|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
604-807 |
3.31e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.10 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 604 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 682
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 683 gEEG-VQIVELLLHAITDVDAK----------ASDEDDTykpgkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 750
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARdndgetplhlAAENGHL--------EIVKLLLEAGADVNAKdNDGKTALDLAAENGNL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462574024 751 LVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKLALIDRLISHGADIL 807
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-186 |
9.98e-22 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 96.18 E-value: 9.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 157
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218
|
90 100
....*....|....*....|....*....
gi 2462574024 158 lFQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642 219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
85-186 |
1.23e-17 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 88.35 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 85 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 163
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107
|
90 100
....*....|....*....|...
gi 2462574024 164 KADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185 108 IQGLQEGPGKYTWANGNVYLGDM 130
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
607-805 |
2.36e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.02 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 607 LSMIERRKRWRTIKLLLRRGADPNLCCVPMQV-LFLAVKAGDVDGVRLLLEHGARTDICFPPQlsTLTPLHIAAALpgeE 685
Cdd:PHA02875 39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESeLHDAVEEGDVKAVEELLDLGKFADDVFYKD--GMTPLHLATIL---K 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 686 GVQIVELLLHAITDVDAKASDEDDTYKPGKCARDI--VRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGAD 762
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIkgIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462574024 763 PNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 805
Cdd:PHA02875 194 IDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
639-765 |
1.21e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 639 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEGVQivelllhaitdvdakasdeddtykpgkcar 718
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAA----KNGHL------------------------------ 43
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462574024 719 DIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 765
Cdd:pfam12796 44 EIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
346-419 |
8.06e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 8.06e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462574024 346 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666 85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
356-431 |
1.02e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 1.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 356 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 431
Cdd:pfam12796 5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
376-428 |
1.87e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462574024 376 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 428
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
639-763 |
1.89e-04 |
|
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: 45.39 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 639 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALPGEEGVQIV-----ELLLHAITdvdakasdeDDTY 711
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALYDNLEAAVVLmeaapELVNEPMT---------SDLY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 712 KpGKCARDI---------VRLLLSHGA---NP------------NLLWSGHSPLSLSIASGNELVVKELLTQGADP 763
Cdd:cd22192 88 Q-GETALHIavvnqnlnlVRELIARGAdvvSPratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
114-136 |
5.27e-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: 5.27e-04
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
113-133 |
1.24e-03 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 36.93 E-value: 1.24e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
381-410 |
3.51e-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: 3.51e-03
10 20 30
....*....|....*....|....*....|
gi 2462574024 381 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 410
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
604-807 |
3.31e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.10 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 604 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 682
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 683 gEEG-VQIVELLLHAITDVDAK----------ASDEDDTykpgkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 750
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARdndgetplhlAAENGHL--------EIVKLLLEAGADVNAKdNDGKTALDLAAENGNL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462574024 751 LVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKLALIDRLISHGADIL 807
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-186 |
9.98e-22 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 96.18 E-value: 9.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 157
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218
|
90 100
....*....|....*....|....*....
gi 2462574024 158 lFQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642 219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
639-808 |
8.53e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.78 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 639 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAK----------ASDED 708
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQdndgntplhlAAANG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 709 DTykpgkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGlGSALCVACdltyehqr 787
Cdd:COG0666 165 NL--------EIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTALDLAA-------- 227
|
170 180
....*....|....*....|.
gi 2462574024 788 nMDSKLALIDRLISHGADILK 808
Cdd:COG0666 228 -ENGNLEIVKLLLEAGADLNA 247
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-186 |
3.33e-19 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 88.86 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMymktrlf 159
Cdd:COG4642 185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTM------- 257
|
90 100
....*....|....*....|....*..
gi 2462574024 160 qglykadqrfgpgveTYPDGSQDVGLW 186
Cdd:COG4642 258 ---------------TYADGSVYEGEW 269
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
80-186 |
8.23e-19 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 87.70 E-value: 8.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKT-RL 158
Cdd:COG4642 116 GGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANgDV 195
|
90 100
....*....|....*....|....*...
