|
Name |
Accession |
Description |
Interval |
E-value |
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
159-265 |
8.14e-22 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 96.18 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 159 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 236
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218
|
90 100
....*....|....*....|....*....
gi 2217328645 237 lFQGLYKADQRFGPGVETYPDGSQDVGLW 265
Cdd:COG4642 219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
683-843 |
2.61e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 89.63 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 683 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 761
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 762 gEEG-VQIVELLLHAITDVDAK----------ASDEDDTykpgkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGN- 828
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARdndgetplhlAAENGHL--------EIVKLLLEAGADVNAKdNDGKTALDLAAENGNl 232
|
170
....*....|....*
gi 2217328645 829 ELIDRLISHGADILK 843
Cdd:COG0666 233 EIVKLLLEAGADLNA 247
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
164-265 |
1.15e-17 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 88.35 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 164 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 242
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107
|
90 100
....*....|....*....|...
gi 2217328645 243 KADQRFGPGVETYPDGSQDVGLW 265
Cdd:PLN03185 108 IQGLQEGPGKYTWANGNVYLGDM 130
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
425-498 |
7.72e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 7.72e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217328645 425 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:COG0666 85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
698-841 |
1.77e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 64.28 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 698 IKLLLRRGADPN----LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVqiVELLL 773
Cdd:PHA03095 30 VRRLLAAGADVNfrgeYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCGFTPLHLYLYNATTLDV--IKLLI 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217328645 774 HAITDVDAKaSDEDDT----YKPGKCAR-DIVRLLLSHGANPN-LLWSGHSPLSLSIASGN---ELIDRLISHGADI 841
Cdd:PHA03095 105 KAGADVNAK-DKVGRTplhvYLSGFNINpKVIRLLLRKGADVNaLDLYGMTPLAVLLKSRNanvELLRLLIDAGADV 180
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
718-841 |
1.32e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.89 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 718 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEGVQivelllhaitdvdakasdeddtykpgkcar 797
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAA----KNGHL------------------------------ 43
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217328645 798 DIVRLLLSHgANPNLLWSGHSPLSLSIASGN-ELIDRLISHGADI 841
Cdd:pfam12796 44 EIVKLLLEH-ADVNLKDNGRTALHYAARSGHlEIVKLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
435-510 |
9.84e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 9.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328645 435 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 510
Cdd:pfam12796 5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
455-507 |
1.79e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217328645 455 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 507
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
718-841 |
7.31e-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: 46.54 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 718 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALPGEEGVQIV-----ELLLHAITdvdakasdeDDTY 790
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALYDNLEAAVVLmeaapELVNEPMT---------SDLY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328645 791 KpGKCARDI---------VRLLLSHGA---NP------------NLLWSGHSPLSLSIASGNELIDR-LISHGADI 841
Cdd:cd22192 88 Q-GETALHIavvnqnlnlVRELIARGAdvvSPratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRlLIEHGADI 162
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
193-215 |
4.10e-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: 38.16 E-value: 4.10e-04
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
192-212 |
9.62e-04 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 37.32 E-value: 9.62e-04
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
460-489 |
3.39e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|
gi 2217328645 460 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 489
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
159-265 |
8.14e-22 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 96.18 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 159 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 236
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218
|
90 100
....*....|....*....|....*....
