|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
276-526 |
5.90e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.72 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 276 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 354
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 355 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 433
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 434 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 512
Cdd:COG0666 200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
250
....*....|....
gi 544346158 513 ALIDRLISHGADIL 526
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-156 |
1.63e-18 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 86.16 E-value: 1.63e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKT 156
Cdd:COG4642 185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYAD 261
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
85-150 |
3.71e-15 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 79.49 E-value: 3.71e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 85 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG 150
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLG 93
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
294-524 |
3.80e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.86 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 294 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 371
Cdd:PHA02875 21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 372 VDakasdeDDTYKPGKLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEREDDNkcardIVRLLLSHGANPN 451
Cdd:PHA02875 94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544346158 452 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 524
Cdd:PHA02875 163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
419-484 |
2.80e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 2.80e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 419 GRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 484
Cdd:pfam12796 30 GRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
641-681 |
2.93e-09 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 52.81 E-value: 2.93e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 544346158 641 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 681
Cdd:pfam01753 1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
311-482 |
1.24e-05 |
|
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: 48.47 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 311 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdeddtykpgkl 388
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 389 dllpsslkLSNEPGPPQAYYstdtalpeegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 453
Cdd:cd22192 77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133
|
170 180
....*....|....*....|....*....
gi 544346158 454 WSGHSPLSLSIASGNELVVKELLTQGADP 482
Cdd:cd22192 134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
419-452 |
3.71e-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: 41.03 E-value: 3.71e-05
10 20 30
....*....|....*....|....*....|....
gi 544346158 419 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 452
Cdd:smart00248 2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
114-136 |
1.66e-04 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 38.93 E-value: 1.66e-04
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
113-133 |
4.73e-04 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 37.71 E-value: 4.73e-04
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
166-198 |
2.75e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|...
gi 544346158 166 DIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 198
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
276-526 |
5.90e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.72 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 276 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 354
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 355 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 433
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 434 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 512
Cdd:COG0666 200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
250
....*....|....
gi 544346158 513 ALIDRLISHGADIL 526
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
311-527 |
2.00e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.02 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 311 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKASDeddtykpgkldl 390
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQDND------------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 391 lpsslklsnepgppqayystdtalpeegGRTALHMACEREDdnkcaRDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 469
Cdd:COG0666 153 ----------------------------GNTPLHLAAANGN-----LEIVKLLLEAGADVNARdNDGETPLHLAAENGHL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 544346158 470 LVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADILK 527
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDG-KTALDLAA---------ENGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
311-525 |
3.09e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 91.55 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 311 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKASDeddtykpgkldl 390
