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Conserved domains on  [gi|109940213|sp|Q15327|]
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RecName: Full=Ankyrin repeat domain-containing protein 1; AltName: Full=Cardiac ankyrin repeat protein; AltName: Full=Cytokine-inducible gene C-193 protein; AltName: Full=Cytokine-inducible nuclear protein

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

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-291 7.46e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 122 PTFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDV 201
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 202 LKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIK 281
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170
                 ....*....|
gi 109940213 282 NCAGKTPMDL 291
Cdd:COG0666  216 DNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-291 7.46e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 122 PTFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDV 201
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 202 LKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIK 281
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170
                 ....*....|
gi 109940213 282 NCAGKTPMDL 291
Cdd:COG0666  216 DNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
190-282 6.55e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 6.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  190 IHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIAcEADLNAKDrEGDTPLHDAVRLNRYKMIR 269
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 109940213  270 LLIMYGADLNIKN 282
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-289 7.59e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 7.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 150 DEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRT 229
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 230 GHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRyKMIRLLImYGADLNIKNCAGKTPM 289
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPL 258
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-291 5.24e-13

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: 69.27  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 120 DVPTFLkAALENKLPVVEKFLSdknNPDvCDEYKR-----TALHRACLEGHLAIVEKLMEAGAQIEFRDMLES-----TA 189
Cdd:cd22192   18 ESPLLL-AAKENDVQAIKKLLK---CPS-CDLFQRgalgeTALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgeTA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 190 IHWASRGGNLDVLKLLLNKGAK-ISAR----------DKLLSTALHV---AVRTGHYECAEHLIACEADLNAKDREGDTP 255
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpKNLIYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 109940213 256 LHDAV----RLNRYKMIRLLIMYGADLN------IKNCAGKTPMDL 291
Cdd:cd22192  173 LHILVlqpnKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKL 218
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 159-283 6.89e-06

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: 47.77  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  159 RACLEGHLAIVEKLMEAGA--QIEFRDML-ESTAIHWASRGGNLDVLKLLLNKGAKISARDkllsTALHVAVRTGH---Y 232
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKklNINCPDRLgRSALFVAAIENENLELTELLLNLSCRGAVGD----TLLHAISLEYVdavE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109940213  233 ECAEHLIACEADLN----AKDREGD------TPLHDAVRLNRYKMIRLLIMYGADLNIKNC 283
Cdd:TIGR00870  99 AILLHLLAAFRKSGplelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARAC 159
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 251-280 1.03e-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: 38.72  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 109940213   251 EGDTPLHDAVRLNRYKMIRLLIMYGADLNI 280
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-291 7.46e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 122 PTFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDV 201
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 202 LKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIK 281
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170
                 ....*....|
gi 109940213 282 NCAGKTPMDL 291
Cdd:COG0666  216 DNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-297 7.32e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 7.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 124 FLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLK 203
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNC 283
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        170
                 ....*....|....
gi 109940213 284 AGKTPMDLVLHWQN 297
Cdd:COG0666  251 DGLTALLLAAAAGA 264
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-309 9.89e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 9.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 124 FLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLK 203
Cdd:COG0666   25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNC 283
Cdd:COG0666  105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                        170       180
                 ....*....|....*....|....*...
gi 109940213 284 AGKTPmdlvLHW--QNGTKAIFDSLREN 309
Cdd:COG0666  185 DGETP----LHLaaENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
127-289 7.13e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 7.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 127 AALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLL 206
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 207 NKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGK 286
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                 ...
gi 109940213 287 TPM 289
Cdd:COG0666  287 TLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
190-282 6.55e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 6.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  190 IHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIAcEADLNAKDrEGDTPLHDAVRLNRYKMIR 269
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 109940213  270 LLIMYGADLNIKN 282
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
133-295 7.00e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 7.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 133 LPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKI 212
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 213 SARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPmdlv 292
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP---- 156


                 ...
gi 109940213 293 LHW 295
Cdd:COG0666  157 LHL 159
Ank_2 pfam12796
Ankyrin repeats (3 copies);
157-249 1.85e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  157 LHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKgAKISARDKLLsTALHVAVRTGHYECAE 236
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 109940213  237 HLIACEADLNAKD 249
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-289 7.59e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 7.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 150 DEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRT 229
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 230 GHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRyKMIRLLImYGADLNIKNCAGKTPM 289
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
127-216 4.00e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  127 AALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEaGAQIEFRDMLEsTAIHWASRGGNLDVLKLLL 206
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 109940213  207 NKGAKISARD 216
Cdd:pfam12796  82 EKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 120-297 5.58e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 120 DVPTFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRAC-LEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGN 198
Cdd:PHA02876 308 ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 199 LDVLKLLLNKGAKISARDKLLSTALHVAV-RTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLN-RYKMIRLLIMYGA 276
Cdd:PHA02876 388 VVIINTLLDYGADIEALSQKIGTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467

                        170       180
                 ....*....|....*....|.
gi 109940213 277 DLNIKNCAGKTPMDLVLHWQN 297
Cdd:PHA02876 468 DVNAINIQNQYPLLIALEYHG 488
PHA03095 PHA03095
ankyrin-like protein; Provisional
 166-293 6.13e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 166 LAIVEKLMEAGAQIEFRDMLESTAIHWASRGGN---LDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYE-CAEHLIAC 241
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109940213 242 EADLNAKDREGDTPLHdaVRLN----RYKMIRLLIMYGADLNIKNCAGKTPMDLVL 293
Cdd:PHA03095 107 GADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLL 160
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 126-288 2.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 2.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 126 KAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLE--GHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGG--NLDV 201
Cdd:PHA03100  79 KYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKI 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 202 LKLLLNKGAKISARDKLlstalhvavrtghyecaEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIK 281
Cdd:PHA03100 159 LKLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221


                 ....*..
gi 109940213 282 NCAGKTP 288
Cdd:PHA03100 222 NKYGDTP 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 161-289 5.14e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 5.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 161 CLEGHLaiVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIA 240
Cdd:PHA02874 101 CIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 109940213 241 CEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPM 289
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 131-298 6.15e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 6.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 131 NKLPVVEKFLSDKNNPDVCDEYKRTALHrACLEG---HLAIVEKLMEAGAQIEFRDMLESTAIHW--ASRGGNLDVLKLL 205
Cdd:PHA03095  95 TTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 206 LNKGAKISARDKLLSTALHV----------------------AVRTGHYECAEH---------------LIACEADLNAK 248
Cdd:PHA03095 174 IDAGADVYAVDDRFRSLLHHhlqsfkprarivreliragcdpAATDMLGNTPLHsmatgssckrslvlpLLIAGISINAR 253

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109940213 249 DREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPMDLVLHWQNG 298
Cdd:PHA03095 254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 143-300 7.28e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 143 KNNPDVCDEYKRTALHRACLEGHlaIVEKLMEAGAQIEFRDM-LESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLST 221
Cdd:PHA02878 126 KNIQTIDLVYIDKKSKDDIIEAE--ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 222 ALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAV-RLNRYKMIRLLIMYGADLNIKNCA-GKTPMDLVLHWQNGT 299
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERKL 283


                 .
gi 109940213 300 K 300
Cdd:PHA02878 284 K 284
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 133-289 1.59e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 133 LPVVEKFLSDKNN-PDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLL------ 205
Cdd:PHA02874  14 IEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvd 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 206 -----------------LNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMI 268
Cdd:PHA02874  94 tsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII 173

                        170       180
                 ....*....|....*....|.
gi 109940213 269 RLLIMYGADLNIKNCAGKTPM 289
Cdd:PHA02874 174 KLLLEKGAYANVKDNNGESPL 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-291 5.24e-13

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: 69.27  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 120 DVPTFLkAALENKLPVVEKFLSdknNPDvCDEYKR-----TALHRACLEGHLAIVEKLMEAGAQIEFRDMLES-----TA 189
Cdd:cd22192   18 ESPLLL-AAKENDVQAIKKLLK---CPS-CDLFQRgalgeTALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgeTA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 190 IHWASRGGNLDVLKLLLNKGAK-ISAR----------DKLLSTALHV---AVRTGHYECAEHLIACEADLNAKDREGDTP 255
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpKNLIYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 109940213 256 LHDAV----RLNRYKMIRLLIMYGADLN------IKNCAGKTPMDL 291
Cdd:cd22192  173 LHILVlqpnKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKL 218
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 154-293 1.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 154 RTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAV-RTGHY 232
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDY 248

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109940213 233 ECAEHLIACEADLNAKDR-EGDTPLHDAVRLNRykMIRLLIMYGADLNIKNCAGKTPMDLVL 293
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 166-293 3.21e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 166 LAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHY-----ECAEHLIA 240
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109940213 241 CEADLNAKDREGDTPLHDAV--RLNRYKMIRLLIMYGADLNIKNCAGKTPMDLVL 293
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 123-306 5.90e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 5.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 123 TFLKAALEN-KLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDV 201
Cdd:PHA02874 126 TFLHYAIKKgDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 202 LKLLLNKGAKISARDKLLSTALHVAVRtgHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYK-MIRLLIMYGADLNI 280
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISI 283

                        170       180
                 ....*....|....*....|....*.
gi 109940213 281 KNCAGKTPMDLVLHWQNGTKAIFDSL 306
Cdd:PHA02874 284 KDNKGENPIDTAFKYINKDPVIKDII 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 123-289 7.84e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 7.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 123 TFLKAALENKLPVVEKFL---SDKNNPDVCDEykrTALH-RACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGN 198
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLeagADVNAPERCGF---TPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 199 LD--VLKLLLNKGAKISARDKLLSTALHVAVRTGH--YECAEHLIACEADLNAKDREGDTPLH---DAVRlNRYKMIRLL 271
Cdd:PHA03095 130 INpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHhhlQSFK-PRARIVREL 208

                        170
                 ....*....|....*...
gi 109940213 272 IMYGADLNIKNCAGKTPM 289
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPL 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
223-295 2.41e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 2.41e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109940213  223 LHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYgADLNIKNcAGKTPmdlvLHW 295
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTA----LHY 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
186-239 4.44e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 4.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 109940213  186 ESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLI 239
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 123-261 5.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 5.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 123 TFLKAALENKLPVVEKFL----SDKNNPDVCDEYkrtALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWA-SRGG 197
Cdd:PHA02878 170 TALHYATENKDQRLTELLlsygANVNIPDKTNNS---PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCK 246

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109940213 198 NLDVLKLLLNKGAKISARDKLLS-TALHVAVRTGhyECAEHLIACEADLNAKDREGDTPLHDAVR 261
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYILGlTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 142-279 2.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 142 DKNNPDVcdeykRTALHRACLEGHLAIVEKLMEAGAQIE---FRDMLesTAIHWASRGGNLDVLKLLLNKGA--KISARD 216
Cdd:PHA02875  62 DVKYPDI-----ESELHDAVEEGDVKAVEELLDLGKFADdvfYKDGM--TPLHLATILKKLDIMKLLIARGAdpDIPNTD 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109940213 217 KllSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLN 279
Cdd:PHA02875 135 K--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 149-272 6.49e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 149 CDEYKRTALHRACLEGHL-------AIVEKLMEAGAQIEFRDMLESTAIHWASRGG---NLDVLKLLLNkGAKISARDKL 218
Cdd:PHA03095 178 ADVYAVDDRFRSLLHHHLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRY 256

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 109940213 219 LSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLI 272
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 130-319 1.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 130 ENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKG 209
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 210 AKISARDkllsTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRL-NRYKMIRLLIMYGADLNIKNCAGKTP 288
Cdd:PHA02876 235 SNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETP 310

                        170       180       190
                 ....*....|....*....|....*....|.
gi 109940213 289 MDLvlhwqngtkaifdsLRENSYKTSRIATF 319
Cdd:PHA02876 311 LYL--------------MAKNGYDTENIRTL 327
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-279 2.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 125 LKAALE---NKLPVVEKFLSDKNNPDVCDEykrtalhracleghlaiVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDV 201
Cdd:PHA03100 145 LHLYLEsnkIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 202 LKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDR----EGDTPLHDavrLNRYKMIRLLIMYGAD 277
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtllyFKDKDLNT---ITKIKMLKKSIMYMFL 284


                 ..
gi 109940213 278 LN 279
Cdd:PHA03100 285 LD 286
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 116-282 3.38e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 116 TEPVDVPTFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASR 195
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 196 GGNLDVLKLLLNkGAKIS---ARDKLLSTalhvAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLI 272
Cdd:PLN03192 601 AKHHKIFRILYH-FASISdphAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675

                        170
                 ....*....|
gi 109940213 273 MYGADLNIKN 282
Cdd:PLN03192 676 MNGADVDKAN 685
Ank_5 pfam13857
Ankyrin repeats (many copies);
238-292 6.88e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 6.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 109940213  238 LIACE-ADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPMDLV 292
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-206 7.03e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 7.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 109940213  154 RTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLL 206
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 127-280 8.87e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 127 AALENKLPVVEKFL-SDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLL 205
Cdd:PHA02875  75 AVEEGDVKAVEELLdLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109940213 206 LNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGD-TPLHDAVRLNRYKMIRLLIMYGADLNI 280
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 154-304 1.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 154 RTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYE 233
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109940213 234 CAEHLIaceaDLN--AKD---REGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPMDLVLHWQ--NGTKAIFD 304
Cdd:PHA02875  83 AVEELL----DLGkfADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGdiKGIELLID 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
220-272 5.35e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 5.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 109940213  220 STALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLI 272
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
204-257 1.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 109940213  204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLH 257
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 202-276 3.68e-07

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 49.43  E-value: 3.68e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109940213 202 LKLLLNKGAKISARDKLL-STALHVAVRTGHYECAEHLiaCE---ADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGA 276
Cdd:PHA02743  76 IELLVNMGADINARELGTgNTLLHIAASTKNYELAEWL--CRqlgVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 184-274 4.07e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 4.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 184 MLESTAIHWASRGGNLDVlKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLN 263
Cdd:PTZ00322  81 MLTVELCQLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159

                         90
                 ....*....|.
gi 109940213 264 RYKMIRLLIMY 274
Cdd:PTZ00322 160 FREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 238-306 1.24e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109940213 238 LIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPMDLVLhwQNGTKAIFDSL 306
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE--ENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
122-172 1.83e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 109940213  122 PTFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKL 172
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 172-248 3.03e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 172 LMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIAC-----EADLN 246
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfELGAN 180


                 ..
gi 109940213 247 AK 248
Cdd:PTZ00322 181 AK 182
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 159-283 6.89e-06

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: 47.77  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  159 RACLEGHLAIVEKLMEAGA--QIEFRDML-ESTAIHWASRGGNLDVLKLLLNKGAKISARDkllsTALHVAVRTGH---Y 232
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKklNINCPDRLgRSALFVAAIENENLELTELLLNLSCRGAVGD----TLLHAISLEYVdavE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109940213  233 ECAEHLIACEADLN----AKDREGD------TPLHDAVRLNRYKMIRLLIMYGADLNIKNC 283
Cdd:TIGR00870  99 AILLHLLAAFRKSGplelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARAC 159
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 190-309 1.18e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.48  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 190 IHWASRGGnlDVLKLLLNKGAKISARDKLLS-------TALHVAVRTGHYECAEH---LIACEADLNAKDR-EGDTPLHD 258
Cdd:PHA02736  21 LHYLCRNG--GVTDLLAFKNAISDENRYLVLeynrhgkQCVHIVSNPDKADPQEKlklLMEWGADINGKERvFGNTPLHI 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109940213 259 AVRLNRYKMIRLLIMY-GADLNIKNCAGKTPMDLVLHwQNGTKaIFDSLREN 309
Cdd:PHA02736  99 AVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACE-RHDAK-MMNILRAK 148
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 251-282 1.44e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 109940213  251 EGDTPLHDAV-RLNRYKMIRLLIMYGADLNIKN 282
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-206 2.50e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 2.50e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109940213 140 LSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLL 206
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 251-280 7.48e-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: 39.16  E-value: 7.48e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 109940213  251 EGDTPLHDAVRLNRYKMIRLLIMYGADLNI 280
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 221-250 9.61e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 9.61e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 109940213  221 TALHVAV-RTGHYECAEHLIACEADLNAKDR 250
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 251-280 1.03e-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: 38.72  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 109940213   251 EGDTPLHDAVRLNRYKMIRLLIMYGADLNI 280
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-217 1.45e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 1.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 109940213  188 TAIHWAS-RGGNLDVLKLLLNKGAKISARDK 217
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 188-214 1.92e-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: 37.95  E-value: 1.92e-04
                           10        20
                   ....*....|....*....|....*..
gi 109940213   188 TAIHWASRGGNLDVLKLLLNKGAKISA 214
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
188-226 4.57e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 4.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 109940213  188 TAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVA 226
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02917 PHA02917
ankyrin-like protein; Provisional
 244-287 6.02e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.52  E-value: 6.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 109940213 244 DLNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKT 287
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 221-247 1.02e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.02e-03
                           10        20
                   ....*....|....*....|....*..
gi 109940213   221 TALHVAVRTGHYECAEHLIACEADLNA 247
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 138-291 1.14e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 138 KFLSDKNNPDVCDEYKR-----TALHRACL---EGHLAIVEKLMEAG------AQIEFRDMLES-----TAIHWASRGGN 198
Cdd:cd21882    6 GLLECLRWYLTDSAYQRgatgkTCLHKAALnlnDGVNEAIMLLLEAApdsgnpKELVNAPCTDEfyqgqTALHIAIENRN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 199 LDVLKLLLNKGAKISARDKllSTALHVAVRTGHY--ECAEHLIACE----------------ADLNAKDREGDTPLH--- 257
Cdd:cd21882   86 LNLVRLLVENGADVSARAT--GRFFRKSPGNLFYfgELPLSLAACTnqeeivrlllengaqpAALEAQDSLGNTVLHalv 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109940213 258 ---DAVRLNRY---KMIRLLIMYGADLN-------IKNCAGKTPMDL 291
Cdd:cd21882  164 lqaDNTPENSAfvcQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKL 210
PHA02741 PHA02741
hypothetical protein; Provisional
 191-308 1.20e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 191 HWASRGGNLDVLKLLL------NKGAKISARDKLLSTALHVAVRTGHYECA----EHLIACEADLNAKDR-EGDTPLHDA 259
Cdd:PHA02741  26 HEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAQLAaeiiDHLIELGADINAQEMlEGDTALHLA 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 109940213 260 VRLNRYKMIRLLIMY-GADLNIKNCAGKTPMDLVLhwQNGTKAIFDSLRE 308
Cdd:PHA02741 106 AHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAI--DNEDVAMMQILRE 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
252-297 1.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 109940213  252 GDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPMDLVLHWQN 297
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 149-291 2.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.65  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 149 CDEYKRTALHrACLEG---HLAIVEKLMEAGAQIEF--RDMLESTAIHWASRGGNL--DVLKLLLNKGAKISARDKLLST 221
Cdd:PHA02859  47 CNDLYETPIF-SCLEKdkvNVEILKFLIENGADVNFktRDNNLSALHHYLSFNKNVepEILKILIDSGSSITEEDEDGKN 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109940213 222 ALHV-----AVRTghyECAEHLIACEADLNAKDREGDTPLHDAVRL-NRYKMIRLLIMYGADLNIKNCAGKTPMDL 291
Cdd:PHA02859 126 LLHMymcnfNVRI---NVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-214 3.22e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 3.22e-03
                          10        20
                  ....*....|....*....|....*..
gi 109940213  188 TAIHWASRGGNLDVLKLLLNKGAKISA 214
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 152-180 3.99e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 3.99e-03
                           10        20
                   ....*....|....*....|....*....
gi 109940213   152 YKRTALHRACLEGHLAIVEKLMEAGAQIE 180
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 221-247 4.45e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|....*..
gi 109940213  221 TALHVAVRTGHYECAEHLIACEADLNA 247
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 134-239 4.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 134 PVVEKFLSDKNNPDVCDEYKRTALHRA---CLEghLAIVEKLMEAGAQIEFRD-MLESTAIHWASRggNLDVLKLLLNKG 209
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYG 290

