|
Name |
Accession |
Description |
Interval |
E-value |
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
17-283 |
1.72e-113 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 328.09 E-value: 1.72e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 17 AAEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDgPRGAVEWATLLDRLTVQETRFFRHPPS 96
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTS-HRGEEELAELLDLMTTNETRFFRESKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 97 FELLERYLGERLRRE-GMPRPWALWSVGCSSGEEPYSLAMCAAQVLRGqEREDFFGVTGTDISLHALQRARQANYPARKL 175
Cdd:smart00138 80 FEALEEKVLPLLIASrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPK-GREPDVKILATDIDLKALEKARAGIYPEREL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 176 EQLEAGLVERYCERQaDGSFSVKTILTERVCCARLNVLDLaKAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERLAPGG 255
Cdd:smart00138 159 EDLPKALLARYFKEV-EDKYRVKPELKERVRFAKHNLLAE-SPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGG 236
|
250 260
....*....|....*....|....*...
gi 15595609 256 LLVIGVGEVVDWSHPELEPVADERVLAF 283
Cdd:smart00138 237 YLFLGHSESLPGLTDKFEPIEGTVYFYS 264
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
13-287 |
1.01e-89 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 267.80 E-value: 1.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 13 ADMSAAEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDGPRgavEWATLLDRLTVQETRFFR 92
Cdd:COG1352 2 AELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPE---ELQALIDALTINVTEFFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 93 HPPSFELLERY-LGERLRREGMPRPWALWSVGCSSGEEPYSLAMCAAQVLRGQEREDFfGVTGTDISLHALQRARQANYP 171
Cdd:COG1352 79 DPEHFEALREEvLPELLARRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRV-EILATDISEEALEKARAGIYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 172 ARKLEQLEAGLVERYCERQaDGSFSVKTILTERVCCARLNVLDLAkAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERL 251
Cdd:COG1352 158 ERSLRGLPPEYLSRYFTKE-GGRYRIKPELREMVTFAQHNLLDDP-PPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 15595609 252 APGGLLVIGVGEVVDWSHPELEPVADERVLAFTRKG 287
Cdd:COG1352 236 APGGYLFLGHSESLGGLSDLFEPVDKKGRFIYRKRA 271
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
86-277 |
2.06e-80 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 241.03 E-value: 2.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 86 QETRFFRHPPSFELLERYLGERLRREGMPRPWALWSVGCSSGEEPYSLAMCAAQVLRGQEREDfFGVTGTDISLHALQRA 165
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWD-FKILATDIDLSVLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 166 RQANYPARKLEQLEAGLVERYCERQADGSFSVKTILTERVCCARLNVLDLaKAPWSGMDVIFCQNLLIYFRRWRRREILN 245
Cdd:pfam01739 80 RAGVYPERELEGLPEELLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDE-YPPLGDFDVIFCRNVLIYFDEETQRKILN 158
|
170 180 190
....*....|....*....|....*....|..
gi 15595609 246 RLAERLAPGGLLVIGVGEVVDWsHPELEPVAD 277
Cdd:pfam01739 159 RFAEKLKPGGYLFLGHSEALPG-NPDKFKKVG 189
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
15-263 |
3.04e-35 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 128.31 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 15 MSAAEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDGPRGAvEWATLLDRLTVQETRFFRHP 94
Cdd:PRK10611 22 LSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNSA-EWQAFINALTTNLTAFFREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 95 PSFELLERYLGerlRREGMPRpwaLWSVGCSSGEEPYSLAMCAAQVLrgQEREDFFGVTGTDISLHALQRARQANYPARK 174
Cdd:PRK10611 101 HHFPILAEHAR---RRSGEYR---VWSAAASTGEEPYSIAMTLADTL--GTAPGRWKVFASDIDTEVLEKARSGIYRQEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 175 LEQLEAGLVERYCERQA---DGSFSVKTILTERVCCARLNVLDLAKAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERL 251
Cdd:PRK10611 173 LKTLSPQQLQRYFMRGTgphEGLVRVRQELANYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLL 252
|
250
....*....|..
