|
Name |
Accession |
Description |
Interval |
E-value |
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
39-151 |
1.44e-28 |
|
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: 103.56 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 39 IDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:COG2227 14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAREraaELNVDFVQGDLEDLPLEDGSFDLVI 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 814585857 116 ANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPR 151
Cdd:COG2227 93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
54-143 |
6.82e-24 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 90.70 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 54 VLDFGCGPGRDLQTFTRM-GHIAVGLDGSERFAQMARE-----DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPKQE 127
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERAREraaeaGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 814585857 128 LPRVLKQLHGALKPGG 143
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
53-146 |
5.97e-15 |
|
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: 67.84 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 53 TVLDFGCGPGRDLQTF-TRMGHIAVGLDGSERFAQMARE------DSGCEVLQQDFLKLDL-PNARFDGIFANAVLFHIP 124
Cdd:cd02440 1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPeADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|..
gi 814585857 125 kQELPRVLKQLHGALKPGGVLF 146
Cdd:cd02440 81 -EDLARFLEEARRLLKPGGVLV 101
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
40-185 |
1.22e-10 |
|
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: 58.84 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 40 DALLRHIQGAAPFT---VLDFGCGPG---RDL-QTFTRMGHIAvgLDGSERFAQMAREDSGCEV--LQQDFLKLDLPNAR 110
Cdd:TIGR02072 21 KRLLALLKEKGIFIpasVLDIGCGTGyltRALlKRFPQAEFIA--LDISAGMLAQAKTKLSENVqfICGDAEKLPLEDSS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 111 FDGIFANAVL--FHipkqELPRVLKQLHGALKPGGVL-FSSNPRGDNRE-----GWNGPRYGSYHDLEAWqsLLTAAGFV 182
Cdd:TIGR02072 99 FDLIVSNLALqwCD----DLSQALSELARVLKPGGLLaFSTFGPGTLHElrqsfGQHGLRYLSLDELKAL--LKNSFELL 172
|
...
gi 814585857 183 ELE 185
Cdd:TIGR02072 173 TLE 175
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
40-143 |
3.24e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 57.64 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 40 DALLRHIQGAAPFTVLDFGCGPGRDLQTFTRM----GHiAVGLDGSER---FAQMAREDSG--CEVLQQDFLKLDLPNAR 110
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSEAmlaLAKERAAGLGpnVEFVRGDADGLPFPDGS 87
|
90 100 110
....*....|....*....|....*....|...
gi 814585857 111 FDGIFANAVLFHIPkqELPRVLKQLHGALKPGG 143
Cdd:PRK08317 88 FDAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
39-117 |
5.44e-04 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 39.03 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 39 IDALLRHIQGAAPFTVLDFGCGPGRdlqtFT----RMGH--IAVGLDgsERFAQMARE----DSGCEVLQQDFLKLDLPN 108
Cdd:smart00650 2 IDKIVRAANLRPGDTVLEIGPGKGA----LTeellERAKrvTAIEID--PRLAPRLREkfaaADNLTVIHGDALKFDLPK 75
|
....*....
