|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
576-826 |
9.52e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.72 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 576 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 654
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 655 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 733
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 812
Cdd:COG0666 200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
250
....*....|....
gi 1983575845 813 ALIDRLISHGADIL 826
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
52-158 |
8.68e-22 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 96.18 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 129
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218
|
90 100
....*....|....*....|....*....
gi 1983575845 130 lFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642 219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
57-158 |
7.70e-18 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 88.74 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 57 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 135
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107
|
90 100
....*....|....*....|...
gi 1983575845 136 KADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185 108 IQGLQEGPGKYTWANGNVYLGDM 130
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
594-824 |
6.28e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.86 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 594 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 671
Cdd:PHA02875 21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 672 VDakasdeDDTYKPGKLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEREDDNkcardIVRLLLSHGANPN 751
Cdd:PHA02875 94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845 752 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 824
Cdd:PHA02875 163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
318-391 |
8.23e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 8.23e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845 318 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666 85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
719-784 |
4.07e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 4.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 719 GRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:pfam12796 30 GRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
941-981 |
2.00e-09 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 53.58 E-value: 2.00e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1983575845 941 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 981
Cdd:pfam01753 1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
328-403 |
1.04e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 1.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 403
Cdd:pfam12796 5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
348-400 |
1.91e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1983575845 348 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 400
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
611-782 |
1.97e-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: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 611 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdeddtykpgkl 688
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 689 dllpsslkLSNEPGPPQAYYstdtalpeegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 753
Cdd:cd22192 77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133
|
170 180
....*....|....*....|....*....
gi 1983575845 754 WSGHSPLSLSIASGNELVVKELLTQGADP 782
Cdd:cd22192 134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
719-752 |
5.28e-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: 5.28e-05
10 20 30
....*....|....*....|....*....|....
gi 1983575845 719 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 752
Cdd:smart00248 2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
86-108 |
3.52e-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: 38.54 E-value: 3.52e-04
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
85-105 |
9.10e-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: 9.10e-04
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
353-382 |
3.57e-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: 3.57e-03
10 20 30
....*....|....*....|....*....|
gi 1983575845 353 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 382
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
576-826 |
9.52e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.72 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 576 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 654
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 655 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 733
Cdd:COG0666 162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 812
Cdd:COG0666 200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
250
....*....|....
gi 1983575845 813 ALIDRLISHGADIL 826
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
52-158 |
8.68e-22 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 96.18 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 129
Cdd:COG4642 139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218
|
90 100
....*....|....*....|....*....
gi 1983575845 130 lFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642 219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
611-827 |
3.21e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.02 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 611 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKASDeddtykpgkldl 690
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQDND------------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 691 lpsslklsnepgppqayystdtalpeegGRTALHMACEREDdnkcaRDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 769
Cdd:COG0666 153 ----------------------------GNTPLHLAAANGN-----LEIVKLLLEAGADVNARdNDGETPLHLAAENGHL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845 770 LVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADILK 827
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDG-KTALDLAA---------ENGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
611-825 |
4.96e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 91.55 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 611 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKASDeddtykpgkldl 690
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINA---KDDGGNTLLHAAAR---NGDLEIVKLLLEAGADVNARDKD------------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 691 lpsslklsnepgppqayystdtalpeegGRTALHMACEREDDnkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 769
Cdd:COG0666 120 ----------------------------GETPLHLAAYNGNL-----EIVKLLLEAGADVNAQdNDGNTPLHLAAANGNL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 770 LVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADI 825
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDG-ETPLHLAA---------ENGHLEIVKLLLEAGADV 212
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
52-158 |
3.01e-19 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 88.86 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMymktrlf 131
Cdd:COG4642 185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTM------- 257
|
90 100
....*....|....*....|....*..
gi 1983575845 132 qglykadqrfgpgveTYPDGSQDVGLW 158
Cdd:COG4642 258 ---------------TYADGSVYEGEW 269
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
57-158 |
7.70e-18 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 88.74 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 57 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 135
Cdd:PLN03185 28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107
|
90 100
....*....|....*....|...
