|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
161-451 |
4.64e-176 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 496.06 E-value: 4.64e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 161 PLPPTMGLPLQKKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAIS 240
Cdd:PTZ00338 1 TGGSKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 241 NG-FMNLAVRHGDALRSDLGVFDVCAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVS 319
Cdd:PTZ00338 81 SPlASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 320 LFCTVQRVCKVDAKHFTPPPKVDSVVVKVVPRPNLIDVDFKEWDGLMRICFGRKNRTLHALFRRASILSMLEANYKTWCT 399
Cdd:PTZ00338 161 LLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 237835739 400 -LNKCAPTSQ-PFREFCLGVLSATGLGDRRSVTIDIDTYFSLLLAFNKKGIHFV 451
Cdd:PTZ00338 241 mINKKVPVSLePFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHFV 294
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
163-392 |
2.18e-63 |
|
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439801 [Multi-domain] Cd Length: 270 Bit Score: 206.90 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 163 PPTMGLPLQKKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNG 242
Cdd:COG0030 4 SRRYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 243 fmNLAVRHGDALRSDL-----GVFDVCAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAAN 317
Cdd:COG0030 84 --NLTVIEGDALKVDLpalaaGEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 318 VSLFCTVQRVCKVDAKHFTPPPKvdsvv--vkvvPRPNLIDVDFKEWDGLMRICFGRKNRTLH----ALFRRASILSMLE 391
Cdd:COG0030 162 VQYYADVEILFTVPPEAFYPPPKvdsavvrltprPEPLVPVADEKLFFRVVKAAFSQRRKTLRnslkSLFSKERLEEALE 241
|
.
gi 237835739 392 A 392
Cdd:COG0030 242 A 242
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
172-383 |
3.61e-60 |
|
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273252 [Multi-domain] Cd Length: 254 Bit Score: 198.22 E-value: 3.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 172 KKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAIsnGFMNLAVRHG 251
Cdd:TIGR00755 5 KSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLS--LYNNLEIIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 252 DALRSDLGVFDV----CAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVSLFCTVQRV 327
Cdd:TIGR00755 83 DALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 237835739 328 CKVDAKHFTPPPKVDSVVVKVVPRPNLI-DVDFKEWDGLMRICFGRKNRTLHALFRR 383
Cdd:TIGR00755 163 FKVPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKN 219
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
184-340 |
3.47e-55 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 181.94 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 184 VLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfmNLAVRHGDALRSDLG--VF 261
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAAD--NLTVIHGDALKFDLPklQP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237835739 262 DVCAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVSLFCTVQRVCKVDAKHFTPPPK 340
Cdd:smart00650 79 YKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
167-413 |
2.65e-51 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 175.25 E-value: 2.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 167 GLPLQKKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfmNL 246
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDE--NL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 247 AVRHGDALRSDLGVF-------DVCAANLPYQISSHFLLRLL-AHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANV 318
Cdd:pfam00398 79 TVIHQDFLKFEFPSLvthihqeFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 319 SLFCTVQRVCKVDAKHFTPPPKVDSVVVKVVPRPNLI--DVDFKEWDGLMRICFGRKNRTLHALFRRASILSMLEANYKT 396
Cdd:pfam00398 159 QAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPhpVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSSH 238
|
250 260
....*....|....*....|
gi 237835739 397 WCTLN---KCAPTSQPFREF 413
Cdd:pfam00398 239 GINDNalvKKLSPEQTLDIF 258
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
199-295 |
3.02e-09 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 54.36 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 199 TVLEIGPGTGNLTMRLL-PVAREVVALDVDARMVNEVKKRAISNGFMNLAVRHGDALRSDLGV---FDVCAANLPYQISS 274
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEAdesFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|...