gi 814585857 109 ARFDGIFAN 117
Cdd:smart00650 76 LQPYKVVGN 84
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
39-151 |
1.44e-28 |
|
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: 103.56 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 39 IDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:COG2227 14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAREraaELNVDFVQGDLEDLPLEDGSFDLVI 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 814585857 116 ANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPR 151
Cdd:COG2227 93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
10-207 |
6.85e-27 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 101.23 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 10 QITATTLDHYNSVAEDFregtrDHDVSQN---------IDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDG 80
Cdd:COG4976 2 ALDAYVEALFDQYADSY-----DAALVEDlgyeapallAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 81 SERFAQMARE-DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPRGDNREgwn 159
Cdd:COG4976 77 SEEMLAKAREkGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIFSVEDADGSG--- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 814585857 160 gpRYgsYHDLEAWQSLLTAAGFvelehyyrpaglpreQQPWLASVWRK 207
Cdd:COG4976 152 --RY--AHSLDYVRDLLAAAGF---------------EVPGLLVVARK 180
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
54-143 |
6.82e-24 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 90.70 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 54 VLDFGCGPGRDLQTFTRM-GHIAVGLDGSERFAQMARE-----DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPKQE 127
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERAREraaeaGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 814585857 128 LPRVLKQLHGALKPGG 143
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
19-181 |
2.85e-23 |
|
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: 90.44 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 19 YNSVAEDFREGtrdhdvsqniDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE-----DSG 93
Cdd:COG2226 1 FDRVAARYDGR----------EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAREraaeaGLN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 94 CEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPrgdnregwngprygSYHDLEAWQ 173
Cdd:COG2226 71 VEFVVGDAEDLPFPDGSFDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDF--------------SPPDLAELE 134
|
....*...
gi 814585857 174 SLLTAAGF 181
Cdd:COG2226 135 ELLAEAGF 142
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
50-146 |
3.43e-23 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 89.11 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 50 APFTVLDFGCGPGRDLQTFTRM--GHIAVGLDGSERFAQMARE-DSGCEVLQQDFLKLDlPNARFDGIFANAVLFHIPkq 126
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARArLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLP-- 77
|
90 100
....*....|....*....|
gi 814585857 127 ELPRVLKQLHGALKPGGVLF 146
Cdd:COG4106 78 DHAALLARLAAALAPGGVLA 97
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
55-146 |
5.97e-20 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 80.40 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 55 LDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRV 131
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkapREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVE--DPERA 78
|
90
....*....|....*
gi 814585857 132 LKQLHGALKPGGVLF 146
Cdd:pfam08241 79 LREIARVLKPGGILI 93
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
50-182 |
4.56e-19 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 81.12 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 50 APFTVLDFGCGPGRDLQTFTRMGHIAV-GLDGSERFAQMARED------SGCEVLQQDFLKL-DLPNARFDGIFANAVLF 121
Cdd:COG0500 26 KGGRVLDLGCGTGRNLLALAARFGGRViGIDLSPEAIALARARaakaglGNVEFLVADLAELdPLPAESFDLVVAFGVLH 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585857 122 HIPKQELPRVLKQLHGALKPGGVLF----SSNPRGDNREGWNGPRYGSYHDLEAWQSLLTAAGFV 182
Cdd:COG0500 106 HLPPEEREALLRELARALKPGGVLLlsasDAAAALSLARLLLLATASLLELLLLLRLLALELYLR 170
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
17-146 |
1.16e-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: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 17 DHYNSVAEDFRE-------------GTRDHDVSQNIDALLRHIQGAAPF----TVLDFGCGPGRDLQTFTRM-GHIAVGL 78
Cdd:COG2230 1 HHYDLGNDFYRLfldptmtyscayfEDPDDTLEEAQEAKLDLILRKLGLkpgmRVLDIGCGWGGLALYLARRyGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585857 79 DGSERFAQMARE-------DSGCEVLQQDFLKLDlPNARFDGIFANAVLFHIPKQELPRVLKQLHGALKPGGVLF 146
Cdd:COG2230 81 TLSPEQLEYAREraaeaglADRVEVRLADYRDLP-ADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
53-146 |
5.97e-15 |
|
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: 67.84 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 53 TVLDFGCGPGRDLQTF-TRMGHIAVGLDGSERFAQMARE------DSGCEVLQQDFLKLDL-PNARFDGIFANAVLFHIP 124
Cdd:cd02440 1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPeADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|..