gi 1983575845 136 KADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185 108 IQGLQEGPGKYTWANGNVYLGDM 130
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
594-824 |
6.28e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.86 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 594 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 671
Cdd:PHA02875 21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 672 VDakasdeDDTYKPGKLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEREDDNkcardIVRLLLSHGANPN 751
Cdd:PHA02875 94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845 752 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 824
Cdd:PHA02875 163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
|
|
| COG4642 |
COG4642 |
Uncharacterized conserved protein [Function unknown]; |
49-158 |
9.49e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443680 [Multi-domain] Cd Length: 271 Bit Score: 66.52 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 49 QLVQGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKT 128
Cdd:COG4642 90 DGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYAD 169
|
90 100 110
....*....|....*....|....*....|.
gi 1983575845 129 -RLFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642 170 gDRYEGEFKNGKRHGQGTLTYANGDVYEGEF 200
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
574-781 |
2.63e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 574 MRRMALSMIERRKRWRTIKLLLRRGADPN------LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQlstLTPL 647
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINsstknnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG---ITPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 648 HIAAALPGEEgVQIVELLLHAITDVDAKASDEDD------TYKPGKLDLLpsSLKLSNepgppQAY------------YS 709
Cdd:PHA03100 111 LYAISKKSNS-YSIVEYLLDNGANVNIKNSDGENllhlylESNKIDLKIL--KLLIDK-----GVDinaknrvnyllsYG 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983575845 710 TDTALPEEGGRTALHMACERedDNKcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGAD 781
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYN--NNP---EFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
318-391 |
8.23e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 8.23e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845 318 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666 85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
324-391 |
3.30e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 62.28 E-value: 3.30e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845 324 MILKAEEGNHEWIcRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666 124 LHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
719-784 |
4.07e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 4.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 719 GRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:pfam12796 30 GRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
611-752 |
4.99e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.05 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 611 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAAlpgEEGVQIVELLL-HAITDVDakasdeddtykpgkld 689
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAAK---NGHLEIVKLLLeHADVNLK---------------- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983575845 690 llpsslklsnepgppqayystdtalpeEGGRTALHMACEreddnKCARDIVRLLLSHGANPNL 752
Cdd:pfam12796 59 ---------------------------DNGRTALHYAAR-----SGHLEIVKLLLEKGADINV 89
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
941-981 |
2.00e-09 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 53.58 E-value: 2.00e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1983575845 941 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 981
Cdd:pfam01753 1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
328-393 |
2.30e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 59.58 E-value: 2.30e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSM 393
Cdd:COG0666 161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
590-675 |
2.92e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.12 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 590 TIKLLLRRGADPNLC-CVPMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLSTLTPLHIAAalpgEEG-VQIVELLLH 667
Cdd:pfam12796 12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82
|
....*...
gi 1983575845 668 AITDVDAK 675
Cdd:pfam12796 83 KGADINVK 90
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
51-127 |
5.52e-09 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 60.23 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 51 VQGVQE------WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTM 124
Cdd:PLN03185 108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187
|
...
gi 1983575845 125 YMK 127
Cdd:PLN03185 188 YPA 190
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
59-158 |
8.67e-09 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 59.46 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 59 DGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTmYMKTR--LFQGLYK 136
Cdd:PLN03185 7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGTDgtTYKGRWR 85
|
90 100
....*....|....*....|..