gi 237835739 275 HFLLRLL--AHRPPFRCAVLMFQ 295
Cdd:cd02440 81 EDLARFLeeARRLLKPGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
161-451 |
4.64e-176 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 496.06 E-value: 4.64e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 161 PLPPTMGLPLQKKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAIS 240
Cdd:PTZ00338 1 TGGSKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 241 NG-FMNLAVRHGDALRSDLGVFDVCAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVS 319
Cdd:PTZ00338 81 SPlASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 320 LFCTVQRVCKVDAKHFTPPPKVDSVVVKVVPRPNLIDVDFKEWDGLMRICFGRKNRTLHALFRRASILSMLEANYKTWCT 399
Cdd:PTZ00338 161 LLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 237835739 400 -LNKCAPTSQ-PFREFCLGVLSATGLGDRRSVTIDIDTYFSLLLAFNKKGIHFV 451
Cdd:PTZ00338 241 mINKKVPVSLePFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHFV 294
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
163-392 |
2.18e-63 |
|
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439801 [Multi-domain] Cd Length: 270 Bit Score: 206.90 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 163 PPTMGLPLQKKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNG 242
Cdd:COG0030 4 SRRYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 243 fmNLAVRHGDALRSDL-----GVFDVCAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAAN 317
Cdd:COG0030 84 --NLTVIEGDALKVDLpalaaGEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 318 VSLFCTVQRVCKVDAKHFTPPPKvdsvv--vkvvPRPNLIDVDFKEWDGLMRICFGRKNRTLH----ALFRRASILSMLE 391
Cdd:COG0030 162 VQYYADVEILFTVPPEAFYPPPKvdsavvrltprPEPLVPVADEKLFFRVVKAAFSQRRKTLRnslkSLFSKERLEEALE 241
|
.
gi 237835739 392 A 392
Cdd:COG0030 242 A 242
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
172-383 |
3.61e-60 |
|
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273252 [Multi-domain] Cd Length: 254 Bit Score: 198.22 E-value: 3.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 172 KKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAIsnGFMNLAVRHG 251
Cdd:TIGR00755 5 KSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLS--LYNNLEIIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 252 DALRSDLGVFDV----CAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVSLFCTVQRV 327
Cdd:TIGR00755 83 DALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 237835739 328 CKVDAKHFTPPPKVDSVVVKVVPRPNLI-DVDFKEWDGLMRICFGRKNRTLHALFRR 383
Cdd:TIGR00755 163 FKVPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKN 219
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
172-394 |
1.65e-58 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 193.96 E-value: 1.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 172 KKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfmNLAVRHG 251
Cdd:PRK14896 5 KKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAG--NVEIIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 252 DALRSDLGVFDVCAANLPYQISSHFLLRLLAHRppFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVSLFCTVQRVCKVD 331
Cdd:PRK14896 83 DALKVDLPEFNKVVSNLPYQISSPITFKLLKHG--FEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEIVEKVP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237835739 332 AKHFTPPPKVDSVVVKVVPRPNLIDVDFKE-WDGLMRICFGRKNRTLhalfRRASILSMLEANY 394
Cdd:PRK14896 161 PGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTL----RNALKNSAHISGK 220
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
184-340 |
3.47e-55 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 181.94 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 184 VLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfmNLAVRHGDALRSDLG--VF 261
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAAD--NLTVIHGDALKFDLPklQP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237835739 262 DVCAANLPYQISSHFLLRLLAHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANVSLFCTVQRVCKVDAKHFTPPPK 340
Cdd:smart00650 79 YKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
167-413 |
2.65e-51 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 175.25 E-value: 2.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 167 GLPLQKKFGQHLLKNQAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfmNL 246
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDE--NL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 247 AVRHGDALRSDLGVF-------DVCAANLPYQISSHFLLRLL-AHRPPFRCAVLMFQKEFGERLMAQPGDKNYCRLAANV 318
Cdd:pfam00398 79 TVIHQDFLKFEFPSLvthihqeFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 319 SLFCTVQRVCKVDAKHFTPPPKVDSVVVKVVPRPNLI--DVDFKEWDGLMRICFGRKNRTLHALFRRASILSMLEANYKT 396
Cdd:pfam00398 159 QAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPhpVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSSH 238
|
250 260
....*....|....*....|
gi 237835739 397 WCTLN---KCAPTSQPFREF 413
Cdd:pfam00398 239 GINDNalvKKLSPEQTLDIF 258
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
186-285 |
1.62e-11 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 61.93 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 186 DKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGFmNLAVRHGDALRSDL--GVFDV 263
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFpdGSFDL 90
|
90 100
....*....|....*....|..
gi 237835739 264 caanlpyqISSHFLLRLLAHRP 285
Cdd:COG2226 91 --------VISSFVLHHLPDPE 104
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
199-295 |
3.02e-09 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 54.36 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 199 TVLEIGPGTGNLTMRLL-PVAREVVALDVDARMVNEVKKRAISNGFMNLAVRHGDALRSDLGV---FDVCAANLPYQISS 274
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEAdesFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|...
gi 237835739 275 HFLLRLL--AHRPPFRCAVLMFQ 295
Cdd:cd02440 81 EDLARFLeeARRLLKPGGVLVLT 103
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
200-267 |
5.36e-09 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 53.34 E-value: 5.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237835739 200 VLEIGPGTGNLTMRLLP-VAREVVALDVDARMVNEVKKRAISNGFmNLAVRHGDA--LRSDLGVFDVCAAN 267
Cdd:pfam13649 1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAedLPFPDGSFDLVVSS 70
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
187-263 |
6.28e-09 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 55.86 E-value: 6.28e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237835739 187 KIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGFMNLAVRHGDALR--SDLGVFDV 263
Cdd:COG2518 57 RMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALgwPEHAPFDR 135
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
190-270 |
3.71e-08 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 53.36 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 190 QAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGFMNLAVrhgDALRSDL------GVFDV 263
Cdd:PRK14968 17 ENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGV---EVIRSDLfepfrgDKFDV 93
|
....*..
gi 237835739 264 CAANLPY 270
Cdd:PRK14968 94 ILFNPPY 100
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
182-270 |
6.31e-08 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 52.69 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 182 QAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGFMnlavrHGD--ALRSDLG 259
Cdd:COG4976 32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLL-----VADlaDLAEPDG 106
|
90
....*....|...
gi 237835739 260 VFD--VCAANLPY 270
Cdd:COG4976 107 RFDliVAADVLTY 119
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
182-264 |
1.44e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 52.25 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 182 QAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLlpvAREV------VALDVDARMVNEVKKRAISNGfMNLAVRHGDALR 255
Cdd:PRK08317 5 RRYRARTFELLAVQPGDRVLDVGCGPGNDAREL---ARRVgpegrvVGIDRSEAMLALAKERAAGLG-PNVEFVRGDADG 80
|
90
....*....|.
gi 237835739 256 SDL--GVFDVC 264
Cdd:PRK08317 81 LPFpdGSFDAV 91
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
191-270 |
7.06e-07 |
|
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 129628 [Multi-domain] Cd Length: 179 Bit Score: 49.47 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 191 AADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfMNLAVRHGDALRSDLGVFDVCAANLPY 270
Cdd:TIGR00537 14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNN-VGLDVVMTDLFKGVRGKFDVILFNPPY 92
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
185-263 |
2.49e-06 |
|
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: 46.55 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 185 LDKIVQAAdIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISngfMNLAVRHGDALRSDL--GVFD 262
Cdd:COG2227 14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDLPLedGSFD 89
|
.
gi 237835739 263 V 263
Cdd:COG2227 90 L 90
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
201-268 |
2.72e-06 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 45.73 E-value: 2.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 201 LEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGfmnLAVRHGDALRSDL--GVFDVCAANL 268
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG---LTFVVGDAEDLPFpdNSFDLVLSSE 67
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
201-263 |
6.26e-06 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 44.67 E-value: 6.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237835739 201 LEIGPGTGNLTMRLLPVAR--EVVALDVDARMVNEVKKRAISNG---FMNLAVRHGDALRSDLGVFDV 263
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALEAARERLAALGllnAVRVELFQLDLGELDPGSFDV 68
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
188-275 |
9.28e-06 |
|
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 46.10 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 188 IVQAADIRSSDTVLEigP--GTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGFMNLAVRHGDALRSDL--GVFDV 263
Cdd:COG1041 18 LVNLAGAKEGDTVLD--PfcGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLadESVDA 95
|
90
....*....|..
gi 237835739 264 CAANLPYQISSH 275
Cdd:COG1041 96 IVTDPPYGRSSK 107
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
199-267 |
1.43e-05 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 43.66 E-value: 1.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237835739 199 TVLEIGPGTGNLTMRLL---PVAReVVALDVDARMVNEVKKRAIsngfmNLAVRHGDALRSDL-GVFDVCAAN 267
Cdd:COG4106 4 RVLDLGCGTGRLTALLAerfPGAR-VTGVDLSPEMLARARARLP-----NVRFVVADLRDLDPpEPFDLVVSN 70
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
194-254 |
1.84e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 44.72 E-value: 1.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237835739 194 IRSSDTVLEIGPGTGNLTMRLLPVAR---EVVALDVDARMVNEVKKRAISNGFMNLAVRHGDAL 254
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIE 64
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
183-283 |
3.13e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 44.91 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 183 AVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLL-PVAREVVALDVDARMVNEVKKRAISNGFMNLAVRHGDALRSD---L 258
Cdd:COG0500 13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDplpA 92
|
90 100
....*....|....*....|....*.