gi 814585857 125 kQELPRVLKQLHGALKPGGVLF 146
Cdd:cd02440 81 -EDLARFLEEARRLLKPGGVLV 101
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
53-181 |
1.29e-12 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 62.83 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 53 TVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMAREDSgcEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRVL 132
Cdd:pfam13489 25 RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNV--RFDQFDEQEAAVPAGKFDVIVAREVLEHVP--DPPALL 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585857 133 KQLHGALKPGGVLFSSNPRGDNREG-----WNGPRY----GSYHDLEAWQSLLTAAGF 181
Cdd:pfam13489 101 RQIAALLKPGGLLLLSTPLASDEADrllleWPYLRPrnghISLFSARSLKRLLEEAGF 158
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
53-152 |
1.14e-11 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 60.12 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 53 TVLDFGCGPGRDL-QTFTRMGHIA--VGLDGSERFAQMARED------SGCEVLQQDFLKLD--LPNARFDGIFANAVLF 121
Cdd:pfam13847 6 RVLDLGCGTGHLSfELAEELGPNAevVGIDISEEAIEKARENaqklgfDNVEFEQGDIEELPelLEDDKFDVVISNCVLN 85
|
90 100 110
....*....|....*....|....*....|.
gi 814585857 122 HIPkqELPRVLKQLHGALKPGGVLFSSNPRG 152
Cdd:pfam13847 86 HIP--DPDKVLQEILRVLKPGGRLIISDPDS 114
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
55-145 |
1.03e-10 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 56.22 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 55 LDFGCGPGRDLQTFTRMGHIA--VGLDGSERFAQMARE----DSGCEVLQQDFLKLDLPN---ARFDGIFANAVLFHIPk 125
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARErlaaLGLLNAVRVELFQLDLGEldpGSFDVVVASNVLHHLA- 79
|
90 100
....*....|....*....|
gi 814585857 126 qELPRVLKQLHGALKPGGVL 145
Cdd:pfam08242 80 -DPRAVLRNIRRLLKPGGVL 98
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
40-185 |
1.22e-10 |
|
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: 58.84 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 40 DALLRHIQGAAPFT---VLDFGCGPG---RDL-QTFTRMGHIAvgLDGSERFAQMAREDSGCEV--LQQDFLKLDLPNAR 110
Cdd:TIGR02072 21 KRLLALLKEKGIFIpasVLDIGCGTGyltRALlKRFPQAEFIA--LDISAGMLAQAKTKLSENVqfICGDAEKLPLEDSS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 111 FDGIFANAVL--FHipkqELPRVLKQLHGALKPGGVL-FSSNPRGDNRE-----GWNGPRYGSYHDLEAWqsLLTAAGFV 182
Cdd:TIGR02072 99 FDLIVSNLALqwCD----DLSQALSELARVLKPGGLLaFSTFGPGTLHElrqsfGQHGLRYLSLDELKAL--LKNSFELL 172
|
...
gi 814585857 183 ELE 185
Cdd:TIGR02072 173 TLE 175
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
40-143 |
3.24e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 57.64 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 40 DALLRHIQGAAPFTVLDFGCGPGRDLQTFTRM----GHiAVGLDGSER---FAQMAREDSG--CEVLQQDFLKLDLPNAR 110
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSEAmlaLAKERAAGLGpnVEFVRGDADGLPFPDGS 87
|
90 100 110
....*....|....*....|....*....|...
