|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11036 |
PRK11036 |
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
1-255 |
0e+00 |
|
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
Pssm-ID: 182918 Cd Length: 255 Bit Score: 546.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 1 MQDRNFDDIAEKFSRNIYGTTKGQLRQAILWQDLDRVLAEMGPQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMID 80
Cdd:PRK11036 1 MQDRNFDDIAEKFSRNIYGTTKGQIRQAILWQDLDRLLAELPPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 81 RAKQAAEAKGVSDNMQFIHCAAQDVASHLETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYNAHGLLMHNM 160
Cdd:PRK11036 81 RAKQAAEAKGVSDNMQFIHCAAQDIAQHLETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGGALSLMFYNANGLLMHNM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 161 VAGNFDYVQAGMPKKKKRTLSPDYPRDPTQVYLWLEEAGWQIMGKTGVRVFHDYLREKHQQRDCYEALLELETRYCRQEP 240
Cdd:PRK11036 161 VAGNFDYVQAGMPKRKKRTLSPDYPLDPEQVYQWLEEAGWQIMGKTGVRVFHDYLRNKHQQRDCFEALLELEQRYCRQEP 240
|
250
....*....|....*
gi 15830258 241 YITLGRYIHVTARKP 255
Cdd:PRK11036 241 YISLGRYIHVTARKP 255
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
33-151 |
3.10e-33 |
|
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: 117.43 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 33 DLDRVLAEMGPQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVsdnmQFIHCAAQDVASHLETp 112
Cdd:COG2227 13 RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLPLEDGS- 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 15830258 113 VDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYN 151
Cdd:COG2227 88 FDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
48-143 |
6.02e-21 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 84.54 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 48 VLDAGGGEGQTAIKMAER-GHQVILCDLSAQMIDRAKQAAEAKGVsdNMQFIHCAAQDVASHLETpVDLILFHAVLEWVA 126
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGS-FDLVVSSGVLHHLP 77
|
90
....*....|....*....
gi 15830258 127 DP--RSVLQTLWSVLRPGG 143
Cdd:pfam13649 78 DPdlEAALREIARVLKPGG 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
47-150 |
2.02e-17 |
|
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: 75.54 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAER-GHQVILCDLSAQMIDRAKQAAEAKGvSDNMQFIHCAAQDVASHLETPVDLILFHAVLEW- 124
Cdd:cd02440 1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPEADESFDVIISDPPLHHl 79
|
90 100
....*....|....*....|....*.
gi 15830258 125 VADPRSVLQTLWSVLRPGGVLSLMFY 150
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVLTLV 105
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
47-145 |
9.70e-09 |
|
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 54.21 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAERGHQV--ILCDLSAQMIDRAKQAaeakgVSDNMQFIhCAAQDVASHLETPVDLILFHAVLEW 124
Cdd:TIGR02072 37 SVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTK-----LSENVQFI-CGDAEKLPLEDSSFDLIVSNLALQW 110
|
90 100
....*....|....*....|.
gi 15830258 125 VADPRSVLQTLWSVLRPGGVL 145
Cdd:TIGR02072 111 CDDLSQALSELARVLKPGGLL 131
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
46-148 |
4.07e-03 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 37.40 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 46 LRVLDAGGGEGQTAIKMAER-GH-QVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHcaaQDVASHLETPV-DLILFHAVL 122
Cdd:smart00828 1 KRVLDFGCGYGSDLIDLAERhPHlQLHGYTISPEQAEVGRERIRALGLQGRIRIFY---RDSAKDPFPDTyDLVFGFEVI 77
|
90 100
....*....|....*....|....*.