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINA---KDDGGNTLLHAAAR---NGDLEIVKLLLEAGADVNARDKD------------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 391 lpsslklsnepgppqayystdtalpeegGRTALHMACEREDDnkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 469
Cdd:COG0666 120 ----------------------------GETPLHLAAYNGNL-----EIVKLLLEAGADVNAQdNDGNTPLHLAAANGNL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 470 LVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADI 525
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDG-ETPLHLAA---------ENGHLEIVKLLLEAGADV 212
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-156 |
1.63e-18 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 86.16 E-value: 1.63e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKT 156
Cdd:COG4642 185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYAD 261
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-155 |
2.83e-15 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 76.53 E-value: 2.83e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK 155
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYA 214
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-153 |
3.37e-15 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 76.53 E-value: 3.37e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMY 153
Cdd:COG4642 162 QGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLT 235
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
85-150 |
3.71e-15 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 79.49 E-value: 3.71e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 85 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG 150
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLG 93
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-141 |
1.45e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 68.44 E-value: 1.45e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTF 141
Cdd:COG4642 208 QGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
294-524 |
3.80e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.86 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 294 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 371
Cdd:PHA02875 21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 372 VDakasdeDDTYKPGKLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEREDDNkcardIVRLLLSHGANPN 451
Cdd:PHA02875 94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544346158 452 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 524
Cdd:PHA02875 163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
274-481 |
1.59e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 274 MRRMALSMIERRKRWRTIKLLLRRGADPN------LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQlstLTPL 347
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINsstknnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG---ITPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 348 HIAAALPGEEgVQIVELLLHAITDVDAKASDEDD------TYKPGKLDLLpsSLKLSNepgppQAY------------YS 409
Cdd:PHA03100 111 LYAISKKSNS-YSIVEYLLDNGANVNIKNSDGENllhlylESNKIDLKIL--KLLIDK-----GVDinaknrvnyllsYG 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346158 410 TDTALPEEGGRTALHMACERedDNKcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGAD 481
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYN--NNP---EFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-153 |
4.97e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 63.82 E-value: 4.97e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMY 153
Cdd:COG4642 116 GGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLT 189
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
419-484 |
2.80e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 2.80e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 419 GRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 484
Cdd:pfam12796 30 GRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
311-452 |
3.44e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.05 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 311 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAAlpgEEGVQIVELLL-HAITDVDakasdeddtykpgkld 389
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAAK---NGHLEIVKLLLeHADVNLK---------------- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346158 390 llpsslklsnepgppqayystdtalpeEGGRTALHMACEreddnKCARDIVRLLLSHGANPNL 452
Cdd:pfam12796 59 ---------------------------DNGRTALHYAAR-----SGHLEIVKLLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
290-375 |
2.01e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.12 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 290 TIKLLLRRGADPNLC-CVPMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLSTLTPLHIAAalpgEEG-VQIVELLLH 367
Cdd:pfam12796 12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82
|
....*...
gi 544346158 368 AITDVDAK 375
Cdd:pfam12796 83 KGADINVK 90
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
79-161 |
2.87e-09 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 60.23 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 79 VQGVQE------WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTM 152
Cdd:PLN03185 108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187
|
90
....*....|
gi 544346158 153 YMK-TRLFQT 161
Cdd:PLN03185 188 YPAgSRVPAV 197
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
641-681 |