gi 814585857 111 FDGIFANAVLFHIPkqELPRVLKQLHGALKPGG 143
Cdd:PRK08317 88 FDAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
|
|
| PRK01683 |
PRK01683 |
trans-aconitate 2-methyltransferase; Provisional |
42-145 |
3.19e-08 |
|
trans-aconitate 2-methyltransferase; Provisional
Pssm-ID: 234970 Cd Length: 258 Bit Score: 52.25 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 42 LLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIA--VGLDGSERFAQMAREdsgcEVLQQDFLKLDL----PNARFDGIF 115
Cdd:PRK01683 23 LLARVPLENPRYVVDLGCGPGNSTELLVERWPAAriTGIDSSPAMLAEARS----RLPDCQFVEADIaswqPPQALDLIF 98
|
90 100 110
....*....|....*....|....*....|
gi 814585857 116 ANAVLFHIPKQElpRVLKQLHGALKPGGVL 145
Cdd:PRK01683 99 ANASLQWLPDHL--ELFPRLVSLLAPGGVL 126
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
54-184 |
8.59e-07 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 48.59 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 54 VLDFGCG-PGRDLQTFTRMGHIAVGLDGSERFAQMAREDS---GCEVLQQ--DFLKLDLPNARFDGIFANAVLFHIpkQE 127
Cdd:PLN02336 270 VLDVGCGiGGGDFYMAENFDVHVVGIDLSVNMISFALERAigrKCSVEFEvaDCTKKTYPDNSFDVIYSRDTILHI--QD 347
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585857 128 LPRVLKQLHGALKPGG-VLFSSNPRgdnREGWNGPRYGSY--------HDLEAWQSLLTAAGFVEL 184
Cdd:PLN02336 348 KPALFRSFFKWLKPGGkVLISDYCR---SPGTPSPEFAEYikqrgydlHDVQAYGQMLKDAGFDDV 410
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
42-159 |
1.04e-06 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 48.04 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 42 LLRHIQGAAPFTVLDFGCGPGRDLQTFT-RMGHIAVGLDGSERFAQMARE----DSGCEVLQQDFLKLDLPNARFDGIFA 116
Cdd:PTZ00098 44 ILSDIELNENSKVLDIGSGLGGGCKYINeKYGAHVHGVDICEKMVNIAKLrnsdKNKIEFEANDILKKDFPENTFDMIYS 123
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 814585857 117 NAVLFHIPKQELPRVLKQLHGALKPGGVLFSSNPRGDNREGWN 159
Cdd:PTZ00098 124 RDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADKIENWD 166
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
37-145 |
1.40e-06 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 47.45 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 37 QNIDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE-DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:PRK10258 29 QSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQkDAADHYLAGDIESLPLATATFDLAW 108
|
90 100 110
....*....|....*....|....*....|.
gi 814585857 116 AN-AVLFHipkQELPRVLKQLHGALKPGGVL 145
Cdd:PRK10258 109 SNlAVQWC---GNLSTALRELYRVVRPGGVV 136
|
|
| COG4627 |
COG4627 |
Predicted SAM-depedendent methyltransferase [General function prediction only]; |
103-145 |
3.65e-06 |
|
Predicted SAM-depedendent methyltransferase [General function prediction only];
Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 45.24 E-value: 3.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 814585857 103 KLDLPNARFDGIFANAVLFHIPKQELPRVLKQLHGALKPGGVL 145
Cdd:COG4627 39 PLPFPDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGIL 81
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
53-189 |
3.88e-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: 45.32 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 53 TVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE------DSGCEVLQQDFLKLDLPNARFDGIFANA-------V 119
Cdd:COG1041 29 TVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGAREnlehygYEDADVIRGDARDLPLADESVDAIVTDPpygrsskI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585857 120 LFHIPKQELPRVLKQLHGALKPGGVL-FSSNPRgdnregwngprygsyhdleaWQSLLTAAGFVELEHYYR 189
Cdd:COG1041 109 SGEELLELYEKALEEAARVLKPGGRVvIVTPRD--------------------IDELLEEAGFKVLERHEQ 159
|
|