gi 15830258 123 EWVADPRSVLQTLWSVLRPGGVLSLM 148
Cdd:smart00828 78 HHIKDKMDLFSNISRHLKDGGHLVLA 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11036 |
PRK11036 |
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
1-255 |
0e+00 |
|
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
Pssm-ID: 182918 Cd Length: 255 Bit Score: 546.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 1 MQDRNFDDIAEKFSRNIYGTTKGQLRQAILWQDLDRVLAEMGPQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMID 80
Cdd:PRK11036 1 MQDRNFDDIAEKFSRNIYGTTKGQIRQAILWQDLDRLLAELPPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 81 RAKQAAEAKGVSDNMQFIHCAAQDVASHLETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYNAHGLLMHNM 160
Cdd:PRK11036 81 RAKQAAEAKGVSDNMQFIHCAAQDIAQHLETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGGALSLMFYNANGLLMHNM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 161 VAGNFDYVQAGMPKKKKRTLSPDYPRDPTQVYLWLEEAGWQIMGKTGVRVFHDYLREKHQQRDCYEALLELETRYCRQEP 240
Cdd:PRK11036 161 VAGNFDYVQAGMPKRKKRTLSPDYPLDPEQVYQWLEEAGWQIMGKTGVRVFHDYLRNKHQQRDCFEALLELEQRYCRQEP 240
|
250
....*....|....*
gi 15830258 241 YITLGRYIHVTARKP 255
Cdd:PRK11036 241 YISLGRYIHVTARKP 255
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
33-151 |
3.10e-33 |
|
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: 117.43 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 33 DLDRVLAEMGPQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVsdnmQFIHCAAQDVASHLETp 112
Cdd:COG2227 13 RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLPLEDGS- 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 15830258 113 VDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYN 151
Cdd:COG2227 88 FDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
26-145 |
3.30e-24 |
|
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: 94.29 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 26 RQAILWQDLDRVLAEMGPQK-LRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVsdNMQFIHCAAQD 104
Cdd:COG2226 3 RVAARYDGREALLAALGLRPgARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAED 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15830258 105 V----AShletpVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVL 145
Cdd:COG2226 81 LpfpdGS-----FDLVISSFVLHHLPDPERALAEIARVLKPGGRL 120
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
47-145 |
2.18e-21 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 85.65 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAER--GHQVILCDLSAQMIDRAKQAAeakgvsDNMQFIHCAAQDVAshLETPVDLILFHAVLEW 124
Cdd:COG4106 4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLD--PPEPFDLVVSNAALHW 75
|
90 100
....*....|....*....|.
gi 15830258 125 VADPRSVLQTLWSVLRPGGVL 145
Cdd:COG4106 76 LPDHAALLARLAAALAPGGVL 96
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
48-143 |
6.02e-21 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 84.54 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 48 VLDAGGGEGQTAIKMAER-GHQVILCDLSAQMIDRAKQAAEAKGVsdNMQFIHCAAQDVASHLETpVDLILFHAVLEWVA 126
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGS-FDLVVSSGVLHHLP 77
|
90
....*....|....*....
gi 15830258 127 DP--RSVLQTLWSVLRPGG 143
Cdd:pfam13649 78 DPdlEAALREIARVLKPGG 96
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
4-145 |
4.66e-19 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 81.13 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 4 RNFDDIAEKFSRNIYGTTKGQLRQAILWQdLDRVLAEMGPQK-LRVLDAGGGEGQTAIKMAER-GHQVILCDLSAQMIDR 81
Cdd:COG2230 11 RLFLDPTMTYSCAYFEDPDDTLEEAQEAK-LDLILRKLGLKPgMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEY 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830258 82 AKQAAEAKGVSDNMQFIHCAAQDVAshLETPVDLILFHAVLEWVADP--RSVLQTLWSVLRPGGVL 145
Cdd:COG2230 90 ARERAAEAGLADRVEVRLADYRDLP--ADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRL 153
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
43-187 |
6.06e-19 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 82.27 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 43 PQKLRVLDAGGGEGQTAIKMAER-GHQVILCDLSAQMIDRAKQAAEAKGVSdNMQFIHCAAQDVASHLETPVDLILFHAV 121
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLG-NVEFLVADLAELDPLPAESFDLVVAFGV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830258 122 LEWV--ADPRSVLQTLWSVLRPGGVLSLMFYNAHGLLMHNMVAGNFDYVQAGMPKKKKRTLSPDYPRD 187
Cdd:COG0500 104 LHHLppEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRLLALELYLRA 171
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
6-145 |
1.52e-18 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 80.43 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 6 FDDIAEKFSRNIYGTTKGQLRQAILwqdlDRVLAEMGPQK-LRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKq 84
Cdd:COG4976 11 FDQYADSYDAALVEDLGYEAPALLA----EELLARLPPGPfGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830258 85 aaeAKGVSDNmqFIHCAAQDVAsHLETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVL 145
Cdd:COG4976 86 ---EKGVYDR--LLVADLADLA-EPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLF 140
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
49-147 |
4.23e-18 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 76.93 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 49 LDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSdnmqFIHCAAQDVAsHLETPVDLILFHAVLEWVADP 128
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT----FVVGDAEDLP-FPDNSFDLVLSSEVLHHVEDP 75
|
90
....*....|....*....
gi 15830258 129 RSVLQTLWSVLRPGGVLSL 147
Cdd:pfam08241 76 ERALREIARVLKPGGILII 94
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
47-150 |
2.02e-17 |
|
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: 75.54 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAER-GHQVILCDLSAQMIDRAKQAAEAKGvSDNMQFIHCAAQDVASHLETPVDLILFHAVLEW- 124
Cdd:cd02440 1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPEADESFDVIISDPPLHHl 79
|
90 100
....*....|....*....|....*.
gi 15830258 125 VADPRSVLQTLWSVLRPGGVLSLMFY 150
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVLTLV 105
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
49-145 |
6.35e-16 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 71.24 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 49 LDAGGGEGQTAIKMAERGHQ--VILCDLSAQMIDRAKQAAEAKGVsDNMQFIHCAAQDVASHLETPVDLILFHAVLEWVA 126
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGleYTGLDISPAALEAARERLAALGL-LNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79
|
90
....*....|....*....
gi 15830258 127 DPRSVLQTLWSVLRPGGVL 145
Cdd:pfam08242 80 DPRAVLRNIRRLLKPGGVL 98
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
46-199 |
1.92e-15 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 71.29 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 46 LRVLDAGGGEGQTAIKMAER---GHQVILCDLSAQMIDRAKQAAEAKGvSDNMQFIHCAAQDVASHLE-TPVDLILFHAV 121
Cdd:pfam13847 5 MRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLG-FDNVEFEQGDIEELPELLEdDKFDVVISNCV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830258 122 LEWVADPRSVLQTLWSVLRPGGVLSLMFYNAHGLLMHNMVAGNFDYVQagmpkkkkrtlSPDYPRDPTQVYLWLEEAG 199
Cdd:pfam13847 84 LNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAG-----------CVGGAILKKKLYELLEEAG 150
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
27-202 |
3.87e-13 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 65.53 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 27 QAILWQDLDRVLAEMGP---QKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAkgvsdnmqfiHCAAQ 103
Cdd:pfam13489 2 AHQRERLLADLLLRLLPklpSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF----------DQFDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 104 DVASHLETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYNAHgLLMHNMvagnFDYVQAGMPKKKKRTLspd 183
Cdd:pfam13489 72 QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAS-DEADRL----LLEWPYLRPRNGHISL--- 143
|
170
....*....|....*....
gi 15830258 184 ypRDPTQVYLWLEEAGWQI 202
Cdd:pfam13489 144 --FSARSLKRLLEEAGFEV 160
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
34-121 |
2.17e-11 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 61.78 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 34 LDRVLAEMG----PQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSDNMQFihcAAQDVASHL 109
Cdd:PRK07580 49 RDTVLSWLPadgdLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITF---EVGDLESLL 125
|
90
....*....|..
gi 15830258 110 ETpvdlilFHAV 121
Cdd:PRK07580 126 GR------FDTV 131
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
32-146 |
3.17e-10 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 59.00 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 32 QDLDRVLAEMGPQKL-RVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKgvsdnmqfiHCAAQDVAS--H 108
Cdd:PRK10258 29 QSADALLAMLPQRKFtHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD---------HYLAGDIESlpL 99
|
90 100 110
....*....|....*....|....*....|....*...
gi 15830258 109 LETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLS 146
Cdd:PRK10258 100 ATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVA 137
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
47-143 |
4.16e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 58.41 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAER---GHQVILCDLSAQMIDRAKQAAEAKGvsDNMQFIhcaaQDVASHLETP---VDLILFHA 120
Cdd:PRK08317 22 RVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLG--PNVEFV----RGDADGLPFPdgsFDAVRSDR 95
|
90 100
....*....|....*....|...
gi 15830258 121 VLEWVADPRSVLQTLWSVLRPGG 143
Cdd:PRK08317 96 VLQHLEDPARALAEIARVLRPGG 118
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
35-145 |
8.05e-09 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 54.77 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 35 DRVLAEMGPQK-LRVLDAGGGEGQTAIKMAERGH---QVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHCAAqdvashLE 110
Cdd:PRK00216 41 RKTIKWLGVRPgDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDA------EA 114
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15830258 111 TPVDLILFHAV-----LEWVADPRSVLQTLWSVLRPGGVL 145
Cdd:PRK00216 115 LPFPDNSFDAVtiafgLRNVPDIDKALREMYRVLKPGGRL 154
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
47-145 |
9.70e-09 |
|
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 54.21 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAERGHQV--ILCDLSAQMIDRAKQAaeakgVSDNMQFIhCAAQDVASHLETPVDLILFHAVLEW 124
Cdd:TIGR02072 37 SVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTK-----LSENVQFI-CGDAEKLPLEDSSFDLIVSNLALQW 110
|
90 100
....*....|....*....|.
gi 15830258 125 VADPRSVLQTLWSVLRPGGVL 145
Cdd:TIGR02072 111 CDDLSQALSELARVLKPGGLL 131
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
36-162 |
7.31e-07 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 47.87 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 36 RVLAEM-GPQklRVLDAGGGEGQTAIKMAE---RGHQVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHCAAQDVASHLET 111
Cdd:COG4122 9 YLLARLlGAK--RILEIGTGTGYSTLWLARalpDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLAD 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15830258 112 -PVDLILFhavlewVADPRS---VLQTLWSVLRPGGVlsLMFYNAhglLMHNMVA 162
Cdd:COG4122 87 gPFDLVFI------DADKSNypdYLELALPLLRPGGL--IVADNV---LWHGRVA 130
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
47-145 |
1.55e-06 |
|
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: 47.85 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMA----ERGHqVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHcaaQDVASHL-ETPVDLIlfhaV 121
Cdd:COG2519 94 RVLEAGTGSGALTLALAravgPEGK-VYSYERREDFAEIARKNLERFGLPDNVELKL---GDIREGIdEGDVDAV----F 165
|
90 100
....*....|....*....|....
gi 15830258 122 LEwVADPRSVLQTLWSVLRPGGVL 145
Cdd:COG2519 166 LD-MPDPWEALEAVAKALKPGGVL 188
|
|
| PRK01683 |
PRK01683 |
trans-aconitate 2-methyltransferase; Provisional |
47-145 |
3.54e-06 |
|
trans-aconitate 2-methyltransferase; Provisional
Pssm-ID: 234970 Cd Length: 258 Bit Score: 46.86 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAER--GHQVILCDLSAQMIDRAKQAAEakgvsdNMQFIhcaAQDVAS-HLETPVDLILFHAVLE 123
Cdd:PRK01683 34 YVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLP------DCQFV---EADIASwQPPQALDLIFANASLQ 104
|
90 100
....*....|....*....|..
gi 15830258 124 WVADPRSVLQTLWSVLRPGGVL 145
Cdd:PRK01683 105 WLPDHLELFPRLVSLLAPGGVL 126
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
47-117 |
1.19e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 45.03 E-value: 1.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830258 47 RVLDAGGGEGQTAIKMAERG-HQVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHCAAQDVasHLETPVDLIL 117
Cdd:COG4076 38 VVLDIGTGSGLLSMLAARAGaKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDL--DLPEKADVII 107
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
38-146 |
5.57e-05 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 43.40 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 38 LAEMGPQKlRVLDAGGGEGQ----TAIKMAERGHqVILCDLSAQMIDRAKQAAEAKGVsDNMQFI--HCAAQDVASHlet 111
Cdd:PRK11873 72 LAELKPGE-TVLDLGSGGGFdcflAARRVGPTGK-VIGVDMTPEMLAKARANARKAGY-TNVEFRlgEIEALPVADN--- 145
|
90 100 110
....*....|....*....|....*....|....*
gi 15830258 112 PVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLS 146
Cdd:PRK11873 146 SVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFA 180
|
|
| Methyltransf_15 |
pfam09445 |
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ... |
47-114 |
6.10e-05 |
|
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.
Pssm-ID: 370496 Cd Length: 165 Bit Score: 42.32 E-value: 6.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830258 47 RVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHCAAQDVASHLETPVD 114
Cdd:pfam09445 3 RILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKFEKI 70
|
|
| Rsm22 |
COG5459 |
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ... |
38-145 |
1.72e-04 |
|
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins
Pssm-ID: 444210 [Multi-domain] Cd Length: 306 Bit Score: 42.25 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 38 LAEMGPQK--LRVLDAGGGEGQTAIKMA---ERGHQVILCDLSAQMIDRAKQAAEAkGVSDNMQFIHCAAQDVASHLETP 112
Cdd:COG5459 72 LAEAGPDFapLTVLDVGAGPGTAAWAAAdawPSLLDATLLERSAAALALGRRLARA-AANPALETAEWRLADLAAALPAP 150
|
90 100 110
....*....|....*....|....*....|....*.
gi 15830258 113 -VDLILFHAVLEWVADP--RSVLQTLWsvLRPGGVL 145
Cdd:COG5459 151 pADLVVASYVLNELADAarAALVDRLW--LAPDGAL 184
|
|
| PRK14103 |
PRK14103 |
trans-aconitate 2-methyltransferase; Provisional |
34-166 |
2.31e-04 |
|
trans-aconitate 2-methyltransferase; Provisional
Pssm-ID: 184509 Cd Length: 255 Bit Score: 41.60 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 34 LDRVLAEMGPqklRVLDAGGGEGQTAIKMAER--GHQVILCDLSAQMIDRAKqaaeAKGVSdnmqfihCAAQDVASHLET 111
Cdd:PRK14103 22 LARVGAERAR---RVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAAR----ERGVD-------ARTGDVRDWKPK 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830258 112 P-VDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLmfynahgllmhnMVAGNFD 166
Cdd:PRK14103 88 PdTDVVVSNAALQWVPEHADLLVRWVDELAPGSWIAV------------QVPGNFD 131
|
|
| COG2521 |
COG2521 |
Predicted archaeal methyltransferase [General function prediction only]; |
47-186 |
4.62e-04 |
|
Predicted archaeal methyltransferase [General function prediction only];
Pssm-ID: 442011 [Multi-domain] Cd Length: 285 Bit Score: 40.66 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 47 RVLDAGGGEGQTAIKMAERG-HQVILCDLSAQMIDRAKQAAEAKGVSD-NMQFIHC-AAQDVASHLETPVDLILfHavle 123
Cdd:COG2521 135 RVLDTCTGLGYTAIEALKRGaREVITVEKDPNVLELAELNPWSRELANeRIKIILGdASEVIKTFPDESFDAII-H---- 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830258 124 wvaD-PR-SVLQTLWS---------VLRPGGVLslmfynahgllmhnmvagnFDYVqaGMPKKKKRtlSPDYPR 186
Cdd:COG2521 210 ---DpPRfSLAGELYSlefyrelyrVLKPGGRL-------------------FHYT--GNPGKKKR--GRDVPR 257
|
|
| PLN02585 |
PLN02585 |
magnesium protoporphyrin IX methyltransferase |
15-97 |
6.37e-04 |
|
magnesium protoporphyrin IX methyltransferase
Pssm-ID: 215319 [Multi-domain] Cd Length: 315 Bit Score: 40.23 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 15 RNIYGTT----KGQL--RQ--------AILWQDLDRVLaemgpQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMID 80
Cdd:PLN02585 106 RKIYGETdevnKVQLdiRLghaqtvekVLLWLAEDGSL-----AGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVA 180
|
90 100
....*....|....*....|.