gi 15595609 252 APGGLLVIGVGE 263
Cdd:PRK10611 253 KPDGLLFAGHSE 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
17-283 |
1.72e-113 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 328.09 E-value: 1.72e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 17 AAEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDgPRGAVEWATLLDRLTVQETRFFRHPPS 96
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTS-HRGEEELAELLDLMTTNETRFFRESKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 97 FELLERYLGERLRRE-GMPRPWALWSVGCSSGEEPYSLAMCAAQVLRGqEREDFFGVTGTDISLHALQRARQANYPARKL 175
Cdd:smart00138 80 FEALEEKVLPLLIASrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPK-GREPDVKILATDIDLKALEKARAGIYPEREL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 176 EQLEAGLVERYCERQaDGSFSVKTILTERVCCARLNVLDLaKAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERLAPGG 255
Cdd:smart00138 159 EDLPKALLARYFKEV-EDKYRVKPELKERVRFAKHNLLAE-SPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGG 236
|
250 260
....*....|....*....|....*...
gi 15595609 256 LLVIGVGEVVDWSHPELEPVADERVLAF 283
Cdd:smart00138 237 YLFLGHSESLPGLTDKFEPIEGTVYFYS 264
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
13-287 |
1.01e-89 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 267.80 E-value: 1.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 13 ADMSAAEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDGPRgavEWATLLDRLTVQETRFFR 92
Cdd:COG1352 2 AELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPE---ELQALIDALTINVTEFFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 93 HPPSFELLERY-LGERLRREGMPRPWALWSVGCSSGEEPYSLAMCAAQVLRGQEREDFfGVTGTDISLHALQRARQANYP 171
Cdd:COG1352 79 DPEHFEALREEvLPELLARRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRV-EILATDISEEALEKARAGIYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 172 ARKLEQLEAGLVERYCERQaDGSFSVKTILTERVCCARLNVLDLAkAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERL 251
Cdd:COG1352 158 ERSLRGLPPEYLSRYFTKE-GGRYRIKPELREMVTFAQHNLLDDP-PPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 15595609 252 APGGLLVIGVGEVVDWSHPELEPVADERVLAFTRKG 287
Cdd:COG1352 236 APGGYLFLGHSESLGGLSDLFEPVDKKGRFIYRKRA 271
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
86-277 |
2.06e-80 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 241.03 E-value: 2.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 86 QETRFFRHPPSFELLERYLGERLRREGMPRPWALWSVGCSSGEEPYSLAMCAAQVLRGQEREDfFGVTGTDISLHALQRA 165
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWD-FKILATDIDLSVLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 166 RQANYPARKLEQLEAGLVERYCERQADGSFSVKTILTERVCCARLNVLDLaKAPWSGMDVIFCQNLLIYFRRWRRREILN 245
Cdd:pfam01739 80 RAGVYPERELEGLPEELLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDE-YPPLGDFDVIFCRNVLIYFDEETQRKILN 158
|
170 180 190
....*....|....*....|....*....|..
gi 15595609 246 RLAERLAPGGLLVIGVGEVVDWsHPELEPVAD 277
Cdd:pfam01739 159 RFAEKLKPGGYLFLGHSEALPG-NPDKFKKVG 189
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
15-263 |
3.04e-35 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 128.31 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 15 MSAAEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDGPRGAvEWATLLDRLTVQETRFFRHP 94
Cdd:PRK10611 22 LSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNSA-EWQAFINALTTNLTAFFREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 95 PSFELLERYLGerlRREGMPRpwaLWSVGCSSGEEPYSLAMCAAQVLrgQEREDFFGVTGTDISLHALQRARQANYPARK 174
Cdd:PRK10611 101 HHFPILAEHAR---RRSGEYR---VWSAAASTGEEPYSIAMTLADTL--GTAPGRWKVFASDIDTEVLEKARSGIYRQEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 175 LEQLEAGLVERYCERQA---DGSFSVKTILTERVCCARLNVLDLAKAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERL 251
Cdd:PRK10611 173 LKTLSPQQLQRYFMRGTgphEGLVRVRQELANYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLL 252
|
250
....*....|..
gi 15595609 252 APGGLLVIGVGE 263
Cdd:PRK10611 253 KPDGLLFAGHSE 264
|
|
| CheR_N |
pfam03705 |
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
18-70 |
9.76e-09 |
|
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase.
