|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
3-198 |
1.49e-148 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 410.28 E-value: 1.49e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 3 MVIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 82
Cdd:PRK11207 1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 83 HTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 162
Cdd:PRK11207 81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
|
170 180 190
....*....|....*....|....*....|....*.
2XVA_D 163 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 198
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
|
|
| tehB |
TIGR00477 |
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular ... |
3-198 |
1.15e-131 |
|
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular processes, Toxin production and resistance]
Pssm-ID: 188054 Cd Length: 195 Bit Score: 367.28 E-value: 1.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 3 MVIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLdNL 82
Cdd:TIGR00477 1 FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNETKEKENL-NL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 83 HTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 162
Cdd:TIGR00477 80 STALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADYPCPLPFSFTFKENELREYY 159
|
170 180 190
....*....|....*....|....*....|....*.
2XVA_D 163 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 198
Cdd:TIGR00477 160 KDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK 195
|
|
| TehB |
pfam03848 |
Tellurite resistance protein TehB; |
3-195 |
1.39e-126 |
|
Tellurite resistance protein TehB;
Pssm-ID: 397776 Cd Length: 193 Bit Score: 354.54 E-value: 1.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 3 MVIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 82
Cdd:pfam03848 1 FYCKKEDYFHKKYNLTPTHSEVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 83 HTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 162
Cdd:pfam03848 81 HTALYDINNATIDENYDFILSTVVLMFLEPERIPGIIANMQECTNPGGYNLIVAAMSTDDVPCTVPFSFTFKEGELKRYY 160
|
170 180 190
....*....|....*....|....*....|...
2XVA_D 163 EGWERVKYNEDVGELHRTDANGNRIKLRFATML 195
Cdd:pfam03848 161 QDWERVKYNEDVGELHKTDANGNRIKLRFATML 193
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
32-135 |
3.69e-18 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 75.63 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 32 KPGKTLDLGCGNGRNSLYLAAN--GYDVDAWDKNAMSIAnveriKSIENLDNLHTRVVDLNNLTFDRQYDFILSTVVLMF 109
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLA-----RARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHW 75
|
90 100
....*....|....*....|....*.
2XVA_D 110 LEAktIPGLIANMQRCTKPGGYNLIV 135
Cdd:COG4106 76 LPD--HAALLARLAAALAPGGVLAVQ 99
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
37-131 |
5.13e-10 |
|
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: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLA-ANGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DRQYDFILSTVVLMFLEAk 113
Cdd:cd02440 3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE- 81
|
90
....*....|....*...
2XVA_D 114 TIPGLIANMQRCTKPGGY 131
Cdd:cd02440 82 DLARFLEEARRLLKPGGV 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
3-198 |
1.49e-148 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 410.28 E-value: 1.49e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 3 MVIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 82
Cdd:PRK11207 1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 83 HTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 162
Cdd:PRK11207 81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
|
170 180 190
....*....|....*....|....*....|....*.
2XVA_D 163 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 198
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
|
|
| tehB |
TIGR00477 |
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular ... |
3-198 |
1.15e-131 |
|
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular processes, Toxin production and resistance]
Pssm-ID: 188054 Cd Length: 195 Bit Score: 367.28 E-value: 1.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 3 MVIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLdNL 82
Cdd:TIGR00477 1 FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNETKEKENL-NL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 83 HTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 162
Cdd:TIGR00477 80 STALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADYPCPLPFSFTFKENELREYY 159
|
170 180 190
....*....|....*....|....*....|....*.
2XVA_D 163 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 198
Cdd:TIGR00477 160 KDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK 195
|
|
| TehB |
pfam03848 |
Tellurite resistance protein TehB; |
3-195 |
1.39e-126 |
|
Tellurite resistance protein TehB;
Pssm-ID: 397776 Cd Length: 193 Bit Score: 354.54 E-value: 1.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 3 MVIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 82
Cdd:pfam03848 1 FYCKKEDYFHKKYNLTPTHSEVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 83 HTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 162
Cdd:pfam03848 81 HTALYDINNATIDENYDFILSTVVLMFLEPERIPGIIANMQECTNPGGYNLIVAAMSTDDVPCTVPFSFTFKEGELKRYY 160
|
170 180 190
....*....|....*....|....*....|...