| PRK15068 |
PRK15068 |
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB; |
40-146 |
4.24e-05 |
|
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
Pssm-ID: 237898 Cd Length: 322 Bit Score: 43.31 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 40 DALLRHIQGAAPFTVLDFGCGPGRDLqtFtRM----GHIAVGLDGSERF-------AQMAREDsgcevLQQDFLKL---D 105
Cdd:PRK15068 112 DRVLPHLSPLKGRTVLDVGCGNGYHM--W-RMlgagAKLVVGIDPSQLFlcqfeavRKLLGND-----QRAHLLPLgieQ 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 814585857 106 LP-NARFDGIFANAVLFHipkqelpR-----VLKQLHGALKPGGVLF 146
Cdd:PRK15068 184 LPaLKAFDTVFSMGVLYH-------RrspldHLKQLKDQLVPGGELV 223
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
53-184 |
1.51e-04 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 41.47 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 53 TVLDFGCGPGRD-LQTFTRMGHI--AVGLDGSERFAQMARED------SGCEVLQQDFLKLDLPNARFDGIFANAVLFHI 123
Cdd:PRK11873 80 TVLDLGSGGGFDcFLAARRVGPTgkVIGVDMTPEMLAKARANarkagyTNVEFRLGEIEALPVADNSVDVIISNCVINLS 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 124 PKQElpRVLKQLHGALKPGG-------VLFSSNPRG--DNREGWNGPRYGSYhDLEAWQSLLTAAGFVEL 184
Cdd:PRK11873 160 PDKE--RVFKEAFRVLKPGGrfaisdvVLRGELPEEirNDAELYAGCVAGAL-QEEEYLAMLAEAGFVDI 226
|
|
| PrmA |
pfam06325 |
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
29-148 |
1.52e-04 |
|
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.
Pssm-ID: 428888 [Multi-domain] Cd Length: 294 Bit Score: 41.48 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 29 GTRDHDVSQ-NIDALLRHIQGAApfTVLDFGCGPGrdlqtftrmghI------------AVGLDGSE---RFAQMAREDS 92
Cdd:pfam06325 141 GTGTHPTTKlCLEALERLVKPGE--SVLDVGCGSG-----------IlaiaalklgakkVVGVDIDPvavRAAKENAELN 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585857 93 GCEVLQQDFLKLDLPNARFDGIFANaVLFHIpkqeLPRVLKQLHGALKPGGVLFSS 148
Cdd:pfam06325 208 GVEARLEVYLPGDLPKEKADVVVAN-ILADP----LIELAPDIYALVKPGGYLILS 258
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
28-146 |
2.96e-04 |
|
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: 40.17 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 28 EGTRdhdvsqnidALLRHIQGAAPFTVLDFGCG------------PGRDLqtftrmghiaVGLDGSERFAQMARE----- 90
Cdd:COG2813 36 IGTR---------LLLEHLPEPLGGRVLDLGCGygviglalakrnPEARV----------TLVDVNARAVELARAnaaan 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585857 91 -DSGCEVLQQDFLKlDLPNARFDGIFANAVlFHIPKQELPRVLKQL----HGALKPGGVLF 146
Cdd:COG2813 97 gLENVEVLWSDGLS-GVPDGSFDLILSNPP-FHAGRAVDKEVAHALiadaARHLRPGGELW 155
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
39-117 |
5.44e-04 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 39.03 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 39 IDALLRHIQGAAPFTVLDFGCGPGRdlqtFT----RMGH--IAVGLDgsERFAQMARE----DSGCEVLQQDFLKLDLPN 108
Cdd:smart00650 2 IDKIVRAANLRPGDTVLEIGPGKGA----LTeellERAKrvTAIEID--PRLAPRLREkfaaADNLTVIHGDALKFDLPK 75
|
....*....
gi 814585857 109 ARFDGIFAN 117
Cdd:smart00650 76 LQPYKVVGN 84
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
39-195 |
9.44e-04 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 38.99 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 39 IDALLRHIQGAAPFTVLDFGCGPG----------RDLQtftrmghiAVGLDGSERFAQMARE------DSGCEVLQQDFL 102
Cdd:PRK09328 97 VEWALEALLLKEPLRVLDLGTGSGaialalakerPDAE--------VTAVDISPEALAVARRnakhglGARVEFLQGDWF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 103 KlDLPNARFDGIFANA--------------VLFHIPKQEL----------PRVLKQLHGALKPGGVLFSsnprgdnrE-G 157
Cdd:PRK09328 169 E-PLPGGRFDLIVSNPpyipeadihllqpeVRDHEPHLALfggedgldfyRRIIEQAPRYLKPGGWLLL--------EiG 239
|
170 180 190
....*....|....*....|....*....|....*...