gi 1983575845 137 ADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185 86 LNLKHGLGYQRYPNGDVFEGSW 107
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
587-784 |
2.74e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.34 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 587 RWRTIKLLLRRGADPNLCCV----PMQVlFLAVKAGDVDGVRLLLEHGArtDICfPPQLSTLTPLHIAAALPGEEgVQIV 662
Cdd:PHA03095 96 TLDVIKLLIKAGADVNAKDKvgrtPLHV-YLSGFNINPKVIRLLLRKGA--DVN-ALDLYGMTPLAVLLKSRNAN-VELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 663 ELLLHAITDVDAKaSDEDDTYkpgkLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEReddNKCARDIVRL 742
Cdd:PHA03095 171 RLLIDAGADVYAV-DDRFRSL----LHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATG---SSCKRSLVLP 242
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1983575845 743 LLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:PHA03095 243 LLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
711-825 |
3.94e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.03 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 711 DTALPEEGGRTALHMACEREDDnkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKG 789
Cdd:COG0666 46 ALALADALGALLLLAAALAGDL-----LVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 1983575845 790 lGSALCVACdltyehqrnMDSKLALIDRLISHGADI 825
Cdd:COG0666 121 -ETPLHLAA---------YNGNLEIVKLLLEAGADV 146
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
579-784 |
5.07e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.13 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 579 LSMIERRKRWRTIKLLLRRGA----DPNLCCVPMQV--LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAA 652
Cdd:PHA03100 1 LYSYIVLTKSRIIKVKNIKYIimedDLNDYSYKKPVlpLYLAKEARNIDVVKILLDNGADINS---STKNNSTPLHYLSN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 653 LPG--EEGVQIVELLLHAITDVDAkasdeddTYKPGKLDLLPSSLKLSNepgppqaYYSTDTALPEEG---------GRT 721
Cdd:PHA03100 78 IKYnlTDVKEIVKLLLEYGANVNA-------PDNNGITPLLYAISKKSN-------SYSIVEYLLDNGanvniknsdGEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 722 ALHMACEREDDNKcarDIVRLLLSHGANPN------LLWS-----------GHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:PHA03100 144 LLHLYLESNKIDL---KILKLLIDKGVDINaknrvnYLLSygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
623-798 |
6.37e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.96 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 623 VRLLLEHGARTDICFPPQLStlTPLHIAAALPGEEgvqIVELLLhaITDVDAKASDEDDTYKpgkldlLPSSLKLSNEPG 702
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGN--TALHYATENKDQR---LTELLL--SYGANVNIPDKTNNSP------LHHAVKHYNKPI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 703 PPQAY-YSTDTALPEEGGRTALHMACEREDDnkcaRDIVRLLLSHGANPNLLWS--GHSPLSLSIASgnELVVKELLTQG 779
Cdd:PHA02878 217 VHILLeNGASTDARDKCGNTPLHISVGYCKD----YDILKLLLEHGVDVNAKSYilGLTALHSSIKS--ERKLKLLLEYG 290
|
170 180
....*....|....*....|....*.
gi 1983575845 780 ADPNL-------PLTKGLGSALCVAC 798
Cdd:PHA02878 291 ADINSlnsykltPLSSAVKQYLCINI 316
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
328-403 |
1.04e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 1.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 403
Cdd:pfam12796 5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
719-752 |
1.09e-06 |
|
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: 1.09e-06
10 20 30
....*....|....*....|....*....|....
gi 1983575845 719 GRTALHMACEREDDnkcaRDIVRLLLSHGANPNL 752
Cdd:pfam00023 2 GNTPLHLAAGRRGN----LEIVKLLLSKGADVNA 31
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
324-391 |
1.18e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 51.49 E-value: 1.18e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845 324 MILKAEEGNHEWICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
348-400 |
1.91e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1983575845 348 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 400
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
723-825 |
2.95e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.26 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 723 LHMACEREDdnkcaRDIVRLLLSHGANPNLLWS-GHSPLSLSIASGNELVVKELLTQgADPNLPlTKGLgSALCVACDLT 801
Cdd:pfam12796 1 LHLAAKNGN-----LELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGR-TALHYAARSG 72
|
90 100
....*....|....*....|....
gi 1983575845 802 YehqrnmdskLALIDRLISHGADI 825
Cdd:pfam12796 73 H---------LEIVKLLLEKGADI 87
|
|
| PLN03185 |
PLN03185 |
phosphatidylinositol phosphate kinase; Provisional |
52-158 |
3.57e-06 |
|
phosphatidylinositol phosphate kinase; Provisional
Pssm-ID: 215619 [Multi-domain] Cd Length: 765 Bit Score: 50.99 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGT-MYMKTRL 130
Cdd:PLN03185 46 NGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKyTWANGNV 125
|
90 100
....*....|....*....|....*...
