|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
1-196 |
2.03e-150 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 414.90 E-value: 2.03e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 1 MIIRDENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:PRK11207 1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:PRK11207 81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446509218 161 EGWEMVKYNENVGELHRTDANGNRIKLRFATILARK 196
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
|
|
| tehB |
TIGR00477 |
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular ... |
1-196 |
6.07e-128 |
|
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: 358.03 E-value: 6.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 1 MIIRDENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLDnL 80
Cdd:TIGR00477 1 FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNETKEKENLN-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:TIGR00477 80 STALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADYPCPLPFSFTFKENELREYY 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 446509218 161 EGWEMVKYNENVGELHRTDANGNRIKLRFATILARK 196
Cdd:TIGR00477 160 KDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK 195
|
|
| TehB |
pfam03848 |
Tellurite resistance protein TehB; |
1-193 |
2.77e-122 |
|
Tellurite resistance protein TehB;
Pssm-ID: 397776 Cd Length: 193 Bit Score: 343.37 E-value: 2.77e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 1 MIIRDENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:pfam03848 1 FYCKKEDYFHKKYNLTPTHSEVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:pfam03848 81 HTALYDINNATIDENYDFILSTVVLMFLEPERIPGIIANMQECTNPGGYNLIVAAMSTDDVPCTVPFSFTFKEGELKRYY 160
|
170 180 190
....*....|....*....|....*....|...
gi 446509218 161 EGWEMVKYNENVGELHRTDANGNRIKLRFATIL 193
Cdd:pfam03848 161 QDWERVKYNEDVGELHKTDANGNRIKLRFATML 193
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
29-135 |
9.58e-19 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 78.82 E-value: 9.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 29 VKPGKT-LDLGCGNGRNSLYLAAN-GYEVDAWDKNAMSIANVERIKSIENL-DNLHTRVVDLNNLTFDGQYDFILSTVVL 105
Cdd:COG2230 49 LKPGMRvLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVSIGMF 128
|
90 100 110
....*....|....*....|....*....|
gi 446509218 106 MFLEAKTIPGLIANMQRCTKPGGYNLIVAA 135
Cdd:COG2230 129 EHVGPENYPAYFAKVARLLKPGGRLLLHTP 158
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
35-129 |
9.95e-11 |
|
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: 56.28 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLA-ANGYEVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DGQYDFILSTVVLMFLEAk 111
Cdd:cd02440 3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE- 81
|
90
....*....|....*...
gi 446509218 112 TIPGLIANMQRCTKPGGY 129
Cdd:cd02440 82 DLARFLEEARRLLKPGGV 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11207 |
PRK11207 |
tellurite resistance methyltransferase TehB; |
1-196 |
2.03e-150 |
|
tellurite resistance methyltransferase TehB;
Pssm-ID: 183040 Cd Length: 197 Bit Score: 414.90 E-value: 2.03e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 1 MIIRDENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:PRK11207 1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:PRK11207 81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446509218 161 EGWEMVKYNENVGELHRTDANGNRIKLRFATILARK 196
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
|
|
| tehB |
TIGR00477 |
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular ... |
1-196 |
6.07e-128 |
|
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: 358.03 E-value: 6.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 1 MIIRDENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLDnL 80
Cdd:TIGR00477 1 FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNETKEKENLN-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:TIGR00477 80 STALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADYPCPLPFSFTFKENELREYY 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 446509218 161 EGWEMVKYNENVGELHRTDANGNRIKLRFATILARK 196
Cdd:TIGR00477 160 KDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK 195
|
|
| TehB |
pfam03848 |
Tellurite resistance protein TehB; |
1-193 |
2.77e-122 |
|
Tellurite resistance protein TehB;
Pssm-ID: 397776 Cd Length: 193 Bit Score: 343.37 E-value: 2.77e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 1 MIIRDENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:pfam03848 1 FYCKKEDYFHKKYNLTPTHSEVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:pfam03848 81 HTALYDINNATIDENYDFILSTVVLMFLEPERIPGIIANMQECTNPGGYNLIVAAMSTDDVPCTVPFSFTFKEGELKRYY 160
|
170 180 190
....*....|....*....|....*....|...