2XVA_D 163 EGWERVKYNEDVGELHRTDANGNRIKLRFATML 195
Cdd:pfam03848 161 QDWERVKYNEDVGELHKTDANGNRIKLRFATML 193
|
|
| PRK12335 |
PRK12335 |
tellurite resistance protein TehB; Provisional |
8-199 |
1.39e-117 |
|
tellurite resistance protein TehB; Provisional
Pssm-ID: 183450 [Multi-domain] Cd Length: 287 Bit Score: 335.37 E-value: 1.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 8 ENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLdNLHTRVV 87
Cdd:PRK12335 96 EDYFHKKYNLTATHSEVLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENL-NIRTGLY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 88 DLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYYEGWER 167
Cdd:PRK12335 175 DINSASIQEEYDFILSTVVLMFLNRERIPAIIKNMQEHTNPGGYNLIVCAMDTEDYPCPMPFSFTFKEGELKDYYQDWEI 254
|
170 180 190
....*....|....*....|....*....|..
2XVA_D 168 VKYNEDVGELHRTDANGNRIKLRFATMLARKK 199
Cdd:PRK12335 255 VKYNENVGHLHKTDENGNRIKLRFATLLAKKV 286
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
32-135 |
3.69e-18 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 75.63 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 32 KPGKTLDLGCGNGRNSLYLAAN--GYDVDAWDKNAMSIAnveriKSIENLDNLHTRVVDLNNLTFDRQYDFILSTVVLMF 109
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLA-----RARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHW 75
|
90 100
....*....|....*....|....*.
2XVA_D 110 LEAktIPGLIANMQRCTKPGGYNLIV 135
Cdd:COG4106 76 LPD--HAALLARLAAALAPGGVLAVQ 99
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
31-137 |
1.27e-17 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 76.12 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 31 VKPGKT-LDLGCGNGRNSLYLAAN-GYDVDAWDKNAMSIANVERIKSIENL-DNLHTRVVDLNNLTFDRQYDFILSTVVL 107
Cdd:COG2230 49 LKPGMRvLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVSIGMF 128
|
90 100 110
....*....|....*....|....*....|
2XVA_D 108 MFLEAKTIPGLIANMQRCTKPGGYNLIVAA 137
Cdd:COG2230 129 EHVGPENYPAYFAKVARLLKPGGRLLLHTP 158
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
37-130 |
4.18e-17 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 72.98 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLAAN-GYDVDAWDKNAMSIANVERIKSIENLdNLHTRVVDLNNLTF-DRQYDFILSTVVLMFLEAKT 114
Cdd:pfam13649 2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFpDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
2XVA_D 115 IPGLIANMQRCTKPGG 130
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
30-136 |
4.68e-17 |
|
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: 73.51 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 30 VVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDknaMSIANVERIKSIENLDNLHTRVVDLNNLTF-DRQYDFILSTVVLM 108
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARRGADVTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLeDGSFDLVICSEVLE 98
|
90 100
....*....|....*....|....*...
2XVA_D 109 FLEakTIPGLIANMQRCTKPGGYnLIVA 136
Cdd:COG2227 99 HLP--DPAALLRELARLLKPGGL-LLLS 123
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
32-142 |
2.39e-16 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 73.80 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 32 KPGKTLDLGCGNGRNSLYLAA-NGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DRQYDFILSTVVLM 108
Cdd:COG0500 26 KGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPlpAESFDLVVAFGVLH 105
|
90 100 110
....*....|....*....|....*....|....
2XVA_D 109 FLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTAD 142
Cdd:COG0500 106 HLPPEEREALLRELARALKPGGVLLLSASDAAAA 139
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
20-136 |
2.13e-15 |
|
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: 69.64 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 20 THSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERiKSIENLDNLHTRVVDLNNLTF-DRQY 98
Cdd:COG2226 10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARE-RAAEAGLNVEFVVGDAEDLPFpDGSF 88
|
90 100 110
....*....|....*....|....*....|....*...