gi 1983575845 131 FQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185 126 YLGDMKGGKMSGKGTLTWVSGDSYEGQW 153
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
578-764 |
5.18e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 50.26 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 578 ALSMIERRKRWRTIKLLLRRGADPNlccVPMQV----LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAL 653
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVN---IPDKTnnspLHHAVKHYNKPIVHILLENGASTDA---RDKCGNTPLHISVGY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 654 PgeEGVQIVELLLHAITDVDAKasdeddtykpgkldllpSSLKlsnepgppqayystdtalpeegGRTALHMACEREddn 733
Cdd:PHA02878 245 C--KDYDILKLLLEHGVDVNAK-----------------SYIL----------------------GLTALHSSIKSE--- 280
|
170 180 190
....*....|....*....|....*....|..
gi 1983575845 734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSI 764
Cdd:PHA02878 281 ----RKLKLLLEYGADINSLnSYKLTPLSSAV 308
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
619-825 |
1.00e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 49.25 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 619 DVDGVRLLLEHGArtDICFPPQLSTlTPLHIAAALPGEEGVQIVELLLHAITDVDAKasdedDTYkpgkldllpsslkls 698
Cdd:PHA03095 26 TVEEVRRLLAAGA--DVNFRGEYGK-TPLHLYLHYSSEKVKDIVRLLLEAGADVNAP-----ERC--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 699 nepgppqayystdtalpeegGRTALHMACEreddNKCARDIVRLLLSHGANPNL-LWSGHSPLS--LSIASGNELVVKEL 775
Cdd:PHA03095 83 --------------------GFTPLHLYLY----NATTLDVIKLLIKAGADVNAkDKVGRTPLHvyLSGFNINPKVIRLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 776 LTQGADPNlpltkglgsalcvACDLtYEHQ------RNMDSKLALIDRLISHGADI 825
Cdd:PHA03095 139 LRKGADVN-------------ALDL-YGMTplavllKSRNANVELLRLLIDAGADV 180
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
328-381 |
1.22e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 44.72 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1983575845 328 AEEGNHEwICRILKDNFASADVADakGYTVLAAAATHCHNDIVNLLLDCGADVN 381
Cdd:pfam12796 38 AKNGHLE-IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGADIN 88
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
611-782 |
1.97e-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: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 611 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdeddtykpgkl 688
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 689 dllpsslkLSNEPGPPQAYYstdtalpeegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 753
Cdd:cd22192 77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133
|
170 180
....*....|....*....|....*....
gi 1983575845 754 WSGHSPLSLSIASGNELVVKELLTQGADP 782
Cdd:cd22192 134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
591-782 |
4.93e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.94 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 591 IKLLLRRGADPN----LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVqiVELLL 666
Cdd:PHA03095 30 VRRLLAAGADVNfrgeYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCGFTPLHLYLYNATTLDV--IKLLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 667 HAITDVDAKasdedDTYkpgkldllpsslklsnepgppqayystdtalpeegGRTALHmACEReddNKCAR-DIVRLLLS 745
Cdd:PHA03095 105 KAGADVNAK-----DKV-----------------------------------GRTPLH-VYLS---GFNINpKVIRLLLR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1983575845 746 HGANPN-LLWSGHSPLSLSIASGN---ELvVKELLTQGADP 782
Cdd:PHA03095 141 KGADVNaLDLYGMTPLAVLLKSRNanvEL-LRLLIDAGADV 180
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
719-752 |
5.28e-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: 5.28e-05
10 20 30
....*....|....*....|....*....|....
gi 1983575845 719 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 752
Cdd:smart00248 2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
354-391 |
1.10e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1983575845 354 GYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
328-391 |
1.77e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 44.56 E-value: 1.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845 328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666 194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
|
|
| MORN |
pfam02493 |
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ... |
86-108 |
3.52e-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: 38.54 E-value: 3.52e-04
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
579-753 |
3.61e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.21 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 579 LSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlsTLTPLHIAAAlpg 655
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 656 EEGVQIVELLLHAITDVDakasdeddtykpgkldllpsslklsnepgppqaYYStdtalpEEGGRTALhmaCEREDDNKC 735
Cdd:PHA02875 178 KGDIAICKMLLDSGANID---------------------------------YFG------KNGCVAAL---CYAIENNKI 215
|
170
....*....|....*...
