|
Name |
Accession |
Description |
Interval |
E-value |
| methyl_ArsM |
NF040538 |
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ... |
42-321 |
5.74e-44 |
|
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.
Pssm-ID: 439748 Cd Length: 352 Bit Score: 155.40 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 42 YIRKSLQNVHEEVTSRYYGCGLVVPEHLENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEYHTEK 121
Cdd:NF040538 33 YDAQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 122 FGFQtpNVTFLHGQI-----------EMLAEAG-----------------------IQKESYDIVISNCVINLV--PDKQ 165
Cdd:NF040538 113 TGSA--NLRFFRASIsdlktdlelaeERLSGEScenlaswknfeqflsdsrqsnplIADNSIDLVVSNCVINLVgtTEKQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 166 KVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDLAVIAKKIGFcpprlvTANIITVGNKELER 245
Cdd:NF040538 191 NVFAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTK 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 246 VLGDCRFVSATFRLFKLPKTEPAGR--CQVVYNGGimghEKELIFDANFTFKEGEAVEVDEETAAILRNSRFAHDFLF 321
Cdd:NF040538 265 RIGSVEFYSVTVTATKPLEAVVGSGdmTTVIYRGP----WTEVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFV 338
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
60-265 |
1.66e-43 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 151.64 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 60 GCGLvvPEHLENCR----ILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQ 135
Cdd:PRK11873 65 GCGN--PTALAELKpgetVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGYT--NVEFRLGE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 136 IEMLAEAgiqKESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKD 215
Cdd:PRK11873 137 IEALPVA---DNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEE 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 216 LAVIAKKIGFCPPRLVTANIITVGN-KELERVLG-------DCRFVSATFRLFKLPKT 265
Cdd:PRK11873 214 YLAMLAEAGFVDITIQPKREYRIPDaREFLEDWGiapgrqlDGYIVSATVEATKPAAT 271
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
70-216 |
5.55e-34 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 122.91 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 70 ENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQIEMLAEAgIQKESY 149
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARE----NAQKLGFD--NVEFEQGDIEELPEL-LEDDKF 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074188857 150 DIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDL 216
Cdd:pfam13847 76 DVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
73-185 |
5.92e-22 |
|
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: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQlvgQKGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiqkESYDIV 152
Cdd:COG2226 25 RVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELAR-------ERAAEAGLNVEFVVGDAEDLPFPD---GSFDLV 91
|
90 100 110
....*....|....*....|....*....|...
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG2226 92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
73-188 |
3.55e-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: 70.92 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAYleyhteKFGFQTPNVTFLHGQIEMLAEAGIqkESYDIV 152
Cdd:cd02440 1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEAD--ESFDVI 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 2074188857 153 ISNCVIN-LVPDKQKVLREVYQVLKYGGELYFSDVYA 188
Cdd:cd02440 71 ISDPPLHhLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
68-185 |
7.01e-11 |
|
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: 61.53 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 68 HLENCRILDLGSGSGrdcYVLSQLVGQ--KGHITGIDMTKVQVEVAKAYLeyhtekfgfqTPNVTFLHGQIEMLAeagIQ 145
Cdd:TIGR02072 32 IFIPASVLDIGCGTG---YLTRALLKRfpQAEFIALDISAGMLAQAKTKL----------SENVQFICGDAEKLP---LE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2074188857 146 KESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:TIGR02072 96 DSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| methyl_ArsM |
NF040538 |
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ... |
42-321 |
5.74e-44 |
|
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.
Pssm-ID: 439748 Cd Length: 352 Bit Score: 155.40 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 42 YIRKSLQNVHEEVTSRYYGCGLVVPEHLENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEYHTEK 121
Cdd:NF040538 33 YDAQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 122 FGFQtpNVTFLHGQI-----------EMLAEAG-----------------------IQKESYDIVISNCVINLV--PDKQ 165
Cdd:NF040538 113 TGSA--NLRFFRASIsdlktdlelaeERLSGEScenlaswknfeqflsdsrqsnplIADNSIDLVVSNCVINLVgtTEKQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 166 KVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDLAVIAKKIGFcpprlvTANIITVGNKELER 245
Cdd:NF040538 191 NVFAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTK 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 246 VLGDCRFVSATFRLFKLPKTEPAGR--CQVVYNGGimghEKELIFDANFTFKEGEAVEVDEETAAILRNSRFAHDFLF 321
Cdd:NF040538 265 RIGSVEFYSVTVTATKPLEAVVGSGdmTTVIYRGP----WTEVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFV 338
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
60-265 |
1.66e-43 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 151.64 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 60 GCGLvvPEHLENCR----ILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQ 135
Cdd:PRK11873 65 GCGN--PTALAELKpgetVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGYT--NVEFRLGE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 136 IEMLAEAgiqKESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKD 215
Cdd:PRK11873 137 IEALPVA---DNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEE 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 216 LAVIAKKIGFCPPRLVTANIITVGN-KELERVLG-------DCRFVSATFRLFKLPKT 265
Cdd:PRK11873 214 YLAMLAEAGFVDITIQPKREYRIPDaREFLEDWGiapgrqlDGYIVSATVEATKPAAT 271
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
70-216 |
5.55e-34 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 122.91 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 70 ENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQIEMLAEAgIQKESY 149
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARE----NAQKLGFD--NVEFEQGDIEELPEL-LEDDKF 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074188857 150 DIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDL 216
Cdd:pfam13847 76 DVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
73-185 |
5.92e-22 |
|
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: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQlvgQKGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiqkESYDIV 152
Cdd:COG2226 25 RVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELAR-------ERAAEAGLNVEFVVGDAEDLPFPD---GSFDLV 91
|
90 100 110
....*....|....*....|....*....|...
