFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNInPKVIRLLLR-KGADVnALDLYGMTPLAVLLK 161

                         90
                 ....*....|....*.
gi 19353050  248 NGHVEIG--KLLLQRG 261
Cdd:PHA03095 162 SRNANVEllRLLIDAG 177
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH