NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|31560506|ref|NP_038496|]
View 

ankyrin repeat domain-containing protein 1 [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];
124-291 1.15e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 1.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 124 FLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLK 203
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNC 283
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217


                ....*...
gi 31560506 284 AGKTPMDL 291
Cdd:COG0666 218 DGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-291 1.15e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 1.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 124 FLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLK 203
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNC 283
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217


                ....*...
gi 31560506 284 AGKTPMDL 291
Cdd:COG0666 218 DGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
157-249 2.94e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506   157 LHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKgAKISARDKLLsTALHVAVRTGHYECAE 236
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 31560506   237 HLIACEADLNAKD 249
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-317 3.76e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  150 DEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRT 229
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  230 GHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRyKMIRLLMTfGADLKVKNCAGKTPMDLVLHWQSgTKAIFDSLken 309
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINPPC-DIDIIDIL--- 274


                 ....*...
gi 31560506  310 AYKNSRIA 317
Cdd:PHA02874 275 LYHKADIS 282
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-291 6.98e-12

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: 65.80  E-value: 6.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 120 DVPRFLkAALENKLPVVEKFLSdknSPDvCDEYKR-----TALHRACLEGHLAIVEKLMEAGAQIEFRDMLES-----TA 189
Cdd:cd22192  18 ESPLLL-AAKENDVQAIKKLLK---CPS-CDLFQRgalgeTALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgeTA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 190 IHWACRGGNADVLKLLLNKGAK-ISAR----------DKLLSTALHV---AVRTGHYECAEHLIACEADLNAKDREGDTP 255
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpKNLIYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31560506 256 LHDAV----RLNRYKMIRLLMTFGADLK------VKNCAGKTPMDL 291
Cdd:cd22192 173 LHILVlqpnKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKL 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 188-214 3.95e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 3.95e-05
                           10        20
                   ....*....|....*....|....*..
gi 31560506    188 TAIHWACRGGNADVLKLLLNKGAKISA 214
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 159-283 1.10e-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: 40.83  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506   159 RACLEGHLAIVEKLMEAGA--QIEFRDML-ESTAIHWACRGGNADVLKLLLNKGAKISARDkllsTALHVAVRTGH---Y 232
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKklNINCPDRLgRSALFVAAIENENLELTELLLNLSCRGAVGD----TLLHAISLEYVdavE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31560506   233 ECAEHLIACEADLN----AKDREGD------TPLHDAVRLNRYKMIRLLMTFGADLKVKNC 283
Cdd:TIGR00870  99 AILLHLLAAFRKSGplelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARAC 159
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-291 1.15e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 1.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 124 FLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLK 203
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNC 283
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217


                ....*...
gi 31560506 284 AGKTPMDL 291
Cdd:COG0666 218 DGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-295 1.58e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 124 FLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLK 203
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNC 283
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                       170
                ....*....|..
gi 31560506 284 AGKTPMDLVLHW 295
Cdd:COG0666 251 DGLTALLLAAAA 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
127-289 3.01e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.21  E-value: 3.01e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 127 AALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLL 206
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 207 NKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGK 286
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                ...
gi 31560506 287 TPM 289
Cdd:COG0666 287 TLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
123-295 8.06e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 8.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 123 RFLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVL 202
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 203 KLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKN 282
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                       170
                ....*....|...
gi 31560506 283 CAGKTPmdlvLHW 295
Cdd:COG0666 184 NDGETP----LHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
157-249 2.94e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506   157 LHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKgAKISARDKLLsTALHVAVRTGHYECAE 236
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 31560506   237 HLIACEADLNAKD 249
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
190-282 9.56e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 9.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506   190 IHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIAcEADLNAKDrEGDTPLHDAVRLNRYKMIR 269
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 31560506   270 LLMTFGADLKVKN 282
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-295 4.30e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 4.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 150 DEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRT 229
Cdd:COG0666  18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31560506 230 GHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPmdlvLHW 295
Cdd:COG0666  98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP----LHL 159
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-317 3.76e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  150 DEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRT 229
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  230 GHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRyKMIRLLMTfGADLKVKNCAGKTPMDLVLHWQSgTKAIFDSLken 309
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINPPC-DIDIIDIL--- 274


                 ....*...
gi 31560506  310 AYKNSRIA 317
Cdd:PHA02874 275 LYHKADIS 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
127-216 7.14e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 7.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506   127 AALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEaGAQIEFRDMLEsTAIHWACRGGNADVLKLLL 206
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 31560506   207 NKGAKISARD 216
Cdd:pfam12796  82 EKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 147-297 8.61e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 8.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  147 DVCDEYKRTALHRAC-LEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHV 225
Cdd:PHA02876 335 NAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF 414

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31560506  226 AV-RTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLN-RYKMIRLLMTFGADLKVKNCAGKTPMDLVLHWQS 297
Cdd:PHA02876 415 ALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG 488
PHA03095 PHA03095
ankyrin-like protein; Provisional
 166-293 2.70e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  166 LAIVEKLMEAGAQIEFRDMLESTAIHWACRGGN---ADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYE-CAEHLIAC 241
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31560506  242 EADLNAKDREGDTPLHdaVRLN----RYKMIRLLMTFGADLKVKNCAGKTPMDLVL 293
Cdd:PHA03095 107 GADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLL 160
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 161-297 4.73e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.39  E-value: 4.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  161 CLEGHLaiVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIA 240
Cdd:PHA02874 101 CIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 31560506  241 CEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPM-DLVLHWQS 297
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLhNAIIHNRS 236
PHA03095 PHA03095
ankyrin-like protein; Provisional
 131-299 2.02e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  131 NKLPVVEKFLSDKNSPDVCDEYKRTALHrACLEG---HLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADV--LKLL 205
Cdd:PHA03095  95 TTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  206 LNKGAKISARDKLLSTALH---VAVRTgHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKmiRLLMTF----GADL 278
Cdd:PHA03095 174 IDAGADVYAVDDRFRSLLHhhlQSFKP-RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCK--RSLVLPlliaGISI 250

                        170       180
                 ....*....|....*....|.
gi 31560506  279 KVKNCAGKTPmdlvLHWQSGT 299
Cdd:PHA03095 251 NARNRYGQTP----LHYAAVF 267
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 133-289 2.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  133 LPVVEKFLSDK-NSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLL------ 205
Cdd:PHA02874  14 IEAIEKIIKNKgNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvd 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  206 -----------------LNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMI 268
Cdd:PHA02874  94 tsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII 173

                        170       180
                 ....*....|....*....|.
gi 31560506  269 RLLMTFGADLKVKNCAGKTPM 289
Cdd:PHA02874 174 KLLLEKGAYANVKDNNGESPL 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 143-300 9.31e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 9.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  143 KNSPDVCDEYKRTALHRACLEGHlaIVEKLMEAGAQIEFRDM-LESTAIHWACRGGNADVLKLLLNKGAKISARDKLLST 221
Cdd:PHA02878 126 KNIQTIDLVYIDKKSKDDIIEAE--ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  222 ALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAV-RLNRYKMIRLLMTFGADLKVKNCA-GKTPMDLVLHWQSGT 299
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERKL 283


                 .
gi 31560506  300 K 300
Cdd:PHA02878 284 K 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 199-294 1.34e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  199 ADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAE---HLIACEADLNAKDREGDTPLHDAVRL-NRYKMIRLLMTF 274
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKA 106

                         90       100
                 ....*....|....*....|
gi 31560506  275 GADLKVKNCAGKTPmdlvLH 294
Cdd:PHA03095 107 GADVNAKDKVGRTP----LH 122
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 126-288 3.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 3.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  126 KAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLE--GHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNAD--V 201
Cdd:PHA03100  79 KYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkI 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  202 LKLLLNKGAKISARDKLlstalhvavrtghyecaEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVK 281
Cdd:PHA03100 159 LKLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221


                 ....*..
gi 31560506  282 NCAGKTP 288
Cdd:PHA03100 222 NKYGDTP 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-291 6.98e-12

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: 65.80  E-value: 6.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 120 DVPRFLkAALENKLPVVEKFLSdknSPDvCDEYKR-----TALHRACLEGHLAIVEKLMEAGAQIEFRDMLES-----TA 189
Cdd:cd22192  18 ESPLLL-AAKENDVQAIKKLLK---CPS-CDLFQRgalgeTALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgeTA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 190 IHWACRGGNADVLKLLLNKGAK-ISAR----------DKLLSTALHV---AVRTGHYECAEHLIACEADLNAKDREGDTP 255
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpKNLIYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31560506 256 LHDAV----RLNRYKMIRLLMTFGADLK------VKNCAGKTPMDL 291
Cdd:cd22192 173 LHILVlqpnKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKL 218
PHA03095 PHA03095
ankyrin-like protein; Provisional
 142-289 8.13e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 8.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  142 DKNSPDVCDEykrTALH-RACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGN--ADVLKLLLNKGAKISARDKL 218
Cdd:PHA03095  75 DVNAPERCGF---TPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLY 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31560506  219 LSTALHVAVRTGH--YECAEHLIACEADLNAKDREGDTPLH---DAVRlNRYKMIRLLMTFGADLKVKNCAGKTPM 289
Cdd:PHA03095 152 GMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHhhlQSFK-PRARIVRELIRAGCDPAATDMLGNTPL 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 199-307 1.44e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  199 ADVLKLLLNKGAKISARDK-LLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGAD 277
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110
                 ....*....|....*....|....*....|
gi 31560506  278 LKVKNCAGKTPmdlvLHWQSGTKAIFDSLK 307
Cdd:PHA02878 227 TDARDKCGNTP----LHISVGYCKDYDILK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 125-261 6.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 6.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  125 LKAALENKLPVVEKFL----SDKNSPDVCDEYkrtALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWAC-RGGNA 199
Cdd:PHA02878 172 LHYATENKDQRLTELLlsygANVNIPDKTNNS---PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDY 248

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31560506  200 DVLKLLLNKGAKISARDKLLS-TALHVAVRTGhyECAEHLIACEADLNAKDREGDTPLHDAVR 261
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYILGlTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 166-293 6.67e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 6.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  166 LAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHY-----ECAEHLIA 240
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 31560506  241 CEADLNAKDREGDTPLHDAV--RLNRYKMIRLLMTFGADLKVKNCAGKTPMDLVL 293
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
Ank_2 pfam12796
Ankyrin repeats (3 copies);
223-295 2.07e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31560506   223 LHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFgADLKVKNcAGKTPmdlvLHW 295
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTA----LHY 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
186-239 2.44e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 31560506   186 ESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLI 239
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 124-313 2.99e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  124 FLKAALEN-KLPVVE---KFLSDKNSPDVCDEYkrtALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNA 199
Cdd:PHA02874 127 FLHYAIKKgDLESIKmlfEYGADVNIEDDNGCY---PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  200 DVLKLLLNKGAKISARDKLLSTALHVAVRtgHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYK-MIRLLMTFGADL 278
Cdd:PHA02874 204 ACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADI 281

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 31560506  279 KVKNCAGKTPMDLVLHWQSGTKAIFDSLKENAYKN 313
Cdd:PHA02874 282 SIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIK 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
 149-272 2.06e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  149 CDEYKRTALHRACLEGHL-------AIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKL--LLNKGAKISARDKLL 219
Cdd:PHA03095 178 ADVYAVDDRFRSLLHHHLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 31560506  220 STALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLM 272
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 142-288 2.57e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  142 DKNSPDVcdeykRTALHRACLEGHLAIVEKLMEAGAQIE---FRDMLesTAIHWACRGGNADVLKLLLNKGA--KISARD 216
Cdd:PHA02875  62 DVKYPDI-----ESELHDAVEEGDVKAVEELLDLGKFADdvfYKDGM--TPLHLATILKKLDIMKLLIARGAdpDIPNTD 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31560506  217 KllSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLkvkNCAGKTP 288
Cdd:PHA02875 135 K--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 172-289 2.96e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  172 LMEAGAQIEFRDMLESTAIHWACRGGN-ADVLKLLLNKGAKISARDKLLSTALHVAVRTGH-YECAEHLIACEADLNAKD 249
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 31560506  250 REGDTPLHDAVRLNRYKMIRL-LMTFGADLKVKNCAGKTPM 289
Cdd:PHA02876 339 RLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPI 379
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-206 9.36e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 9.36e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31560506   154 RTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLL 206
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 130-292 1.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  130 ENKLPVVEKFL---SDKNSPDVcdeYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLL 206
Cdd:PHA02876 155 QDELLIAEMLLeggADVNAKDI---YCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  207 NKGAKISARDkllsTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRL-NRYKMIRLLMTFGADLKVKNCAG 285
Cdd:PHA02876 232 DNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG 307