gi 446509218 161 EGWEMVKYNENVGELHRTDANGNRIKLRFATIL 193
Cdd:pfam03848 161 QDWERVKYNEDVGELHKTDANGNRIKLRFATML 193
|
|
| PRK12335 |
PRK12335 |
tellurite resistance protein TehB; Provisional |
6-197 |
6.77e-117 |
|
tellurite resistance protein TehB; Provisional
Pssm-ID: 183450 [Multi-domain] Cd Length: 287 Bit Score: 333.45 E-value: 6.77e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 6 ENYFTEKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIENLdNLHTRVV 85
Cdd:PRK12335 96 EDYFHKKYNLTATHSEVLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENL-NIRTGLY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 86 DLNNLTFDGQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYYEGWEM 165
Cdd:PRK12335 175 DINSASIQEEYDFILSTVVLMFLNRERIPAIIKNMQEHTNPGGYNLIVCAMDTEDYPCPMPFSFTFKEGELKDYYQDWEI 254
|
170 180 190
....*....|....*....|....*....|..
gi 446509218 166 VKYNENVGELHRTDANGNRIKLRFATILARKK 197
Cdd:PRK12335 255 VKYNENVGHLHKTDENGNRIKLRFATLLAKKV 286
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
29-135 |
9.58e-19 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 78.82 E-value: 9.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 29 VKPGKT-LDLGCGNGRNSLYLAAN-GYEVDAWDKNAMSIANVERIKSIENL-DNLHTRVVDLNNLTFDGQYDFILSTVVL 105
Cdd:COG2230 49 LKPGMRvLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVSIGMF 128
|
90 100 110
....*....|....*....|....*....|
gi 446509218 106 MFLEAKTIPGLIANMQRCTKPGGYNLIVAA 135
Cdd:COG2230 129 EHVGPENYPAYFAKVARLLKPGGRLLLHTP 158
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
30-133 |
2.58e-18 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 76.02 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 30 KPGKTLDLGCGNGRNSLYLAAN--GYEVDAWDKNAMSIAnveriKSIENLDNLHTRVVDLNNLTFDGQYDFILSTVVLMF 107
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLA-----RARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHW 75
|
90 100
....*....|....*....|....*.
gi 446509218 108 LEAktIPGLIANMQRCTKPGGYNLIV 133
Cdd:COG4106 76 LPD--HAALLARLAAALAPGGVLAVQ 99
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
35-128 |
5.21e-18 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 75.29 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLAAN-GYEVDAWDKNAMSIANVERIKSIENLdNLHTRVVDLNNLTF-DGQYDFILSTVVLMFLEAKT 112
Cdd:pfam13649 2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFpDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 446509218 113 IPGLIANMQRCTKPGG 128
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
28-134 |
1.12e-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: 75.05 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 28 VVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDknaMSIANVERIKSIENLDNLHTRVVDLNNLTF-DGQYDFILSTVVLM 106
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARRGADVTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLeDGSFDLVICSEVLE 98
|
90 100
....*....|....*....|....*...
gi 446509218 107 FLEakTIPGLIANMQRCTKPGGYnLIVA 134
Cdd:COG2227 99 HLP--DPAALLRELARLLKPGGL-LLLS 123
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
11-134 |
8.63e-17 |
|
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: 73.49 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 11 EKYELTRthsEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERiKSIENLDNLHTRVVDLNNL 90
Cdd:COG2226 6 ARYDGRE---ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARE-RAAEAGLNVEFVVGDAEDL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446509218 91 TF-DGQYDFILSTVVLMFLEAKtiPGLIANMQRCTKPGGYnLIVA 134
Cdd:COG2226 82 PFpDGSFDLVISSFVLHHLPDP--ERALAEIARVLKPGGR-LVVV 123
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
30-140 |
9.83e-17 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 74.57 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 30 KPGKTLDLGCGNGRNSLYLAA-NGYEVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DGQYDFILSTVVLM 106
Cdd:COG0500 26 KGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPlpAESFDLVVAFGVLH 105
|
90 100 110
....*....|....*....|....*....|....
gi 446509218 107 FLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTAD 140
Cdd:COG0500 106 HLPPEEREALLRELARALKPGGVLLLSASDAAAA 139
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
35-129 |
1.70e-14 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 65.76 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLAANGYEVDAWDknaMSIANVERIKSIENLDNLHTRVVDLNNLTF-DGQYDFILSTVVLMFLEAktI 113
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFpDNSFDLVLSSEVLHHVED--P 75
|
90
....*....|....*.
gi 446509218 114 PGLIANMQRCTKPGGY 129
Cdd:pfam08241 76 ERALREIARVLKPGGI 91
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
17-158 |
3.67e-11 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 59.24 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 17 RTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWD--KNAMSIAnveRIKSIEnlDNLHtrVVDLNNLTF-D 93
Cdd:COG4976 33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDlsEEMLAKA---REKGVY--DRLL--VADLADLAEpD 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446509218 94 GQYDFILSTVVLMFLEAktIPGLIANMQRCTKPGGynLIVAAMDTADypcTVGFpFAFKEGELRR 158
Cdd:COG4976 106 GRFDLIVAADVLTYLGD--LAAVFAGVARALKPGG--LFIFSVEDAD---GSGR-YAHSLDYVRD 162
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
35-129 |
9.95e-11 |
|
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: 56.28 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLA-ANGYEVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DGQYDFILSTVVLMFLEAk 111
Cdd:cd02440 3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE- 81
|
90
....*....|....*...
gi 446509218 112 TIPGLIANMQRCTKPGGY 129
Cdd:cd02440 82 DLARFLEEARRLLKPGGV 99
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
23-101 |
1.11e-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: 52.21 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 23 LEAVKVVKPGKTLDLGCGNGRNSLYLAANG--YEVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTFDGQYDFIL 100
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLII 103
|
.
gi 446509218 101 S 101
Cdd:pfam05175 104 S 104
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
23-134 |
2.07e-08 |
|
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: 51.73 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 23 LEAVKVVKPGKTLDLGCGNGRNSLYLAAN--GYEVDAWDKNAMSIA----NVERiksiENLDNLHTRVVDLNNLTFDGQY 96
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVElaraNAAA----NGLENVEVLWSDGLSGVPDGSF 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446509218 97 DFILS-------------TVVLMFLEAKtipglianmqRCTKPGGYNLIVA 134
Cdd:COG2813 118 DLILSnppfhagravdkeVAHALIADAA----------RHLRPGGELWLVA 158
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
35-129 |
2.14e-08 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 50.06 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLAAN--GYEVDAWDKNAMSIANV-ERIKSIENLDNLHTRVVDLN-NLTFDGQYDFILSTVVLMFLea 110
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAArERLAALGLLNAVRVELFQLDlGELDPGSFDVVVASNVLHHL-- 78
|
90
....*....|....*....
gi 446509218 111 KTIPGLIANMQRCTKPGGY 129
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGGV 97
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
30-132 |
2.22e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 51.27 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 30 KPGKTLDLGCGNGRNSLYLAANGYEVDAWDKNAMSIAnveriksiENLDNLHTRVVDLNNLTF-DGQYDFILSTvvlMFL 108
Cdd:pfam13489 22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIE--------RALLNVRFDQFDEQEAAVpAGKFDVIVAR---EVL 90
|
90 100
....*....|....*....|....*
gi 446509218 109 EA-KTIPGLIANMQRCTKPGGYNLI 132
Cdd:pfam13489 91 EHvPDPPALLRQIAALLKPGGLLLL 115
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
29-138 |
8.99e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 50.71 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 29 VKPGKT-LDLGCGNGRNSLYLAA---NGYEVDAWDKNAMSIANV-ERIKsiENLDNLHTRVVDLNNLTF-DGQYDFILST 102
Cdd:PRK08317 17 VQPGDRvLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLALAkERAA--GLGPNVEFVRGDADGLPFpDGSFDAVRSD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 446509218 103 VVLMFLEAKtiPGLIANMQRCTKPGGYnliVAAMDT 138
Cdd:PRK08317 95 RVLQHLEDP--ARALAEIARVLRPGGR---VVVLDT 125
|
|
| TPMT |
pfam05724 |
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ... |
23-180 |
2.13e-06 |
|
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.
Pssm-ID: 399030 Cd Length: 218 Bit Score: 46.27 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 23 LEAVKVVKPGKTLDLGCGNGRNSLYLAANGYEVDAWD--KNAMSIANVERI---KSIENLDNLHTRVVDLNNLTFD---- 93
Cdd:pfam05724 30 WDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEisELAVEKFFAEAGlspPITELSGFKEYSSGNISLYCGDfftl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 94 -----GQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVaamdTADYPCT--VGFPFAFKEGELRRYYEGwemv 166
Cdd:pfam05724 110 preelGKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRGLLI----TLDYPQTdhEGPPFSVPAAELEALFGG---- 181
|
170
....*....|....
