|
Name |
Accession |
Description |
Interval |
E-value |
| GPCR_chapero_1 |
pfam11904 |
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ... |
156-470 |
4.99e-129 |
|
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.
Pssm-ID: 463391 Cd Length: 298 Bit Score: 380.06 E-value: 4.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 156 RVDITLLGFENMSWIRGRRSFIFKGED-NWAELMEVNHDDKVVTTERfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 234
Cdd:pfam11904 1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904 73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 308 EHQFGAQGQDLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEEFPLSLvEQVIPIIDLMA 387
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 388 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSashiTNFEVDQSVFEIP 467
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294
|
...
gi 530401512 468 ESY 470
Cdd:pfam11904 295 SGY 297
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-119 |
5.31e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 81.92 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530401512 85 GDPEMVYTVLQH------RDYHNTS----MALEGVPELLQKILEA 119
Cdd:COG0666 164 GNLEIVKLLLEAgadvnaRDNDGETplhlAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
13-96 |
6.50e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.97 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 13 LHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENRQGWTVLHEAVSTGDPEMV 90
Cdd:pfam12796 1 LHLAAKNGNLELV-KLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
|
....*.
gi 530401512 91 YTVLQH 96
Cdd:pfam12796 78 KLLLEK 83
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
31-122 |
4.19e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 31 GQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA----- 105
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpd 184
|
90 100
....*....|....*....|.
gi 530401512 106 -LEGVPELLQK---ILEAPDF 122
Cdd:PTZ00322 185 sFTGKPPSLEDspiSSHHPDF 205
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
40-69 |
7.62e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 7.62e-04
10 20 30
....*....|....*....|....*....|
gi 530401512 40 RGRTLLHLAVSLGHLESARVLLRHKADVTK 69
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GPCR_chapero_1 |
pfam11904 |
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ... |
156-470 |
4.99e-129 |
|
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.
Pssm-ID: 463391 Cd Length: 298 Bit Score: 380.06 E-value: 4.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 156 RVDITLLGFENMSWIRGRRSFIFKGED-NWAELMEVNHDDKVVTTERfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 234
Cdd:pfam11904 1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904 73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 308 EHQFGAQGQDLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEEFPLSLvEQVIPIIDLMA 387
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 388 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSashiTNFEVDQSVFEIP 467
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294
|
...
gi 530401512 468 ESY 470
Cdd:pfam11904 295 SGY 297
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-119 |
5.31e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 81.92 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530401512 85 GDPEMVYTVLQH------RDYHNTS----MALEGVPELLQKILEA 119
Cdd:COG0666 164 GNLEIVKLLLEAgadvnaRDNDGETplhlAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
4-90 |
3.70e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 79.23 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 4 ACDAGDHYPLHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIV-KLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
....*....
gi 530401512 82 VSTGDPEMV 90
Cdd:COG0666 194 AENGHLEIV 202
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
4-97 |
7.75e-15 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 75.38 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 4 ACDAGDHYPLHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:COG0666 148 AQDNDGNTPLHLAAANGNLEIV-KLLleAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
|
90
....*....|....*.
gi 530401512 82 VSTGDPEMVYTVLQHR 97
Cdd:COG0666 227 AENGNLEIVKLLLEAG 242
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
13-96 |
6.50e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.97 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 13 LHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENRQGWTVLHEAVSTGDPEMV 90
Cdd:pfam12796 1 LHLAAKNGNLELV-KLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
|
....*.
gi 530401512 91 YTVLQH 96
Cdd:pfam12796 78 KLLLEK 83
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
41-90 |
1.08e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 1.08e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530401512 41 GRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMV 90
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-96 |
1.29e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 62.66 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666 51 DALGALLLLAAALAGDLLVALLLLaAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
|
90
....*....|..
gi 530401512 85 GDPEMVYTVLQH 96
Cdd:COG0666 131 GNLEIVKLLLEA 142
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
45-118 |
1.31e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.43 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 45 LHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQH-----RDYHNTSM---ALEGVPELLQKI 116
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHadvnlKDNGRTALhyaARSGHLEIVKLL 80
|
..
gi 530401512 117 LE 118
Cdd:pfam12796 81 LE 82
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
31-122 |
4.19e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 31 GQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA----- 105
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpd 184
|
90 100
....*....|....*....|.
gi 530401512 106 -LEGVPELLQK---ILEAPDF 122
Cdd:PTZ00322 185 sFTGKPPSLEDspiSSHHPDF 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
4-90 |
5.86e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 48.41 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 4 ACDAGDHYPLHLLVWKNDYrQLEKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:COG0666 181 ARDNDGETPLHLAAENGHL-EIVKLLleAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
|
....*....
gi 530401512 82 VSTGDPEMV 90
Cdd:COG0666 260 AAAGAALIV 268
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
12-97 |
1.40e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.68 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 12 PLHLLVWKNDYRQLEkELQGQNVEAVD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPE 88
Cdd:PHA02875 71 ELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
|
....*....
gi 530401512 89 MVYTVLQHR 97
Cdd:PHA02875 150 GIELLIDHK 158
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
33-81 |
5.39e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 5.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530401512 33 NVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
38-96 |
5.92e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.01 E-value: 5.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 530401512 38 DPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEmVYTVLQH 96
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYH 612
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
40-72 |
1.34e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.19 E-value: 1.34e-04
10 20 30
....*....|....*....|....*....|....
gi 530401512 40 RGRTLLHLAV-SLGHLESARVLLRHKADVTKENR 72
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
29-71 |
1.97e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.48 E-value: 1.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530401512 29 LQGQNVEAVDpRGRTLLHLAVSLGHLESARVLLRHKADVTKEN 71
Cdd:pfam12796 50 LEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
40-67 |
3.03e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.39 E-value: 3.03e-04
10 20
....*....|....*....|....*...
gi 530401512 40 RGRTLLHLAVSLGHLESARVLLRHKADV 67
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
40-69 |
7.62e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 7.62e-04
10 20 30
....*....|....*....|....*....|
gi 530401512 40 RGRTLLHLAVSLGHLESARVLLRHKADVTK 69
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-119 |
1.66e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 40.71 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 6 DAGDHYPLHLLVWKNDYRQLEKELQGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTG 85
Cdd:COG0666 19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530401512 86 DPEMVYTVLQH------RDYHNTSM----ALEGVPELLQKILEA 119
Cdd:COG0666 99 DLEIVKLLLEAgadvnaRDKDGETPlhlaAYNGNLEIVKLLLEA 142
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
31-101 |
4.48e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 39.95 E-value: 4.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530401512 31 GQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHN 101
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
27-110 |
6.58e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 39.47 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 27 KEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENrqgwtvLHEAVStgdPEMVYTVLQHRDYHNTSM 104
Cdd:PLN03192 639 KELlkQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN------TDDDFS---PTELRELLQKRELGHSIT 709
|
....*.
gi 530401512 105 ALEGVP 110
Cdd:PLN03192 710 IVDSVP 715
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
6-96 |
8.54e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 39.09 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401512 6 DAGDHYPLHLLVWKNDYRQLEKELQ-GQNVEAVDPRGRTLLHLAVS-LGHLESARVLLRHKADVT-KENRQGWTVLHEAV 82
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLEnGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNaKSYILGLTALHSSI 277
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90
....*....|....
gi 530401512 83 StgDPEMVYTVLQH 96
Cdd:PHA02878 278 K--SERKLKLLLEY 289
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