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG2226 92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
74-179 |
4.67e-21 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 86.46 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 74 ILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiqkESYDIVI 153
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERAR-------ERAAEAGLNVEFVQGDAEDLPFPD---GSFDLVV 68
|
90 100
....*....|....*....|....*...
gi 2074188857 154 SNCVINLV--PDKQKVLREVYQVLKYGG 179
Cdd:pfam13649 69 SSGVLHHLpdPDLEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
69-185 |
2.65e-19 |
|
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: 82.76 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 69 LENCRILDLGSGSGRDCYVLSQLvgqkGH-ITGIDMTKVQVEVAKAYLEYHtekfgfqtpNVTFLHGQIEMLAEAGiqkE 147
Cdd:COG2227 23 PAGGRVLDVGCGTGRLALALARR----GAdVTGVDISPEALEIARERAAEL---------NVDFVQGDLEDLPLED---G 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 2074188857 148 SYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG2227 87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
75-183 |
1.33e-15 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 71.54 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 75 LDLGSGSGRDCYVLSQLVGQkghITGIDMTKVQVEVAKAYLeyhtekfgfQTPNVTFLHGQIEMLaeaGIQKESYDIVIS 154
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKA---------PREGLTFVVGDAEDL---PFPDNSFDLVLS 65
|
90 100
....*....|....*....|....*....
gi 2074188857 155 NCVINLVPDKQKVLREVYQVLKYGGELYF 183
Cdd:pfam08241 66 SEVLHHVEDPERALREIARVLKPGGILII 94
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
73-188 |
3.55e-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: 70.92 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAYleyhteKFGFQTPNVTFLHGQIEMLAEAGIqkESYDIV 152
Cdd:cd02440 1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEAD--ESFDVI 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 2074188857 153 ISNCVIN-LVPDKQKVLREVYQVLKYGGELYFSDVYA 188
Cdd:cd02440 71 ISDPPLHhLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
73-185 |
3.64e-15 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 70.62 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGQkGHITGIDMTKVQVEVAKAYLeyhtekfgfqtPNVTFLHGQIEMLAEAgiqkESYDIV 152
Cdd:COG4106 4 RVLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARL-----------PNVRFVVADLRDLDPP----EPFDLV 67
|
90 100 110
....*....|....*....|....*....|...
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG4106 68 VSNAALHWLPDHAALLARLAAALAPGGVLAVQV 100
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
70-199 |
1.32e-13 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 68.79 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 70 ENCRILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAyleyHTEKFGFqtPNVTFLHGQIEMLAEagIQKESY 149
Cdd:COG0500 26 KGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARA----RAAKAGL--GNVEFLVADLAELDP--LPAESF 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2074188857 150 DIVISNCVINLVP--DKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSH 199
Cdd:COG0500 96 DLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLSASDAAAALSLARLLL 147
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
73-179 |
5.10e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 64.96 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLaeaGIQKESYDIV 152
Cdd:PRK08317 22 RVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAK-------ERAAGLGPNVEFVRGDADGL---PFPDGSFDAV 91
|
90 100
....*....|....*....|....*..
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGG 179
Cdd:PRK08317 92 RSDRVLQHLEDPARALAEIARVLRPGG 118
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
73-184 |
1.16e-11 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 62.71 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVgqkGHITGIDMTKVQVEVAKAYLEYhtekfgfqtpnVTFLHGQIEMLAEAGiqkESYDIV 152
Cdd:COG4976 49 RVLDLGCGTGLLGEALRPRG---YRLTGVDLSEEMLAKAREKGVY-----------DRLLVADLADLAEPD---GRFDLI 111
|
90 100 110
....*....|....*....|....*....|..
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFS 184
Cdd:COG4976 112 VAADVLTYLGDLAAVFAGVARALKPGGLFIFS 143
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
68-185 |
7.01e-11 |
|
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: 61.53 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 68 HLENCRILDLGSGSGrdcYVLSQLVGQ--KGHITGIDMTKVQVEVAKAYLeyhtekfgfqTPNVTFLHGQIEMLAeagIQ 145
Cdd:TIGR02072 32 IFIPASVLDIGCGTG---YLTRALLKRfpQAEFIALDISAGMLAQAKTKL----------SENVQFICGDAEKLP---LE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2074188857 146 KESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:TIGR02072 96 DSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
73-181 |
8.73e-11 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 61.32 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKayleyhtEKF--GFQTPNVTFLHGQIEMLAeagIQKESYD 150
Cdd:PRK00216 54 KVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGR-------EKLrdLGLSGNVEFVQGDAEALP---FPDNSFD 123
|
90 100 110
....*....|....*....|....*....|..