                 ....*..
gi 31560506  286 KTPMDLV 292
Cdd:PHA02876 308 ETPLYLM 314
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 116-282 3.26e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  116 TEPVDVPRFLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACR 195
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  196 GGNADVLKLLLNkGAKIS---ARDKLLSTalhvAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLM 272
Cdd:PLN03192 601 AKHHKIFRILYH-FASISdphAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675

                        170
                 ....*....|
gi 31560506  273 TFGADLKVKN 282
Cdd:PLN03192 676 MNGADVDKAN 685
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-289 8.35e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 8.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506 166 LAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADL 245
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 31560506 246 NAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPM 289
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 127-277 1.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  127 AALENKLPVVEKFL-SDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLL 205
Cdd:PHA02875  75 AVEEGDVKAVEELLdLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31560506  206 LNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGD-TPLHDAVRLNRYKMIRLLMTFGAD 277
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
238-292 1.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 31560506   238 LIACE-ADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPMDLV 292
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
204-257 1.47e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 31560506   204 LLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLH 257
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 154-293 1.63e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  154 RTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYE 233
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31560506  234 CAEHLIaceaDLN--AKD---REGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPMDLVL 293
Cdd:PHA02875  83 AVEELL----DLGkfADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
Ank_4 pfam13637
Ankyrin repeats (many copies);
220-271 2.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 31560506   220 STALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLL 271
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-272 2.52e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31560506  197 GNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLM 272
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 202-276 4.67e-07

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 49.04  E-value: 4.67e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31560506  202 LKLLLNKGAKISARDKLL-STALHVAVRTGHYECAEHLiaCE---ADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGA 276
Cdd:PHA02743  76 IELLVNMGADINARELGTgNTLLHIAASTKNYELAEWL--CRqlgVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 238-291 5.27e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 5.27e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 31560506  238 LIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPMDL 291
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-250 6.13e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  125 LKAALE---NKLPVVEKFLSDKNSPDVCDEykrtalhracleghlaiVEKLMEAGAQIEFRDMLESTAIHWACRGGNADV 201
Cdd:PHA03100 145 LHLYLEsnkIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 31560506  202 LKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDR 250
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-248 1.07e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  141 SDKNSP--DVCDEykrTALHRACLE-GHLAI------VEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAK 211
Cdd:PTZ00322  64 PDHNLTteEVIDP---VVAHMLTVElCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 31560506  212 ISARDKLLSTALHVAVRTGHYECAEHLIAC-----EADLNAK 248
Cdd:PTZ00322 141 PTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfELGANAK 182
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 190-288 1.15e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.56  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  190 IHWACRggNADVLKLLLNKGAKISARDKLLS-------TALHVAVRTGHYECAEH---LIACEADLNAKDR-EGDTPLHD 258
Cdd:PHA02736  21 LHYLCR--NGGVTDLLAFKNAISDENRYLVLeynrhgkQCVHIVSNPDKADPQEKlklLMEWGADINGKERvFGNTPLHI 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 31560506  259 AVRLNRYKMIR-LLMTFGADLKVKNCAGKTP 288
Cdd:PHA02736  99 AVYTQNYELATwLCNQPGVNMEILNYAFKTP 129
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 131-219 2.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  131 NKLPVVEKFLSdKNSP-DVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKG 209
Cdd:PHA03100 170 NAKNRVNYLLS-YGVPiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                         90
                 ....*....|
gi 31560506  210 AKISARDKLL 219
Cdd:PHA03100 249 PSIKTIIETL 258
Ank_4 pfam13637
Ankyrin repeats (many copies);
126-172 5.22e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 5.22e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 31560506   126 KAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKL 172
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-206 3.56e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 3.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31560506  140 LSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLL 206
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 188-214 3.95e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 3.95e-05
                           10        20
                   ....*....|....*....|....*..
gi 31560506    188 TAIHWACRGGNADVLKLLLNKGAKISA 214
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-217 6.55e-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: 39.58  E-value: 6.55e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 31560506   188 TAIHWAC-RGGNADVLKLLLNKGAKISARDK 217
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 235-313 7.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  235 AEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPMDLVLHWQS--GTKAIFDSlKENAYK 312
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNidTIKAIIDN-RSNINK 239