2XVA_D 99 DFILSTVVLMFLEAKtiPGLIANMQRCTKPGGYnLIVA 136
Cdd:COG2226 89 DLVISSFVLHHLPDP--ERALAEIARVLKPGGR-LVVV 123
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
37-131 |
4.60e-13 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 62.30 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLAANGYDVDAWDknaMSIANVERIKSIENLDNLHTRVVDLNNLTF-DRQYDFILSTVVLMFLEAktI 115
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFpDNSFDLVLSSEVLHHVED--P 75
|
90
....*....|....*.
2XVA_D 116 PGLIANMQRCTKPGGY 131
Cdd:pfam08241 76 ERALREIARVLKPGGI 91
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
19-160 |
1.65e-10 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 57.32 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 19 RTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWD--KNAMSIAnveRIKSIEnlDNLHtrVVDLNNLTF-D 95
Cdd:COG4976 33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDlsEEMLAKA---REKGVY--DRLL--VADLADLAEpD 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
2XVA_D 96 RQYDFILSTVVLMFLEAktIPGLIANMQRCTKPGGynLIVAAMDTADypcTVGFpFAFKEGELRR 160
Cdd:COG4976 106 GRFDLIVAADVLTYLGD--LAAVFAGVARALKPGG--LFIFSVEDAD---GSGR-YAHSLDYVRD 162
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
37-131 |
5.13e-10 |
|
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: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLA-ANGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DRQYDFILSTVVLMFLEAk 113
Cdd:cd02440 3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE- 81
|
90
....*....|....*...
2XVA_D 114 TIPGLIANMQRCTKPGGY 131
Cdd:cd02440 82 DLARFLEEARRLLKPGGV 99
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
32-134 |
4.97e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 50.50 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 32 KPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIAnveriksiENLDNLHTRVVDLNNLTF-DRQYDFILSTvvlMFL 110
Cdd:pfam13489 22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIE--------RALLNVRFDQFDEQEAAVpAGKFDVIVAR---EVL 90
|
90 100
....*....|....*....|....*
2XVA_D 111 EA-KTIPGLIANMQRCTKPGGYNLI 134
Cdd:pfam13489 91 EHvPDPPALLRQIAALLKPGGLLLL 115
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
37-131 |
5.15e-08 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 48.90 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLAAN-------GYDVDAwdknAMSIANVERIKSIENLDNLHTRVVDLN-NLTFDRQYDFILSTVVLM 108
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlpgleytGLDISP----AALEAARERLAALGLLNAVRVELFQLDlGELDPGSFDVVVASNVLH 76
|
90 100
....*....|....*....|...
2XVA_D 109 FLeaKTIPGLIANMQRCTKPGGY 131
Cdd:pfam08242 77 HL--ADPRAVLRNIRRLLKPGGV 97
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
25-103 |
5.88e-08 |
|
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.
Pssm-ID: 428349 [Multi-domain] Cd Length: 170 Bit Score: 50.28 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 25 LEAVKVVKPGKTLDLGCGNGRNSLYLAANGYD--VDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTFDRQYDFIL 102
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaeLTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLII 103
|
.
2XVA_D 103 S 103
Cdd:pfam05175 104 S 104
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
25-136 |
1.55e-07 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 49.42 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 25 LEAVKVVKPGKTLDLGCGNGRNSLYLAANGYD--VDAWDKNAMSIA----NVERiksiENLDNLHTRVVDLNNLTFDRQY 98
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVElaraNAAA----NGLENVEVLWSDGLSGVPDGSF 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
2XVA_D 99 DFILS-------------TVVLMFLEAKtipglianmqRCTKPGGYNLIVA 136
Cdd:COG2813 118 DLILSnppfhagravdkeVAHALIADAA----------RHLRPGGELWLVA 158
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
19-140 |
9.91e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 44.54 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 19 RTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAA---NGYDVDAWDKNAMSIANV-ERIKsiENLDNLHTRVVDLNNLTF 94
Cdd:PRK08317 6 RYRARTFELLAVQPGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLALAkERAA--GLGPNVEFVRGDADGLPF 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
2XVA_D 95 DRQY-DFILSTVVLMFLEAKtiPGLIANMQRCTKPGGYnliVAAMDT 140
Cdd:PRK08317 84 PDGSfDAVRSDRVLQHLEDP--ARALAEIARVLRPGGR---VVVLDT 125
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
32-134 |
9.86e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 40.86 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 32 KPGKTLDLGCGNGRNSLYLAANGY---DVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF---DRQYDFILSTV 105
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPElleDDKFDVVISNC 82
|
90 100
....*....|....*....|....*....