2.93e-09 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 52.81 E-value: 2.93e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 544346158 641 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 681
Cdd:pfam01753 1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
287-484 |
1.69e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.34 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 287 RWRTIKLLLRRGADPNLCCV----PMQVlFLAVKAGDVDGVRLLLEHGArtDICfPPQLSTLTPLHIAAALPGEEgVQIV 362
Cdd:PHA03095 96 TLDVIKLLIKAGADVNAKDKvgrtPLHV-YLSGFNINPKVIRLLLRKGA--DVN-ALDLYGMTPLAVLLKSRNAN-VELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 363 ELLLHAITDVDAKaSDEDDTYkpgkLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEReddNKCARDIVRL 442
Cdd:PHA03095 171 RLLIDAGADVYAV-DDRFRSL----LHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATG---SSCKRSLVLP 242
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 544346158 443 LLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNL 484
Cdd:PHA03095 243 LLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
162-384 |
5.17e-08 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 54.96 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 162 HCHNDIVNLLLDCGADVNKCSDEGLTAlsmcflLHYPAqsfkpnvaertipepqeppkfpvvpilsssfmdtnleslyye 241
Cdd:COG0666 130 NGNLEIVKLLLEAGADVNAQDNDGNTP------LHLAA------------------------------------------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 242 lsqamlersaqshsllkmaspspctssfdkgtmrrmalsmieRRKRWRTIKLLLRRGADPNLCCVPMQ-VLFLAVKAGDV 320
Cdd:COG0666 162 ------------------------------------------ANGNLEIVKLLLEAGADVNARDNDGEtPLHLAAENGHL 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544346158 321 DGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEgvqIVELLLHAITDVDAKASDEDDTYK 384
Cdd:COG0666 200 EIVKLLLEAGADVNA---KDNDGKTALDLAAENGNLE---IVKLLLEAGADLNAKDKDGLTALL 257
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
411-525 |
2.53e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.03 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 411 DTALPEEGGRTALHMACEREDDnkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKG 489
Cdd:COG0666 46 ALALADALGALLLLAAALAGDL-----LVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 544346158 490 lGSALCVACdltyehqrnMDSKLALIDRLISHGADI 525
Cdd:COG0666 121 -ETPLHLAA---------YNGNLEIVKLLLEAGADV 146
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
279-484 |
3.19e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.13 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 279 LSMIERRKRWRTIKLLLRRGA----DPNLCCVPMQV--LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAA 352
Cdd:PHA03100 1 LYSYIVLTKSRIIKVKNIKYIimedDLNDYSYKKPVlpLYLAKEARNIDVVKILLDNGADINS---STKNNSTPLHYLSN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 353 LPG--EEGVQIVELLLHAITDVDAkasdeddTYKPGKLDLLPSSLKLSNepgppqaYYSTDTALPEEG---------GRT 421
Cdd:PHA03100 78 IKYnlTDVKEIVKLLLEYGANVNA-------PDNNGITPLLYAISKKSN-------SYSIVEYLLDNGanvniknsdGEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 422 ALHMACEREDDNKcarDIVRLLLSHGANPN------LLWS-----------GHSPLSLSIASGNELVVKELLTQGADPNL 484
Cdd:PHA03100 144 LLHLYLESNKIDL---KILKLLIDKGVDINaknrvnYLLSygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
323-498 |
3.99e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.96 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 323 VRLLLEHGARTDICFPPQLStlTPLHIAAALPGEEgvqIVELLLhaITDVDAKASDEDDTYKpgkldlLPSSLKLSNEPG 402
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGN--TALHYATENKDQR---LTELLL--SYGANVNIPDKTNNSP------LHHAVKHYNKPI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 403 PPQAY-YSTDTALPEEGGRTALHMACEREDDnkcaRDIVRLLLSHGANPNLLWS--GHSPLSLSIASgnELVVKELLTQG 479
Cdd:PHA02878 217 VHILLeNGASTDARDKCGNTPLHISVGYCKD----YDILKLLLEHGVDVNAKSYilGLTALHSSIKS--ERKLKLLLEYG 290
|
170 180
....*....|....*....|....*.
gi 544346158 480 ADPNL-------PLTKGLGSALCVAC 498
Cdd:PHA02878 291 ADINSlnsykltPLSSAVKQYLCINI 316
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
419-452 |
7.65e-07 |
|
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: 45.74 E-value: 7.65e-07
10 20 30
....*....|....*....|....*....|....
gi 544346158 419 GRTALHMACEREDDnkcaRDIVRLLLSHGANPNL 452
Cdd:pfam00023 2 GNTPLHLAAGRRGN----LEIVKLLLSKGADVNA 31
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
423-525 |
2.03e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.26 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 423 LHMACEREDdnkcaRDIVRLLLSHGANPNLLWS-GHSPLSLSIASGNELVVKELLTQgADPNLPlTKGLgSALCVACDLT 501
Cdd:pfam12796 1 LHLAAKNGN-----LELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGR-TALHYAARSG 72
|
90 100
....*....|....*....|....
gi 544346158 502 YehqrnmdskLALIDRLISHGADI 525
Cdd:pfam12796 73 H---------LEIVKLLLEKGADI 87
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
278-464 |
3.28e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 50.26 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 278 ALSMIERRKRWRTIKLLLRRGADPNlccVPMQV----LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAL 353
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVN---IPDKTnnspLHHAVKHYNKPIVHILLENGASTDA---RDKCGNTPLHISVGY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 354 PgeEGVQIVELLLHAITDVDAKasdeddtykpgkldllpSSLKlsnepgppqayystdtalpeegGRTALHMACEREddn 433
Cdd:PHA02878 245 C--KDYDILKLLLEHGVDVNAK-----------------SYIL----------------------GLTALHSSIKSE--- 280
|
170 180 190
....*....|....*....|....*....|..