gi 2217328645 237 lFQGLYKADQRFGPGVETYPDGSQDVGLW 265
Cdd:COG4642 219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
72-265 |
1.54e-19 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 89.63 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 72 GGGWKTTDMEGAhASLSLEDEVSGAGSRQRPLEGKGGETPAAEEPGSLKNYAVFATRDVSAAPEKEEEEAEGPLRAQDLR 151
Cdd:COG4642 23 EGGLAAAGGEGG-GGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 152 ESYIQLV-------QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSH 224
Cdd:COG4642 102 GGGGGGKkggggggGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217328645 225 REGYGTMYMKT-RLFQGLYKADQRFGPGVETYPDGSQDVGLW 265
Cdd:COG4642 182 RHGQGTLTYANgDVYEGEFKNGQRHGQGTYTYADGDRYEGEF 223
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
683-843 |
2.61e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 89.63 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 683 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 761
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 762 gEEG-VQIVELLLHAITDVDAK----------ASDEDDTykpgkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGN- 828
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARdndgetplhlAAENGHL--------EIVKLLLEAGADVNAKdNDGKTALDLAAENGNl 232
|
170
....*....|....*
gi 2217328645 829 ELIDRLISHGADILK 843
Cdd:COG0666 233 EIVKLLLEAGADLNA 247
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
159-265 |
2.82e-19 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 88.86 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 159 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMymktrlf 238
Cdd:COG4642 185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTM------- 257
|
90 100
....*....|....*....|....*..
gi 2217328645 239 qglykadqrfgpgveTYPDGSQDVGLW 265
Cdd:COG4642 258 ---------------TYADGSVYEGEW 269
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
164-265 |
1.15e-17 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 88.35 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 164 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 242
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107
|
90 100
....*....|....*....|...
gi 2217328645 243 KADQRFGPGVETYPDGSQDVGLW 265
Cdd:PLN03185 108 IQGLQEGPGKYTWANGNVYLGDM 130
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
425-498 |
7.72e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 7.72e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217328645 425 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:COG0666 85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
698-841 |
1.77e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 64.28 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 698 IKLLLRRGADPN----LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVqiVELLL 773
Cdd:PHA03095 30 VRRLLAAGADVNfrgeYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCGFTPLHLYLYNATTLDV--IKLLI 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217328645 774 HAITDVDAKaSDEDDT----YKPGKCAR-DIVRLLLSHGANPN-LLWSGHSPLSLSIASGN---ELIDRLISHGADI 841
Cdd:PHA03095 105 KAGADVNAK-DKVGRTplhvYLSGFNINpKVIRLLLRKGADVNaLDLYGMTPLAVLLKSRNanvELLRLLIDAGADV 180
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
696-841 |
1.83e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 696 RTIKLLLRRGADPNLC----CVPMQVLfLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAALPGEEgVQIVEL 771
Cdd:PHA03100 87 EIVKLLLEYGANVNAPdnngITPLLYA-ISKKSNSYSIVEYLLDNGANVNIKNS---DGENLLHLYLESNKID-LKILKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 772 LLHAITDVDAKAS-----------DEDD----------TYKPGKcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGN- 828
Cdd:PHA03100 162 LIDKGVDINAKNRvnyllsygvpiNIKDvygftplhyaVYNNNP---EFVKYLLDLGANPNLVnKYGDTPLHIAILNNNk 238
|
170
....*....|...
gi 2217328645 829 ELIDRLISHGADI 841
Cdd:PHA03100 239 EIFKLLLNNGPSI 251
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
431-498 |
3.10e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 62.28 E-value: 3.10e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217328645 431 MILKAEEGNHEWIcRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:COG0666 124 LHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
718-841 |
1.32e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.89 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 718 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEGVQivelllhaitdvdakasdeddtykpgkcar 797
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAA----KNGHL------------------------------ 43
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217328645 798 DIVRLLLSHgANPNLLWSGHSPLSLSIASGN-ELIDRLISHGADI 841
Cdd:pfam12796 44 EIVKLLLEH-ADVNLKDNGRTALHYAARSGHlEIVKLLLEKGADI 87
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
435-500 |
2.16e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 59.58 E-value: 2.16e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328645 435 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSM 500
Cdd:COG0666 161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
697-782 |
2.76e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.12 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 697 TIKLLLRRGADPNLC-CVPMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLSTLTPLHIAAalpgEEG-VQIVELLLH 774
Cdd:pfam12796 12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82
|
....*...