gi 446509218 167 kyNENVGELHRTDA 180
Cdd:pfam05724 182 --GWKVAELEREDA 193
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
35-136 |
3.92e-05 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 42.90 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLAANGYEVDAWD-KNAMSIANVERIKSIENLDNLHTRVVDLNNLTfdGQYDFILSTVVLMFLEAKTI 113
Cdd:PRK07580 68 LDAGCGVGSLSIPLARRGAKVVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL--GRFDTVVCLDVLIHYPQEDA 145
|
90 100 110
....*....|....*....|....*....|.
gi 446509218 114 PGLIANMQRCTK--------PggYNLIVAAM 136
Cdd:PRK07580 146 ARMLAHLASLTRgsliftfaP--YTPLLALL 174
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
30-132 |
5.05e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 41.63 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 30 KPGKTLDLGCGNGRNSLYLAANGY---EVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF---DGQYDFILSTV 103
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPElleDDKFDVVISNC 82
|
90 100
....*....|....*....|....*....
gi 446509218 104 VLMFLEAKtiPGLIANMQRCTKPGGYNLI 132
Cdd:pfam13847 83 VLNHIPDP--DKVLQEILRVLKPGGRLII 109
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
35-128 |
2.32e-04 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 40.51 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 35 LDLGCGNGRNSLYLAANGYEVDAWDKNAMSIANVERIKSIEnldnlHTRVVDLNNLTF-DGQYDFILSTVVLMFleAKTI 113
Cdd:PRK10258 47 LDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD-----HYLAGDIESLPLaTATFDLAWSNLAVQW--CGNL 119
|
90
....*....|....*
gi 446509218 114 PGLIANMQRCTKPGG 128
Cdd:PRK10258 120 STALRELYRVVRPGG 134
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
2-132 |
4.86e-04 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 40.12 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 2 IIRDENYFTEKYELT---RTHSEVLEAVKVvKPG-KTLDLGCGNGRNSLYLAAN-GYEVDAWDK--NAMSIAnVERikSI 74
Cdd:PLN02336 235 ILRYERVFGEGFVSTgglETTKEFVDKLDL-KPGqKVLDVGCGIGGGDFYMAENfDVHVVGIDLsvNMISFA-LER--AI 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446509218 75 ENLDNLHTRVVDLNNLTF-DGQYDFILSTVVLMFLEAKtiPGLIANMQRCTKPGGYNLI 132
Cdd:PLN02336 311 GRKCSVEFEVADCTKKTYpDNSFDVIYSRDTILHIQDK--PALFRSFFKWLKPGGKVLI 367
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
32-129 |
5.09e-04 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 40.12 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 32 GKT-LDLGCGNGRNSLYLAANGYEVDAWDknamSIANVerIKSIENLDNLHTRV------VDLNNLTF-DGQYDFILSTV 103
Cdd:PLN02336 38 GKSvLELGAGIGRFTGELAKKAGQVIALD----FIESV--IKKNESINGHYKNVkfmcadVTSPDLNIsDGSVDLIFSNW 111
|
90 100
....*....|....*....|....*.
gi 446509218 104 VLMFLEAKTIPGLIANMQRCTKPGGY 129
Cdd:PLN02336 112 LLMYLSDKEVENLAERMVKWLKVGGY 137
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
23-129 |
3.59e-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: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 23 LEAV-KVVKPGKT-LDLGCGngrnS-------LYLAANgyEVDAWDKNAMSIANverikSIENLD--NLHTRV-VDLNNL 90
Cdd:COG2264 139 LEALeKLLKPGKTvLDVGCG----SgilaiaaAKLGAK--RVLAVDIDPVAVEA-----ARENAElnGVEDRIeVVLGDL 207
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446509218 91 TFDGQYDF----ILSTVVLMfleaktipgLIANMQRCTKPGGY 129
Cdd:COG2264 208 LEDGPYDLvvanILANPLIE---------LAPDLAALLKPGGY 241
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
21-101 |
8.74e-03 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 35.90 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509218 21 EVLEAVKVVKPGKTLDLGCGNGRNSLYLAAN--GYEVDAWD--KNAMSIA--NVERIksienldNLHTRVV----DL-NN 89
Cdd:COG2890 103 LALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDisPDALAVArrNAERL-------GLEDRVRflqgDLfEP 175
|
90
....*....|..
gi 446509218 90 LTFDGQYDFILS 101
Cdd:COG2890 176 LPGDGRFDLIVS 187
|
|
| |