gi 1983575845 736 arDIVRLLLSHGANPNLL 753
Cdd:PHA02875 216 --DIVRLFIKRGADCNIM 231
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
719-782 |
8.89e-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: 43.33 E-value: 8.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845 719 GRTALHMACEREDDNkcardIVRLLLSHGAN--------------PNLLWSGHSPLSLSIASGNELVVKELLTQGADP 782
Cdd:cd21882 73 GQTALHIAIENRNLN-----LVRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQP 145
|
|
| MORN |
smart00698 |
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases; |
85-105 |
9.10e-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: 9.10e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
353-385 |
1.32e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 1.32e-03
10 20 30
....*....|....*....|....*....|....
gi 1983575845 353 KGYTVL-AAAATHCHNDIVNLLLDCGADVNKCSD 385
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
358-391 |
1.94e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.56 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|....
gi 1983575845 358 LAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
608-666 |
1.96e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983575845 608 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlstLTPLHIAAAlpgEEGVQIVELLL 666
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
719-751 |
2.12e-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: 2.12e-03
10 20 30
....*....|....*....|....*....|...
gi 1983575845 719 GRTALHMACEREDdnkcaRDIVRLLLSHGANPN 751
Cdd:pfam13606 2 GNTPLHLAARNGR-----LEIVKLLLENGADIN 29
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
589-779 |
2.91e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.10 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 589 RTIKLLLRRGADPNLCC--VPmQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQLSTltplhiaaalpgeegvQIVELLL 666
Cdd:PHA02874 49 KIVELFIKHGADINHINtkIP-HPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEK----------------DMIKTIL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845 667 HAITDVDAKASdEDDTY-----KPGKLDLLPSSLKlsnepgppqayYSTDTALPEEGGRTALHMACEREddnkcARDIVR 741
Cdd:PHA02874 112 DCGIDVNIKDA-ELKTFlhyaiKKGDLESIKMLFE-----------YGADVNIEDDNGCYPIHIAIKHN-----FFDIIK 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1983575845 742 LLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQG 779
Cdd:PHA02874 175 LLLEKGAYANVKdNNGESPLHNAAEYGDYACIKLLIDHG 213
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
719-776 |
3.41e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1983575845 719 GRTALHMACEREDDnkcarDIVRLLLSHGANPNLLW-SGHSPLSLSIASGNELVVKELL 776
Cdd:pfam13637 1 ELTALHAAAASGHL-----ELLRLLLEKGADINAVDgNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
353-382 |
3.57e-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: 3.57e-03
10 20 30
....*....|....*....|....*....|
gi 1983575845 353 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 382
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
339-394 |
3.62e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 3.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845 339 ILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMC 394
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
353-382 |
5.35e-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: 5.35e-03
10 20 30
....*....|....*....|....*....|
gi 1983575845 353 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 382
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
336-394 |
6.10e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 40.39 E-value: 6.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983575845 336 ICRILKDNFASADVADAKGYTVLaaaatHC---HN---DIVNLLLDCGADVNKCSDEGLTALSMC 394
Cdd:PHA03095 65 IVRLLLEAGADVNAPERCGFTPL-----HLylyNAttlDVIKLLIKAGADVNAKDKVGRTPLHVY 124
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
336-391 |
6.85e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.03 E-value: 6.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845 336 ICRILKDNFASADVADAKGYTVLAAAATHC--HNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:PHA03100 88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLL 145
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
645-675 |
9.81e-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: 9.81e-03
10 20 30
....*....|....*....|....*....|.
gi 1983575845 645 TPLHIAAALPGeeGVQIVELLLHAITDVDAK 675
Cdd:pfam00023 4 TPLHLAAGRRG--NLEIVKLLLSKGADVNAR 32
|
|
|