|
Name |
Accession |
Description |
Interval |
E-value |
| GPCR_chapero_1 |
pfam11904 |
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ... |
267-581 |
3.70e-128 |
|
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: 381.60 E-value: 3.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 267 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 345
Cdd:pfam11904 1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 346 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 418
Cdd:pfam11904 73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 419 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 498
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 499 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 578
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295
|
...
gi 1958669178 579 SYH 581
Cdd:pfam11904 296 GYT 298
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
115-201 |
1.70e-15 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 77.69 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIV-KLLLEAGAdvNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
....*....
gi 1958669178 193 VSTGDPEMV 201
Cdd:COG0666 194 AENGHLEIV 202
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
124-207 |
1.88e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.51 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 124 LHLLVWNNDYRQLeKELRDQNAEA--LDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENGQGWTVLHEAVSTGDPEMV 201
Cdd:pfam12796 1 LHLAAKNGNLELV-KLLLENGADAnlQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
|
....*.
gi 1958669178 202 YTVLQH 207
Cdd:pfam12796 78 KLLLEK 83
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
121-208 |
2.83e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.37 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 121 RFPLHLLVWNNDYRQLEkELRDQNAEALD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGD 197
Cdd:PHA02875 69 ESELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
|
90
....*....|.
gi 1958669178 198 PEMVYTVLQHR 208
Cdd:PHA02875 148 IKGIELLIDHK 158
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-180 |
9.02e-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: 9.02e-04
10 20 30
....*....|....*....|....*....|
gi 1958669178 151 RGRTLLHLAVSLGHLESARVLLRHKADVTK 180
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 ... |
267-581 |
3.70e-128 |
|
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: 381.60 E-value: 3.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 267 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 345
Cdd:pfam11904 1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 346 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 418
Cdd:pfam11904 73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 419 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 498
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 499 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 578
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295
|
...
gi 1958669178 579 SYH 581
Cdd:pfam11904 296 GYT 298
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
115-201 |
1.70e-15 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 77.69 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIV-KLLLEAGAdvNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
....*....
gi 1958669178 193 VSTGDPEMV 201
Cdd:COG0666 194 AENGHLEIV 202
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
115-207 |
1.28e-14 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 74.99 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYrQLEKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDL-EIVKLLLEAGAdvNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
90
....*....|....*
gi 1958669178 193 VSTGDPEMVYTVLQH 207
Cdd:COG0666 161 AANGNLEIVKLLLEA 175
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
115-238 |
2.01e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.52 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666 148 AQDNDGNTPLHLAAANGNLEIV-KLLLEAGAdvNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958669178 193 VSTGDPEMVYTVLQHRDYHNTSMALEGVPELLHKILEAPDFYVQMK 238
Cdd:COG0666 227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
124-207 |
1.88e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.51 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 124 LHLLVWNNDYRQLeKELRDQNAEA--LDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENGQGWTVLHEAVSTGDPEMV 201
Cdd:pfam12796 1 LHLAAKNGNLELV-KLLLENGADAnlQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
|
....*.
gi 1958669178 202 YTVLQH 207
Cdd:pfam12796 78 KLLLEK 83
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
152-201 |
1.30e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.90 E-value: 1.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958669178 152 GRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 201
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
109-207 |
4.76e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.12 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 109 LLAMSSARDTSSRFPLHLLVWNNDYRQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTV 188
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
|
90
....*....|....*....
gi 1958669178 189 LHEAVSTGDPEMVYTVLQH 207
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEA 142
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-226 |
2.04e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 156 LHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQH-----RDYHNTSM-------ALEGVPEL 223
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHadvnlKDNGRTALhyaarsgHLEIVKLL 80
|
...
gi 1958669178 224 LHK 226
Cdd:pfam12796 81 LEK 83
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
121-208 |
2.83e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.37 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 121 RFPLHLLVWNNDYRQLEkELRDQNAEALD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGD 197
Cdd:PHA02875 69 ESELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
|
90
....*....|.
gi 1958669178 198 PEMVYTVLQHR 208
Cdd:PHA02875 148 IKGIELLIDHK 158
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
149-233 |
4.85e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 149 DPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA------LEGVPE 222
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpdsFTGKPP 191
|
90
....*....|....
gi 1958669178 223 LLHK---ILEAPDF 233
Cdd:PTZ00322 192 SLEDspiSSHHPDF 205
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
107-207 |
1.59e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.33 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 107 GDLLAMSSARDTSSRFPLHLL--VWNNDYRQLEKELR-DQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENG 183
Cdd:PLN03192 510 GDLLGDNGGEHDDPNMASNLLtvASTGNAALLEELLKaKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDA 589
|
90 100
....*....|....*....|....
gi 1958669178 184 QGWTVLHEAVSTGDPEmVYTVLQH 207
Cdd:PLN03192 590 NGNTALWNAISAKHHK-IFRILYH 612
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
139-192 |
2.09e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 2.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958669178 139 ELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
116-182 |
8.46e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.64 E-value: 8.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958669178 116 RDTSSRFPLHLLVwNNDYRQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKEN 182
Cdd:pfam12796 26 QDKNGRTALHLAA-KNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-182 |
2.24e-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: 38.81 E-value: 2.24e-04
10 20 30
....*....|....*....|....*....|...
gi 1958669178 151 RGRTLLHLAV-SLGHLESARVLLRHKADVTKEN 182
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-178 |
3.59e-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: 3.59e-04
10 20
....*....|....*....|....*...
gi 1958669178 151 RGRTLLHLAVSLGHLESARVLLRHKADV 178
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-180 |
9.02e-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: 9.02e-04
10 20 30
....*....|....*....|....*....|
gi 1958669178 151 RGRTLLHLAVSLGHLESARVLLRHKADVTK 180
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
108-207 |
2.46e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 40.71 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 108 DLLAMSSARDTSSRFPLHLLVWNNDYRQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWT 187
Cdd:COG0666 10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89
|
90 100
....*....|....*....|
gi 1958669178 188 VLHEAVSTGDPEMVYTVLQH 207
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEA 109
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
154-205 |
5.37e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 39.97 E-value: 5.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958669178 154 TLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVL 205
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
|
|
|