                 .
gi 31560506  313 N 313
Cdd:PHA02876 240 N 240
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 221-250 7.74e-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: 39.19  E-value: 7.74e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 31560506   221 TALHVAV-RTGHYECAEHLIACEADLNAKDR 250
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 190-280 8.38e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  190 IHWACRGGNAD---VLKLLLNKGAKISARDKLL-STALHVAVRTGHYECAEHLiaCE---ADLNAKDREGDTPLHDAVRL 262
Cdd:PHA02736  59 VHIVSNPDKADpqeKLKLLMEWGADINGKERVFgNTPLHIAVYTQNYELATWL--CNqpgVNMEILNYAFKTPYYVACER 136

                         90
                 ....*....|....*...
gi 31560506  263 NRYKMIRLLMTFGADLKV 280
Cdd:PHA02736 137 HDAKMMNILRAKGAQCKV 154
Ank_5 pfam13857
Ankyrin repeats (many copies);
188-226 1.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 31560506   188 TAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVA 226
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-214 4.34e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 4.34e-04
                          10        20
                  ....*....|....*....|....*..
gi 31560506   188 TAIHWACRGGNADVLKLLLNKGAKISA 214
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 221-247 7.22e-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: 36.41  E-value: 7.22e-04
                           10        20
                   ....*....|....*....|....*..
gi 31560506    221 TALHVAVRTGHYECAEHLIACEADLNA 247
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 159-283 1.10e-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: 40.83  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506   159 RACLEGHLAIVEKLMEAGA--QIEFRDML-ESTAIHWACRGGNADVLKLLLNKGAKISARDkllsTALHVAVRTGH---Y 232
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKklNINCPDRLgRSALFVAAIENENLELTELLLNLSCRGAVGD----TLLHAISLEYVdavE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31560506   233 ECAEHLIACEADLN----AKDREGD------TPLHDAVRLNRYKMIRLLMTFGADLKVKNC 283
Cdd:TIGR00870  99 AILLHLLAAFRKSGplelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARAC 159
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 134-239 1.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560506  134 PVVEKFLSDKNSPDVCDEYKRTALHRA---CLEghLAIVEKLMEAGAQIEFRD-MLESTAIHWACRggNADVLKLLLNKG 209
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYG 290

                         90       100       110
                 ....*....|....*....|....*....|.
gi 31560506  210 AKISARDKLLSTALHVAVRTGH-YECAEHLI 239
Cdd:PHA02878 291 ADINSLNSYKLTPLSSAVKQYLcINIGRILI 321
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 251-278 1.60e-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: 35.26  E-value: 1.60e-03
                           10        20
                   ....*....|....*....|....*...
gi 31560506    251 EGDTPLHDAVRLNRYKMIRLLMTFGADL 278
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02741 PHA02741
hypothetical protein; Provisional
 222-291 2.30e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 2.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31560506  222 ALHVAVRTGHYECA----EHLIACEADLNAKDR-EGDTPLHDAVRLNRYKMIR-LLMTFGADLKVKNCAGKTPMDL 291
Cdd:PHA02741  63 CIHIAAEKHEAQLAaeiiDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEwLCCQPGIDLHFCNADNKSPFEL 138
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 251-282 2.83e-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: 34.96  E-value: 2.83e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 31560506   251 EGDTPLHDAV-RLNRYKMIRLLMTFGADLKVKN 282
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 152-180 2.89e-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: 34.87  E-value: 2.89e-03
                           10        20
                   ....*....|....*....|....*....
gi 31560506    152 YKRTALHRACLEGHLAIVEKLMEAGAQIE 180
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02917 PHA02917
ankyrin-like protein; Provisional
 244-287 2.98e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.21  E-value: 2.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 31560506  244 DLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKT 287
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 221-247 3.32e-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: 34.54  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|....*..
gi 31560506   221 TALHVAVRTGHYECAEHLIACEADLNA 247
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 246-299 4.90e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 31560506  246 NAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPmdlvLHWQSGT 299
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP----LYYLSGT 115
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 251-278 6.47e-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: 33.77  E-value: 6.47e-03
                          10        20
                  ....*....|....*....|....*...
gi 31560506   251 EGDTPLHDAVRLNRYKMIRLLMTFGADL 278
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 154-183 6.93e-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: 33.80  E-value: 6.93e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 31560506   154 RTALHRACLE-GHLAIVEKLMEAGAQIEFRD 183
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 152-179 9.98e-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: 33.38  E-value: 9.98e-03
                          10        20
                  ....*....|....*....|....*...
gi 31560506   152 YKRTALHRACLEGHLAIVEKLMEAGAQI 179
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
 
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