gi 2462574024 159 FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642 196 YEGEFKNGQRHGQGTYTYADGDRYEGEF 223
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
85-186 |
1.23e-17 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 88.35 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 85 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 163
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107
|
90 100
....*....|....*....|...
gi 2462574024 164 KADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185 108 IQGLQEGPGKYTWANGNVYLGDM 130
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
607-805 |
2.36e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.02 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 607 LSMIERRKRWRTIKLLLRRGADPNLCCVPMQV-LFLAVKAGDVDGVRLLLEHGARTDICFPPQlsTLTPLHIAAALpgeE 685
Cdd:PHA02875 39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESeLHDAVEEGDVKAVEELLDLGKFADDVFYKD--GMTPLHLATIL---K 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 686 GVQIVELLLHAITDVDAKASDEDDTYKPGKCARDI--VRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGAD 762
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIkgIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462574024 763 PNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 805
Cdd:PHA02875 194 IDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
77-186 |
1.07e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 66.52 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 77 QLVQGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKT 156
Cdd:COG4642 90 DGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYAD 169
|
90 100 110
....*....|....*....|....*....|.
gi 2462574024 157 -RLFQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642 170 gDRYEGEFKNGKRHGQGTLTYANGDVYEGEF 200
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
639-765 |
1.21e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 639 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEGVQivelllhaitdvdakasdeddtykpgkcar 718
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAA----KNGHL------------------------------ 43
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462574024 719 DIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 765
Cdd:pfam12796 44 EIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
346-419 |
8.06e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 8.06e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462574024 346 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666 85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
352-419 |
3.23e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 62.28 E-value: 3.23e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462574024 352 MILKAEEGNHEWIcRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666 124 LHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
602-765 |
3.43e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.15 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 602 MRRMALSMIERRKRWRTIKLLLRRGADPN------LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQlstLTPL 675
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINsstknnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG---ITPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 676 HIAAALPGEEgVQIVELLLHAITDVDAKASD------------EDDTykpgkcarDIVRLLLSHGANPN------LLWS- 736
Cdd:PHA03100 111 LYAISKKSNS-YSIVEYLLDNGANVNIKNSDgenllhlylesnKIDL--------KILKLLIDKGVDINaknrvnYLLSy 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462574024 737 ----------GHSPLSLSIASGNELVVKELLTQGADPNL 765
Cdd:PHA03100 182 gvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
356-421 |
2.25e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 59.58 E-value: 2.25e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 356 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSM 421
Cdd:COG0666 161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
618-703 |
2.87e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.12 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 618 TIKLLLRRGADPNLC-CVPMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLSTLTPLHIAAalpgEEG-VQIVELLLH 695
Cdd:pfam12796 12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82
|
....*...
gi 2462574024 696 AITDVDAK 703
Cdd:pfam12796 83 KGADINVK 90
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
79-155 |
7.72e-09 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 59.85 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 79 VQGVQE------WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTM 152
Cdd:PLN03185 108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187
|
...
gi 2462574024 153 YMK 155
Cdd:PLN03185 188 YPA 190
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
87-186 |
1.17e-08 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 59.08 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 87 DGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTmYMKTR--LFQGLYK 164
Cdd:PLN03185 7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGTDgtTYKGRWR 85
|
90 100
....*....|....*....|..