gi 2217328645 775 AITDVDAK 782
Cdd:pfam12796 83 KGADINVK 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
691-812 |
6.35e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 58.43 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 691 RRKRWRTIKLLLRRGADPNLCCVPMQ-VLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEgvqIV 769
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGEtPLHLAAENGHLEIVKLLLEAGADVNA---KDNDGKTALDLAAENGNLE---IV 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217328645 770 ELLLHAITDVDAKASDEDDT--YKPGKCARDIVRLLLSHGANPNL 812
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTAllLAAAAGAALIVKLLLLALLLLAA 280
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
158-234 |
7.18e-09 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 59.85 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 158 VQGVQE------WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTM 231
Cdd:PLN03185 108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187
|
...
gi 2217328645 232 YMK 234
Cdd:PLN03185 188 YPA 190
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
166-265 |
1.10e-08 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 59.08 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 166 DGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTmYMKTR--LFQGLYK 243
Cdd:PLN03185 7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGTDgtTYKGRWR 85
|
90 100
....*....|....*....|..
gi 2217328645 244 ADQRFGPGVETYPDGSQDVGLW 265
Cdd:PLN03185 86 LNLKHGLGYQRYPNGDVFEGSW 107
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
685-837 |
1.81e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 57.97 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 685 ALSMIERRKRWRTIKLLLRRGADPNlccVPMQV----LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAL 760
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVN---IPDKTnnspLHHAVKHYNKPIVHILLENGASTDA---RDKCGNTPLHISVGY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 761 PgeEGVQIVELLLHAITDVDAKASDEDDT-YKPGKCARDIVRLLLSHGANPNLL-WSGHSPLSLSIA--SGNELIDRLIS 836
Cdd:PHA02878 245 C--KDYDILKLLLEHGVDVNAKSYILGLTaLHSSIKSERKLKLLLEYGADINSLnSYKLTPLSSAVKqyLCINIGRILIS 322
|
.
gi 2217328645 837 H 837
Cdd:PHA02878 323 N 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
686-813 |
2.59e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.23 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 686 LSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlsTLTPLHIAAAlpg 762
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217328645 763 EEGVQIVELLLHAITDVDAKASDEDDT---YKPGKCARDIVRLLLSHGANPNLL 813
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDYFGKNGCVAalcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
681-841 |
5.46e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.13 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 681 MRRMALSMIERRKRWRTIKLLLRRGADPN------LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQlstLTPL 754
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINsstknnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG---ITPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 755 HIAAALPGEEgVQIVELLLHAITDVDAKASD------------EDDTykpgkcarDIVRLLLSHGANPNLLwsghsplsl 822
Cdd:PHA03100 111 LYAISKKSNS-YSIVEYLLDNGANVNIKNSDgenllhlylesnKIDL--------KILKLLIDKGVDINAK--------- 172
|
170
....*....|....*....
gi 2217328645 823 siasgNElIDRLISHGADI 841
Cdd:PHA03100 173 -----NR-VNYLLSYGVPI 185
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
686-841 |
5.98e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.07 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 686 LSMIERRKRWRTIKLLLRRGADPNLCCVPMQV-LFLAVKAGDVDGVRLLLEHGARTDICFPPQlsTLTPLHIAAALpgeE 764
Cdd:PHA02875 39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESeLHDAVEEGDVKAVEELLDLGKFADDVFYKD--GMTPLHLATIL---K 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 765 GVQIVELLLHAITDVDAKASDEDDTYKPGKCARDI--VRLLLSHGANPNLL-WSGHSPLSLSIASGNELIDR-LISHGAD 840
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIkgIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKmLLDSGAN 193
|
.