gi 814585857 158 WNGprygsyhdLEAWQSLLTAAGFVELEHYYRPAGLPR 195
Cdd:PRK09328 240 YDQ--------GEAVRALLAAAGFADVETRKDLAGRDR 269
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
42-146 |
3.15e-03 |
|
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: 36.80 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 42 LLRHIQGAAPFTVLDFGCGPGR-DLQTFTRMGHIAV-GLDGSERFAQMARED------SGCEVLQQDFLKlDLPNARFDG 113
Cdd:pfam05175 23 LLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELtMVDINARALESARENlaanglENGEVVASDVYS-GVEDGKFDL 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 814585857 114 IFANAVlFHIPKQELP----RVLKQLHGALKPGGVLF 146
Cdd:pfam05175 102 IISNPP-FHAGLATTYnvaqRFIADAKRHLRPGGELW 137
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
101-146 |
4.33e-03 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 37.27 E-value: 4.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 814585857 101 FLKLDL-----PNARFDGIFANAVL--FHIPKQElpRVLKQLHGALKPGGVLF 146
Cdd:smart00138 189 FAKHNLlaespPLGDFDLIFCRNVLiyFDEPTQR--KLLNRFAEALKPGGYLF 239
|
|
| PRK11036 |
PRK11036 |
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
35-145 |
4.44e-03 |
|
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
Pssm-ID: 182918 Cd Length: 255 Bit Score: 36.87 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 35 VSQNIDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMAR---EDSGceVLQQ-DFLK------- 103
Cdd:PRK11036 30 LWQDLDRLLAEL-PPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKqaaEAKG--VSDNmQFIHcaaqdia 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 814585857 104 --LDLPnarfdgifANAVLFHI-------PKQelprVLKQLHGALKPGGVL 145
Cdd:PRK11036 107 qhLETP--------VDLILFHAvlewvadPKS----VLQTLWSVLRPGGAL 145
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
54-185 |
5.51e-03 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 36.63 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 54 VLDFGCGPGRDLQTF-TRMGHIA-VGLDGSERFAQMARE-------DSGCEVLQQDFLKLDLPnARFDGIFANAVLFHIP 124
Cdd:smart00828 3 VLDFGCGYGSDLIDLaERHPHLQlHGYTISPEQAEVGREriralglQGRIRIFYRDSAKDPFP-DTYDLVFGFEVIHHIK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585857 125 KQELprVLKQLHGALKPGGVLFSSNPRGDNREGWNGPRYGSYH-DLEAWQSLLTAAGFVELE 185
Cdd:smart00828 82 DKMD--LFSNISRHLKDGGHLVLADFIANLLSAIEHEETTSYLvTREEWAELLARNNLRVVE 141
|
|
| TPMT |
pfam05724 |
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ... |
33-143 |
5.65e-03 |
|
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: 36.64 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 33 HDVSQNIDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSE-----------------RFAQMAREDSG-C 94
Cdd:pfam05724 20 EGVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEISElavekffaeaglsppitELSGFKEYSSGnI 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 814585857 95 EVLQQDFLKLDLPN-ARFDGIFANAVLFHIPKQELPRVLKQLHGALKPGG 143
Cdd:pfam05724 100 SLYCGDFFTLPREElGKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGG 149
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
98-146 |
8.50e-03 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 36.29 E-value: 8.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 814585857 98 QQDFLKLDLPNARFDGIF-ANaVL--FHIPKQElpRVLKQLHGALKPGGVLF 146
Cdd:COG1352 194 QHNLLDDPPPFGRFDLIFcRN-VLiyFDPELQR--RVLRRFHDSLAPGGYLF 242
|
|
|