gi 2462574024 165 ADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185 86 LNLKHGLGYQRYPNGDVFEGSW 107
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
653-806 |
2.60e-08 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 56.50 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 653 LLLEHGARTDICFPPQLSTLTPLHIAAALPGEEGVQIVELLLHAITDVDAKASDEDDTYKPGKCARDIVRLLLSHGANPN 732
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462574024 733 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADI 806
Cdd:COG0666 82 AKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAA---------YNGNLEIVKLLLEAGADV 146
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
647-806 |
1.37e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.03 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 647 DVDGVRLLLEHGArtDICFPPQLSTlTPLHIAAALPGEEGVQIVELLLHAITDVDAKASDED---DTYKPGKCARDIVRL 723
Cdd:PHA03095 26 TVEEVRRLLAAGA--DVNFRGEYGK-TPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFtplHLYLYNATTLDVIKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 724 LLSHGANPNL-LWSGHSPLS--LSIASGNELVVKELLTQGADPNlpltkglgsalcvACDLtYEHQ------RNMDSKLA 794
Cdd:PHA03095 103 LIKAGADVNAkDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVN-------------ALDL-YGMTplavllKSRNANVE 168
|
170
....*....|..
gi 2462574024 795 LIDRLISHGADI 806
Cdd:PHA03095 169 LLRLLIDAGADV 180
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
619-779 |
1.71e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.89 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 619 IKLLLRRGADPNLCC--VPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVQIVeLLLHA 696
Cdd:PHA02878 150 TKLLLSYGADINMKDrhKGNTALHYATENKDQRLTELLLSYGANVNI---PDKTNNSPLHHAVKHYNKPIVHIL-LENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 697 ITDVDAKASDEDDTYKPGKCAR-DIVRLLLSHGANPNLLWS--GHSPLSLSIASgnELVVKELLTQGADPNL-------P 766
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKS--ERKLKLLLEYGADINSlnsykltP 303
|
170
....*....|...
gi 2462574024 767 LTKGLGSALCVAC 779
Cdd:PHA02878 304 LSSAVKQYLCINI 316
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
606-745 |
2.56e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 606 ALSMIERRKRWRTIKLLLRRGADPNlccVPMQV----LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAL 681
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVN---IPDKTnnspLHHAVKHYNKPIVHILLENGASTDA---RDKCGNTPLHISVGY 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 682 PgeEGVQIVELLLHAITDVDAKASDEDDT-YKPGKCARDIVRLLLSHGANPNLL-WSGHSPLSLSI 745
Cdd:PHA02878 245 C--KDYDILKLLLEHGVDVNAKSYILGLTaLHSSIKSERKLKLLLEYGADINSLnSYKLTPLSSAV 308
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
607-734 |
2.71e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.23 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 607 LSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlsTLTPLHIAAAlpg 683
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462574024 684 EEGVQIVELLLHAITDVDAKASDEDDT---YKPGKCARDIVRLLLSHGANPNLL 734
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDYFGKNGCVAalcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
618-765 |
7.68e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.72 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 618 TIKLLLRRGADPNLC----CVPMQVlFLAVKAGDVDGVRLLLEHGAR---TDICFppqlstLTPLHIAAALPgEEGVQIV 690
Cdd:PHA03095 134 VIRLLLRKGADVNALdlygMTPLAV-LLKSRNANVELLRLLIDAGADvyaVDDRF------RSLLHHHLQSF-KPRARIV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 691 ELLLHAITDVDAKASDEDDTY----KPGKCARDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNL 765
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLhsmaTGSSCKRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
356-431 |
1.02e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 1.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 356 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 431
Cdd:pfam12796 5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
376-428 |
1.87e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462574024 376 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 428
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
80-186 |
4.62e-06 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 50.60 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 80 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGT-MYMKTRL 158
Cdd:PLN03185 46 NGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKyTWANGNV 125
|
90 100
....*....|....*....|....*...