gi 237835739 259 GVFD-VCAANLPYQISSHFLLRLLAH 283
Cdd:COG0500 93 ESFDlVVAFGVLHHLPPEEREALLRE 118
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
182-263 |
7.35e-05 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 42.99 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 182 QAVLDKIVQAADIRSSDTVLEIGPGTGNLTMRLlpvARE----VVALDVDARMVNEVKKRAISNGFMNLA-VRHGDALRS 256
Cdd:COG2230 37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYL---ARRygvrVTGVTLSPEQLEYARERAAEAGLADRVeVRLADYRDL 113
|
....*...
gi 237835739 257 DL-GVFDV 263
Cdd:COG2230 114 PAdGQFDA 121
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
186-255 |
2.41e-04 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 42.12 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237835739 186 DKIVQAADIRSSDTVLEIGPGTGNLTM----RLLPVAReVVALDVDARMVNEVKKRaisngFMNLAVRHGDALR 255
Cdd:COG3963 35 RAMASEVDWSGAGPVVELGPGTGVFTRailaRGVPDAR-LLAVEINPEFAEHLRRR-----FPRVTVVNGDAED 102
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
188-215 |
4.47e-04 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 42.07 E-value: 4.47e-04
10 20
....*....|....*....|....*...
gi 237835739 188 IVQAADIRSSDTVLEIGPGTGNLTMRLL 215
Cdd:COG2519 83 IIARLDIFPGARVLEAGTGSGALTLALA 110
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
194-258 |
6.02e-04 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 41.56 E-value: 6.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237835739 194 IRSSDTVLEIGPGTGNLTMRLLP-VAREVVALDVDARMVNEVKKRAISNGFM-NLAVRHGDALRSDL 258
Cdd:COG4076 33 VKPGDVVLDIGTGSGLLSMLAARaGAKKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDLDL 99
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
199-264 |
8.22e-04 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 40.98 E-value: 8.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237835739 199 TVLEIGPGTGNLTmrlLPVAR---EVVALDVDARMVNEVKKRA---ISNGFMNLAVrhGDaLRSDLGVFD--VC 264
Cdd:PRK07580 66 RILDAGCGVGSLS---IPLARrgaKVVASDISPQMVEEARERApeaGLAGNITFEV--GD-LESLLGRFDtvVC 133
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
174-255 |
1.57e-03 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 40.14 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 174 FGQHLLKNQAVldkiVQAADIRSSDTVLEIGPGTGNLTMRLLPVAR---EVVALDVDARMVNEVKKRAISNGFM-NLAVR 249
Cdd:PRK00216 33 FGLHRVWRRKT----IKWLGVRPGDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREKLRDLGLSgNVEFV 108
|
....*.
gi 237835739 250 HGDALR 255
Cdd:PRK00216 109 QGDAEA 114
|
|
| pcm |
PRK00312 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; |
187-252 |
3.52e-03 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
Pssm-ID: 178974 [Multi-domain] Cd Length: 212 Bit Score: 39.03 E-value: 3.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237835739 187 KIVQAADIRSSDTVLEIGPGTGNLTMRLLPVAREVVALDVDARMVNEVKKRAISNGFMNLAVRHGD 252
Cdd:PRK00312 69 RMTELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGD 134
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
191-270 |
3.74e-03 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 38.97 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 191 AADIRSSDTVLEIGPGTGNLTMRL---LPVAReVVALDVDARMVNEVKKRAISNGFMN-LAVRHGD--ALRSDLGV--FD 262
Cdd:COG4123 32 FAPVKKGGRVLDLGTGTGVIALMLaqrSPGAR-ITGVEIQPEAAELARRNVALNGLEDrITVIHGDlkEFAAELPPgsFD 110
|
....*...
gi 237835739 263 VCAANLPY 270
Cdd:COG4123 111 LVVSNPPY 118
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
188-269 |
3.84e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 38.73 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237835739 188 IVQAADIRSS---DTVLEIGPGTGNLTMRLLPV-AREVVALDVDARMVnEVKKRAISNGFMNLAVRHGDALR-SDLGVFD 262
Cdd:COG2263 34 LLHLAYLRGDiegKTVLDLGCGTGMLAIGAALLgAKKVVGVDIDPEAL-EIARENAERLGVRVDFIRADVTRiPLGGSVD 112
|
....*..
gi 237835739 263 VCAANLP 269
Cdd:COG2263 113 TVVMNPP 119
|
|
| |