gi 2217328645 841 I 841
Cdd:PHA02875 194 I 194
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
435-510 |
9.84e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 9.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328645 435 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 510
Cdd:pfam12796 5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
431-498 |
1.11e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 51.49 E-value: 1.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217328645 431 MILKAEEGNHEWICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
686-841 |
1.44e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 686 LSMIERRKRWRTIKLLLRRGA----DPNLCCVPMQV--LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAA 759
Cdd:PHA03100 1 LYSYIVLTKSRIIKVKNIKYIimedDLNDYSYKKPVlpLYLAKEARNIDVVKILLDNGADINS---STKNNSTPLHYLSN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 760 LPG--EEGVQIVELLLHAITDVDAKasdEDDTYKP-------GKCARDIVRLLLSHGANPNLLWS-GHSPLSLSIASGN- 828
Cdd:PHA03100 78 IKYnlTDVKEIVKLLLEYGANVNAP---DNNGITPllyaiskKSNSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKi 154
|
170
....*....|....*
gi 2217328645 829 --ELIDRLISHGADI 841
Cdd:PHA03100 155 dlKILKLLIDKGVDI 169
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
455-507 |
1.79e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217328645 455 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 507
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
715-840 |
2.32e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.15 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 715 MQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALpgeEGVQIVELLL--HAITDVDAKASDEDDTYKP 792
Cdd:PHA02875 103 MTPLHLATILKKLDIMKLLIARGADPDI---PNTDKFSPLHLAVMM---GDIKGIELLIdhKACLDIEDCCGCTPLIIAM 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217328645 793 GKCARDIVRLLLSHGANPNLLWSGHSPLSLSIASGNELID---RLISHGAD 840
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDivrLFIKRGAD 227
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
159-265 |
4.46e-06 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 50.60 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 159 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGT-MYMKTRL 237
Cdd:PLN03185 46 NGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKyTWANGNV 125
|
90 100
....*....|....*....|....*...
gi 2217328645 238 FQGLYKADQRFGPGVETYPDGSQDVGLW 265
Cdd:PLN03185 126 YLGDMKGGKMSGKGTLTWVSGDSYEGQW 153
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
697-841 |
4.62e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 50.41 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 697 TIKLLLRRGADPNLC----CVPMQVlFLAVKAGDVDGVRLLLEHGAR---TDICFppqlstLTPLHIAAALPgEEGVQIV 769
Cdd:PHA03095 134 VIRLLLRKGADVNALdlygMTPLAV-LLKSRNANVELLRLLIDAGADvyaVDDRF------RSLLHHHLQSF-KPRARIV 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217328645 770 ELLLHAITDVDAKASDEDDTY----KPGKCARDIVRLLLSHGANPNLL-WSGHSPLSLSIASGN-ELIDRLISHGADI 841
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLhsmaTGSSCKRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNpRACRRLIALGADI 283
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
435-488 |
1.15e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 44.72 E-value: 1.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217328645 435 AEEGNHEwICRILKDNFASADVADakGYTVLAAAATHCHNDIVNLLLDCGADVN 488
Cdd:pfam12796 38 AKNGHLE-IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGADIN 88
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
694-841 |
3.14e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 47.71 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 694 RWRTIKLLLRRGADPNLCCV----PMQVlFLAVKAGDVDGVRLLLEHGArtDICfPPQLSTLTPLHIAAALPGEEgVQIV 769
Cdd:PHA03095 96 TLDVIKLLIKAGADVNAKDKvgrtPLHV-YLSGFNINPKVIRLLLRKGA--DVN-ALDLYGMTPLAVLLKSRNAN-VELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 770 ELLLHAITDVDAKaSDEDDT--------YKPGKCardIVRLLLSHGANPNLLWSGHSPLSLSIASG----NELIDRLISH 837
Cdd:PHA03095 171 RLLIDAGADVYAV-DDRFRSllhhhlqsFKPRAR---IVRELIRAGCDPAATDMLGNTPLHSMATGssckRSLVLPLLIA 246
|
....