2XVA_D 106 VLMFLEAKtiPGLIANMQRCTKPGGYNLI 134
Cdd:pfam13847 83 VLNHIPDP--DKVLQEILRVLKPGGRLII 109
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
4-134 |
1.17e-03 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 38.96 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 4 VIRDENYFTDKYELT---RTHSEVLEAVKVvKPG-KTLDLGCGNGRNSLYLAANgYDVDA----WDKNAMSIAnVERikS 75
Cdd:PLN02336 235 ILRYERVFGEGFVSTgglETTKEFVDKLDL-KPGqKVLDVGCGIGGGDFYMAEN-FDVHVvgidLSVNMISFA-LER--A 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 76 IENLDNLHTRVVDLNNLTF-DRQYDFILSTVVLMFLEAKtiPGLIANMQRCTKPGGYNLI 134
Cdd:PLN02336 310 IGRKCSVEFEVADCTKKTYpDNSFDVIYSRDTILHIQDK--PALFRSFFKWLKPGGKVLI 367
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
37-130 |
2.13e-03 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 37.82 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIEnldnlHTRVVDLNNLTF-DRQYDFILSTVVLMFleAKTI 115
Cdd:PRK10258 47 LDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD-----HYLAGDIESLPLaTATFDLAWSNLAVQW--CGNL 119
|
90
....*....|....*
2XVA_D 116 PGLIANMQRCTKPGG 130
Cdd:PRK10258 120 STALRELYRVVRPGG 134
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
37-138 |
2.66e-03 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 37.51 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 37 LDLGCGNGRNSLYLAANGYDVDAWD-KNAMSIANVERIKSIENLDNLHTRVVDLNNLTfdRQYDFILSTVVLMFLEAKTI 115
Cdd:PRK07580 68 LDAGCGVGSLSIPLARRGAKVVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL--GRFDTVVCLDVLIHYPQEDA 145
|
90 100 110
....*....|....*....|....*....|.
2XVA_D 116 PGLIANMQRCTK--------PggYNLIVAAM 138
Cdd:PRK07580 146 ARMLAHLASLTRgsliftfaP--YTPLLALL 174
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
25-131 |
3.85e-03 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 37.07 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 25 LEAV-KVVKPGKT-LDLGCGngrnS-------LYLAAN---GYDVDAWdknAMSIA--NVERiksieNldNLHTRV-VDL 89
Cdd:COG2264 139 LEALeKLLKPGKTvLDVGCG----SgilaiaaAKLGAKrvlAVDIDPV---AVEAAreNAEL-----N--GVEDRIeVVL 204
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
2XVA_D 90 NNLTFDRQYDF----ILSTVVLMfleaktipgLIANMQRCTKPGGY 131
Cdd:COG2264 205 GDLLEDGPYDLvvanILANPLIE---------LAPDLAALLKPGGY 241
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
34-131 |
8.56e-03 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 36.27 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XVA_D 34 GKT-LDLGCGNGRNSLYLAANGYDVDAWDknamSIANVerIKSIENLDNLHTRV------VDLNNLTF-DRQYDFILSTV 105
Cdd:PLN02336 38 GKSvLELGAGIGRFTGELAKKAGQVIALD----FIESV--IKKNESINGHYKNVkfmcadVTSPDLNIsDGSVDLIFSNW 111
|
90 100
....*....|....*....|....*.
2XVA_D 106 VLMFLEAKTIPGLIANMQRCTKPGGY 131
Cdd:PLN02336 112 LLMYLSDKEVENLAERMVKWLKVGGY 137
|
|
| |