gi 2462574024 159 FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185 126 YLGDMKGGKMSGKGTLTWVSGDSYEGQW 153
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
356-409 |
1.20e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 44.72 E-value: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462574024 356 AEEGNHEwICRILKDNFASADVADakGYTVLAAAATHCHNDIVNLLLDCGADVN 409
Cdd:pfam12796 38 AKNGHLE-IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGADIN 88
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
382-419 |
1.20e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2462574024 382 GYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
356-419 |
1.74e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 44.56 E-value: 1.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462574024 356 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666 194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
639-763 |
1.89e-04 |
|
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: 45.39 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 639 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALPGEEGVQIV-----ELLLHAITdvdakasdeDDTY 711
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALYDNLEAAVVLmeaapELVNEPMT---------SDLY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 712 KpGKCARDI---------VRLLLSHGA---NP------------NLLWSGHSPLSLSIASGNELVVKELLTQGADP 763
Cdd:cd22192 88 Q-GETALHIavvnqnlnlVRELIARGAdvvSPratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
114-136 |
5.27e-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: 5.27e-04
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
688-806 |
5.40e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.72 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 688 QIVELLLHAITDVDAKASDEDDT---YKPGKCARDIVRLLLSHGANPNLLWSG-HSPLSLSIASGNELVVKELLTQGADP 763
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTalhYATENKDQRLTELLLSYGANVNIPDKTnNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462574024 764 NLpltkglgSALCVACDLTYEHQRNMDskLALIDRLISHGADI 806
Cdd:PHA02878 228 DA-------RDKCGNTPLHISVGYCKD--YDILKLLLEHGVDV 261
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
592-727 |
8.91e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574024 592 PCTSSFDKGTMRRMALSMIErrKRWRTIKLLLRRGADPNLCCVPMQVL------FLAVK------AGDVDGVRLLLEHGA 659
Cdd:PTZ00322 29 AKPISFERMAAIQEEIARID--THLEALEATENKDATPDHNLTTEEVIdpvvahMLTVElcqlaaSGDAVGARILLTGGA 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462574024 660 RTDIcfpPQLSTLTPLHIAAALpGEegVQIVELLLHaiTDVDAKASDEDDTyKPGKCA-----RDIVRLLLSH 727
Cdd:PTZ00322 107 DPNC---RDYDGRTPLHIACAN-GH--VQVVRVLLE--FGADPTLLDKDGK-TPLELAeengfREVVQLLSRH 170
|
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
113-133 |
1.24e-03 |
|
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
Pssm-ID: 197832 [Multi-domain] Cd Length: 22 Bit Score: 36.93 E-value: 1.24e-03
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
381-413 |
1.29e-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: 1.29e-03
10 20 30
....*....|....*....|....*....|....
gi 2462574024 381 KGYTVL-AAAATHCHNDIVNLLLDCGADVNKCSD 413
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
386-419 |
1.90e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.56 E-value: 1.90e-03
10 20 30
....*....|....*....|....*....|....
gi 2462574024 386 LAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
636-694 |
2.33e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.87 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462574024 636 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlstLTPLHIAAAlpgEEGVQIVELLL 694
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
381-410 |
3.51e-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: 3.51e-03
10 20 30
....*....|....*....|....*....|
gi 2462574024 381 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 410
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
367-422 |
3.56e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 3.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462574024 367 ILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMC 422
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
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| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
381-410 |
5.26e-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: 5.26e-03
10 20 30
....*....|....*....|....*....|
gi 2462574024 381 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 410
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
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| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
364-422 |
5.98e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 40.39 E-value: 5.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462574024 364 ICRILKDNFASADVADAKGYTVLaaaatHC---HN---DIVNLLLDCGADVNKCSDEGLTALSMC 422
Cdd:PHA03095 65 IVRLLLEAGADVNAPERCGFTPL-----HLylyNAttlDVIKLLIKAGADVNAKDKVGRTPLHVY 124
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| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
364-419 |
6.71e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.03 E-value: 6.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462574024 364 ICRILKDNFASADVADAKGYTVLAAAATHC--HNDIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:PHA03100 88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLL 145
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| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
673-703 |
9.64e-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: 9.64e-03
10 20 30
....*....|....*....|....*....|.
gi 2462574024 673 TPLHIAAALPGeeGVQIVELLLHAITDVDAK 703
Cdd:pfam00023 4 TPLHLAAGRRG--NLEIVKLLLSKGADVNAR 32
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