gi 2217328645 838 GADI 841
Cdd:PHA03095 247 GISI 250
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
701-839 |
4.04e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 701 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 778
Cdd:PHA02875 21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328645 779 VDakasdeDDTYKPGKCAR---------DIVRLLLSHGANPNLLWSGH-SPLSLSIASGN-ELIDRLISHGA 839
Cdd:PHA02875 94 AD------DVFYKDGMTPLhlatilkklDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDiKGIELLIDHKA 159
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
698-841 |
4.85e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.80 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 698 IKLLLRRGADPNLCC--VPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVQIVeLLLHA 775
Cdd:PHA02878 150 TKLLLSYGADINMKDrhKGNTALHYATENKDQRLTELLLSYGANVNI---PDKTNNSPLHHAVKHYNKPIVHIL-LENGA 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328645 776 ITDVDAKASDEDDTYKPGKCAR-DIVRLLLSHGANPNLLWS--GHSPLSLSIASGNELiDRLISHGADI 841
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSERKL-KLLLEYGADI 293
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
718-841 |
7.31e-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: 46.54 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 718 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALPGEEGVQIV-----ELLLHAITdvdakasdeDDTY 790
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALYDNLEAAVVLmeaapELVNEPMT---------SDLY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328645 791 KpGKCARDI---------VRLLLSHGA---NP------------NLLWSGHSPLSLSIASGNELIDR-LISHGADI 841
Cdd:cd22192 88 Q-GETALHIavvnqnlnlVRELIARGAdvvSPratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRlLIEHGADI 162
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
461-498 |
9.35e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 9.35e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2217328645 461 GYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
435-498 |
1.67e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 44.56 E-value: 1.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217328645 435 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:COG0666 194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
671-846 |
1.92e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 671 PCTSSFDKGTMRRMALSMIErrKRWRTIKLLLRRGADPNLCCVPMQVL------FLAVK------AGDVDGVRLLLEHGA 738
Cdd:PTZ00322 29 AKPISFERMAAIQEEIARID--THLEALEATENKDATPDHNLTTEEVIdpvvahMLTVElcqlaaSGDAVGARILLTGGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328645 739 RTDIcfpPQLSTLTPLHIAAALpGEegVQIVELLLHaiTDVDAKASDEDDTyKPGKCA-----RDIVRLLLSHGANPNLL 813
Cdd:PTZ00322 107 DPNC---RDYDGRTPLHIACAN-GH--VQVVRVLLE--FGADPTLLDKDGK-TPLELAeengfREVVQLLSRHSQCHFEL 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217328645 814 WSGHSPLSLSIASGNELIDRLISHGAD---ILKPVM 846
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEDSPISSHHPDfsaVPQPMM 213
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
193-215 |
4.10e-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: 38.16 E-value: 4.10e-04
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
192-212 |
9.62e-04 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 37.32 E-value: 9.62e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
460-492 |
1.25e-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: 37.27 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....
gi 2217328645 460 KGYTVL-AAAATHCHNDIVNLLLDCGADVNKCSD 492
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
715-773 |
1.69e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328645 715 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlstLTPLHIAAAlpgEEGVQIVELLL 773
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
465-498 |
1.83e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.56 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|....
gi 2217328645 465 LAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
460-489 |
3.39e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|
gi 2217328645 460 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 489
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
446-501 |
3.43e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 3.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328645 446 ILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMC 501
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
460-489 |
5.08e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 5.08e-03
10 20 30
....*....|....*....|....*....|
gi 2217328645 460 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 489
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
443-501 |
5.73e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 40.39 E-value: 5.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217328645 443 ICRILKDNFASADVADAKGYTVLaaaatHC---HN---DIVNLLLDCGADVNKCSDEGLTALSMC 501
Cdd:PHA03095 65 IVRLLLEAGADVNAPERCGFTPL-----HLylyNAttlDVIKLLIKAGADVNAKDKVGRTPLHVY 124
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
443-498 |
6.44e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.03 E-value: 6.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217328645 443 ICRILKDNFASADVADAKGYTVLAAAATHC--HNDIVNLLLDCGADVNKCSDEGLTAL 498
Cdd:PHA03100 88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLL 145
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
752-782 |
9.31e-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: 9.31e-03
10 20 30
....*....|....*....|....*....|.
gi 2217328645 752 TPLHIAAALPGeeGVQIVELLLHAITDVDAK 782
Cdd:pfam00023 4 TPLHLAAGRRG--NLEIVKLLLSKGADVNAR 32
|
|
|