                         90       100       110
                 ....*....|....*....|....*....|.
gi 109940213 210 AKISARDKLLSTALHVAVRTGH-YECAEHLI 239
Cdd:PHA02878 291 ADINSLNSYKLTPLSSAVKQYLcINIGRILI 321
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 144-310 4.94e-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: 38.52  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  144 NNPDVCDEYK-RTALHRACLEGHLAIVEKLMEAGAQIEFR----DMLESTAIHWASRG----------GNLDVLKLLLNK 208
Cdd:TIGR00870 118 NDQYTSEFTPgITALHLAAHRQNYEIVKLLLERGASVPARacgdFFVKSQGVDSFYHGesplnaaaclGSPSIVALLSED 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213  209 GAKISARDKLLSTALHVAVR-------------------TGHYECAEHLIACEADLNakdREGDTPLHDAVRLNRYKMIR 269
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVMenefkaeyeelscqmynfaLSLLDKLRDSKELEVILN---HQGLTPLKLAAKEGRIVLFR 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 109940213  270 LLimygadLNIK----------NCagktPMDLVLHWQNGtkaiFDSLRENS 310
Cdd:TIGR00870 275 LK------LAIKykqkkfvawpNG----QQLLSLYWLEE----LDGWRRKQ 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 219-314 5.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.41  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109940213 219 LSTALHVAVRTGHYECAEHLIACEAD-LNAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCagKTPMDLVLHWQN 297
Cdd:PHA02874   1 ASQDLRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINT--KIPHPLLTAIKI 78

                         90
                 ....*....|....*..
gi 109940213 298 GTKAIFDSLRENSYKTS 314
Cdd:PHA02874  79 GAHDIIKLLIDNGVDTS 95
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 154-183 8.27e-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: 33.42  E-value: 8.27e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 109940213  154 RTALHRACLE-GHLAIVEKLMEAGAQIEFRD 183
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 246-299 9.50e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.34  E-value: 9.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 109940213 246 NAKDREGDTPLHDAVRLNRYKMIRLLIMYGADLNIKNCAGKTPmdlvLHWQNGT 299
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP----LYYLSGT 115
 
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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