gi 544346158 434 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSI 464
Cdd:PHA02878 281 ----RKLKLLLEYGADINSLnSYKLTPLSSAV 308
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
319-525 |
6.34e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 49.25 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 319 DVDGVRLLLEHGArtDICFPPQLSTlTPLHIAAALPGEEGVQIVELLLHAITDVDAKasdedDTYkpgkldllpsslkls 398
Cdd:PHA03095 26 TVEEVRRLLAAGA--DVNFRGEYGK-TPLHLYLHYSSEKVKDIVRLLLEAGADVNAP-----ERC--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 399 nepgppqayystdtalpeegGRTALHMACEreddNKCARDIVRLLLSHGANPNL-LWSGHSPLS--LSIASGNELVVKEL 475
Cdd:PHA03095 83 --------------------GFTPLHLYLY----NATTLDVIKLLIKAGADVNAkDKVGRTPLHvyLSGFNINPKVIRLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 544346158 476 LTQGADPNlpltkglgsalcvACDLtYEHQ------RNMDSKLALIDRLISHGADI 525
Cdd:PHA03095 139 LRKGADVN-------------ALDL-YGMTplavllKSRNANVELLRLLIDAGADV 180
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
77-155 |
8.30e-06 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 48.03 E-value: 8.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346158 77 QLVQGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK 155
Cdd:COG4642 90 DGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYA 168
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
87-156 |
8.72e-06 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 49.06 E-value: 8.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 87 DGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTmYMKT 156
Cdd:PLN03185 7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGT 75
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
311-482 |
1.24e-05 |
|
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: 48.47 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 311 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdeddtykpgkl 388
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 389 dllpsslkLSNEPGPPQAYYstdtalpeegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 453
Cdd:cd22192 77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133
|
170 180
....*....|....*....|....*....
gi 544346158 454 WSGHSPLSLSIASGNELVVKELLTQGADP 482
Cdd:cd22192 134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
291-482 |
3.15e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.94 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 291 IKLLLRRGADPN----LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVqiVELLL 366
Cdd:PHA03095 30 VRRLLAAGADVNfrgeYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCGFTPLHLYLYNATTLDV--IKLLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 367 HAITDVDAKasdedDTYkpgkldllpsslklsnepgppqayystdtalpeegGRTALHmACEReddNKCAR-DIVRLLLS 445
Cdd:PHA03095 105 KAGADVNAK-----DKV-----------------------------------GRTPLH-VYLS---GFNINpKVIRLLLR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 544346158 446 HGANPN-LLWSGHSPLSLSIASGN---ELvVKELLTQGADP 482
Cdd:PHA03095 141 KGADVNaLDLYGMTPLAVLLKSRNanvEL-LRLLIDAGADV 180
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
419-452 |
3.71e-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: 41.03 E-value: 3.71e-05
10 20 30
....*....|....*....|....*....|....
gi 544346158 419 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 452
Cdd:smart00248 2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
80-150 |
7.40e-05 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 45.98 E-value: 7.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346158 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG 150
Cdd:PLN03185 46 NGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPG 116
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
114-136 |
1.66e-04 |
|
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.
Pssm-ID: 308220 [Multi-domain] Cd Length: 23 Bit Score: 38.93 E-value: 1.66e-04
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
279-453 |
2.33e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.21 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 279 LSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlsTLTPLHIAAAlpg 355
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 356 EEGVQIVELLLHAITDVDakasdeddtykpgkldllpsslklsnepgppqaYYStdtalpEEGGRTALhmaCEREDDNKC 435
Cdd:PHA02875 178 KGDIAICKMLLDSGANID---------------------------------YFG------KNGCVAAL---CYAIENNKI 215
|
170
....*....|....*...