Pssm-ID: 461017 [Multi-domain] Cd Length: 53 Bit Score: 50.51 E-value: 9.76e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15595609 18 AEFRDWQVLLENRTGVVLNEQRRTFLQASLTARMRELGIGDYHSYYRQVTDGP 70
Cdd:pfam03705 1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
122-257 |
1.29e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 43.13 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 122 VGCSSGEEpysLAMCAAQVLRGQeredffgVTGTDISLHALQRARQanyparKLEQLEAGLVERYcerqadgsfsvktil 201
Cdd:pfam08242 3 IGCGTGTL---LRALLEALPGLE-------YTGLDISPAALEAARE------RLAALGLLNAVRV--------------- 51
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595609 202 tervccaRLNVLDLAKAPWSGMDVIFCQNLLIYFRRWRrrEILNRLAERLAPGGLL 257
Cdd:pfam08242 52 -------ELFQLDLGELDPGSFDVVVASNVLHHLADPR--AVLRNIRRLLKPGGVL 98
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
122-259 |
2.65e-05 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 43.38 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 122 VGCSSGeepySLAMCAAQVLRGQeredffgVTGTDISLHALQRARQANyparkleqLEAGLVERycerqadgsfsvktil 201
Cdd:COG2230 58 IGCGWG----GLALYLARRYGVR-------VTGVTLSPEQLEYARERA--------AEAGLADR---------------- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15595609 202 tervccARLNVLDLAKAPWSGM-DVIFCQNLLIYFRRWRRREILNRLAERLAPGGLLVI 259
Cdd:COG2230 103 ------VEVRLADYRDLPADGQfDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
122-261 |
2.89e-05 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 42.70 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 122 VGCSSGEepysLAMCAAQvlRGQEredffgVTGTDISLHALQRARQanyparKLEQLeaglverycerqadgsfsvktil 201
Cdd:COG2227 31 VGCGTGR----LALALAR--RGAD------VTGVDISPEALEIARE------RAAEL----------------------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 202 teRVCCARLNVLDLAKAPwSGMDVIFCQNLLIYFRRWRrrEILNRLAERLAPGGLLVIGV 261
Cdd:COG2227 70 --NVDFVQGDLEDLPLED-GSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLLST 124
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
95-259 |
3.03e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 44.14 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 95 PSFELLERYLGERLRREGMPRPWALWSVGCSSGeepYSLAMCAAQvLRGQeredffgVTGTDISLHALQRARqANYPARK 174
Cdd:COG0500 6 YSDELLPGLAALLALLERLPKGGRVLDLGCGTG---RNLLALAAR-FGGR-------VIGIDLSPEAIALAR-ARAAKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 175 LEQLEagLVERycerqadgsfsvktiltervccarlNVLDLAKAPWSGMDVIFCQNLLIYFRRWRRREILNRLAERLAPG 254
Cdd:COG0500 74 LGNVE--FLVA-------------------------DLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPG 126
|
....*
gi 15595609 255 GLLVI 259
Cdd:COG0500 127 GVLLL 131
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
122-261 |
2.09e-03 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 36.73 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 122 VGCSSGEEPYSLAmcaaqvlrgqEREDFFGVTGTDISLHALQRARQanyparKLEQLEAglveryceRQADgsfsvktil 201
Cdd:COG4106 8 LGCGTGRLTALLA----------ERFPGARVTGVDLSPEMLARARA------RLPNVRF--------VVAD--------- 54
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595609 202 tervccarLNVLDLAKAPwsgmDVIFCQNLLIYFRRwrRREILNRLAERLAPGGLLVIGV 261
Cdd:COG4106 55 --------LRDLDPPEPF----DLVVSNAALHWLPD--HAALLARLAAALAPGGVLAVQV 100
|
|
| |