gi 15830258 81 ----RAKQAAEAKGVSDNMQF 97
Cdd:PLN02585 181 eaerRAKEALAALPPEVLPKF 201
|
|
| YqjQ |
COG0300 |
Short-chain dehydrogenase [General function prediction only]; |
51-152 |
6.95e-04 |
|
Short-chain dehydrogenase [General function prediction only];
Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 39.85 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 51 AGGGEGQ-TAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSdnmqfIHCAAQDvashletpvdlilfhavlewVADPR 129
Cdd:COG0300 13 ASSGIGRaLARALAARGARVVLVARDAERLEALAAELRAAGAR-----VEVVALD--------------------VTDPD 67
|
90 100
....*....|....*....|...
gi 15830258 130 SVLQTLWSVLRPGGVLSLMFYNA 152
Cdd:COG0300 68 AVAALAEAVLARFGPIDVLVNNA 90
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
47-120 |
1.32e-03 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 38.73 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830258 47 RVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSDN-MQFIHCaaqDVASHL-ETPVDLILFHA 120
Cdd:PRK14968 26 RVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRS---DLFEPFrGDKFDVILFNP 98
|
|
| Methyltransf_24 |
pfam13578 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
59-145 |
3.79e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 433324 [Multi-domain] Cd Length: 106 Bit Score: 36.13 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 59 AIKMAERGHqVILCDLSaQMIDRAKQAAEAKGVSDNMQFIHCAAQDVASHLET-PVDLILF---HAVlewvADPRSVLQT 134
Cdd:pfam13578 17 ALRDNGLGR-LTAVDPD-PGAEEAGALLRKAGLDDRVRLIVGDSREALPSLADgPIDLLFIdgdHTY----EAVLNDLEL 90
|
90
....*....|.
gi 15830258 135 LWSVLRPGGVL 145
Cdd:pfam13578 91 WLPRLAPGGVI 101
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
46-148 |
4.07e-03 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 37.40 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 46 LRVLDAGGGEGQTAIKMAER-GH-QVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHcaaQDVASHLETPV-DLILFHAVL 122
Cdd:smart00828 1 KRVLDFGCGYGSDLIDLAERhPHlQLHGYTISPEQAEVGRERIRALGLQGRIRIFY---RDSAKDPFPDTyDLVFGFEVI 77
|
90 100
....*....|....*....|....*.
gi 15830258 123 EWVADPRSVLQTLWSVLRPGGVLSLM 148
Cdd:smart00828 78 HHIKDKMDLFSNISRHLKDGGHLVLA 103
|
|
| KDSR-like_SDR_c |
cd08939 |
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ... |
48-128 |
6.94e-03 |
|
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187643 [Multi-domain] Cd Length: 239 Bit Score: 36.85 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830258 48 VLDAGGGEG---QTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSDNmQFIHCAAQDVASHLEtpVDlILFHAVLEW 124
Cdd:cd08939 4 VLITGGSSGigkALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASG-QKVSYISADLSDYEE--VE-QAFAQAVEK 79
|
....
gi 15830258 125 VADP 128
Cdd:cd08939 80 GGPP 83
|
|
| |