gi 544346158 436 arDIVRLLLSHGANPNLL 453
Cdd:PHA02875 216 --DIVRLFIKRGADCNIM 231
|
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
113-133 |
4.73e-04 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 37.71 E-value: 4.73e-04
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
419-482 |
6.80e-04 |
|
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: 42.94 E-value: 6.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346158 419 GRTALHMACEREDDNkcardIVRLLLSHGAN--------------PNLLWSGHSPLSLSIASGNELVVKELLTQGADP 482
Cdd:cd21882 73 GQTALHIAIENRNLN-----LVRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQP 145
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
303-485 |
1.24e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 303 LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDicfPPQLSTLTPLHIAAALPGEEGVQivELLLHAITDvdakasdeddt 382
Cdd:PHA02878 33 ASLIPFIPLHQAVEARNLDVVKSLLTRGHNVN---QPDHRDLTPLHIICKEPNKLGMK--EMIRSINKC----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 383 ykpgklDLLPSSLKLSnepgppQAYYSTDTALPE-------EGGRTA-LHMACEREDDNKCARDIVRLLLSHGANPNLL- 453
Cdd:PHA02878 97 ------SVFYTLVAIK------DAFNNRNVEIFKiiltnryKNIQTIdLVYIDKKSKDDIIEAEITKLLLSYGADINMKd 164
|
170 180 190
....*....|....*....|....*....|...
gi 544346158 454 -WSGHSPLSLSIASGNELVVKELLTQGADPNLP 485
Cdd:PHA02878 165 rHKGNTALHYATENKDQRLTELLLSYGANVNIP 197
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
419-451 |
1.49e-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: 36.47 E-value: 1.49e-03
10 20 30
....*....|....*....|....*....|...
gi 544346158 419 GRTALHMACEREDdnkcaRDIVRLLLSHGANPN 451
Cdd:pfam13606 2 GNTPLHLAARNGR-----LEIVKLLLENGADIN 29
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
289-479 |
1.89e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.10 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 289 RTIKLLLRRGADPNLCC--VPmQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQLSTltplhiaaalpgeegvQIVELLL 366
Cdd:PHA02874 49 KIVELFIKHGADINHINtkIP-HPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEK----------------DMIKTIL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 367 HAITDVDAKASdEDDTY-----KPGKLDLLPSSLKlsnepgppqayYSTDTALPEEGGRTALHMACEREddnkcARDIVR 441
Cdd:PHA02874 112 DCGIDVNIKDA-ELKTFlhyaiKKGDLESIKMLFE-----------YGADVNIEDDNGCYPIHIAIKHN-----FFDIIK 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 544346158 442 LLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQG 479
Cdd:PHA02874 175 LLLEKGAYANVKdNNGESPLHNAAEYGDYACIKLLIDHG 213
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
308-366 |
2.47e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346158 308 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlstLTPLHIAAAlpgEEGVQIVELLL 366
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
166-198 |
2.75e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|...
gi 544346158 166 DIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 198
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
419-476 |
4.01e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 4.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 544346158 419 GRTALHMACEREDDnkcarDIVRLLLSHGANPNLLW-SGHSPLSLSIASGNELVVKELL 476
Cdd:pfam13637 1 ELTALHAAAASGHL-----ELLRLLLEKGADINAVDgNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
345-375 |
6.88e-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: 34.57 E-value: 6.88e-03
10 20 30
....*....|....*....|....*....|.
gi 544346158 345 TPLHIAAALPGeeGVQIVELLLHAITDVDAK 375
Cdd:pfam00023 4 TPLHLAAGRRG--NLEIVKLLLSKGADVNAR 32
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
438-527 |
8.77e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 39.24 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346158 438 DIVRLLLSHGANPNllWSGH---SPLSLSIASGNEL---VVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSK 511
Cdd:PHA03095 28 EEVRRLLAAGADVN--FRGEygkTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYN---------ATT 96
|
90
....*....|....*.
gi 544346158 512 LALIDRLISHGADILK 527
Cdd:PHA03095 97 LDVIKLLIKAGADVNA 112
|
|
| |