gi 2074188857 151 IV-ISNCVINlVPDKQKVLREVYQVLKYGGEL 181
Cdd:PRK00216 124 AVtIAFGLRN-VPDIDKALREMYRVLKPGGRL 154
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
69-182 |
9.12e-11 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 61.30 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 69 LENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEyhteKFGFQtpNVTFLHGQIEMLAEagiQKES 148
Cdd:pfam01209 41 KRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAK----EEGKY--NIEFLQGNAEELPF---EDDS 111
|
90 100 110
....*....|....*....|....*....|....
gi 2074188857 149 YDIVISNCVINLVPDKQKVLREVYQVLKYGGELY 182
Cdd:pfam01209 112 FDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVV 145
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
75-181 |
2.53e-10 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 56.99 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 75 LDLGSGSGRDCYVLSQLVGQkGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiQKESYDIVIS 154
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPG-LEYTGLDISPAALEAAR-------ERLAALGLLNAVRVELFQLDLGEL-DPGSFDVVVA 71
|
90 100
....*....|....*....|....*..
gi 2074188857 155 NCVINLVPDKQKVLREVYQVLKYGGEL 181
Cdd:pfam08242 72 SNVLHHLADPRAVLRNIRRLLKPGGVL 98
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
73-185 |
6.59e-08 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 51.47 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAYLeyhtEKFGFqTPNVTFLHGQIEMLAEAGiqkeSYDIV 152
Cdd:COG2230 54 RVLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARERA----AEAGL-ADRVEVRLADYRDLPADG----QFDAI 122
|
90 100 110
....*....|....*....|....*....|....*
gi 2074188857 153 ISNCVINLVPDKQ--KVLREVYQVLKYGGELYFSD 185
Cdd:COG2230 123 VSIGMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
66-225 |
2.65e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 47.04 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 66 PEHLENCRILDLGSGSGRDCyvlsQLVGQKG-HITGIDMTKVQVEVAKAYleyhtekfgfqtpNVTFLHGQIEMLAEAGi 144
Cdd:pfam13489 18 PKLPSPGRVLDFGCGTGIFL----RLLRAQGfSVTGVDPSPIAIERALLN-------------VRFDQFDEQEAAVPAG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 145 qkeSYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKsHKVLWGECLGGALYW--KDLAVIAKK 222
Cdd:pfam13489 80 ---KFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLL-EWPYLRPRNGHISLFsaRSLKRLLEE 155
|
...
gi 2074188857 223 IGF 225
Cdd:pfam13489 156 AGF 158
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
73-179 |
3.84e-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: 47.46 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLeyhtEKFGFqTPNVTFLHGQIemlaEAGIQKESYDIV 152
Cdd:COG2519 94 RVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNL----ERFGL-PDNVELKLGDI----REGIDEGDVDAV 164
|
90 100
....*....|....*....|....*...
gi 2074188857 153 IsncvinL-VPDKQKVLREVYQVLKYGG 179
Cdd:COG2519 165 F------LdMPDPWEALEAVAKALKPGG 186
|
|
| PrmA |
pfam06325 |
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
69-184 |
2.04e-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: 42.64 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 69 LENCRILDLGSGSGrdcyVLS---QLVGQKgHITGIDMTKVQVEVAKAYLEYHtekfgfqtpNVtflHGQIEMLAEAGIQ 145
Cdd:pfam06325 160 KPGESVLDVGCGSG----ILAiaaLKLGAK-KVVGVDIDPVAVRAAKENAELN---------GV---EARLEVYLPGDLP 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2074188857 146 KESYDIVISNC----VINLVPDkqkvlreVYQVLKYGGELYFS 184
Cdd:pfam06325 223 KEKADVVVANIladpLIELAPD-------IYALVKPGGYLILS 258
|
|
| PLN02233 |
PLN02233 |
ubiquinone biosynthesis methyltransferase |
73-178 |
2.93e-04 |
|
ubiquinone biosynthesis methyltransferase
Pssm-ID: 177877 [Multi-domain] Cd Length: 261 Bit Score: 42.19 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYleyhtekfgfQTPNVTFLHGQIEMlaeagIQKESYDIV 152
Cdd:PLN02233 76 RVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAASR----------QELKAKSCYKNIEW-----IEGDATDLP 140
|
90 100 110
....*....|....*....|....*....|....*
gi 2074188857 153 ISNCVINLVP---------DKQKVLREVYQVLKYG 178
Cdd:PLN02233 141 FDDCYFDAITmgyglrnvvDRLKAMQEMYRVLKPG 175
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
65-183 |
4.66e-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: 40.94 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 65 VPEHLENcRILDLGSGSGrdcyVLS---QLVGQKGHITGIDMTKVQVEVAKAYLEYHtekfgfQTPNVTFLHGQiemlAE 141
Cdd:COG2813 45 LPEPLGG-RVLDLGCGYG----VIGlalAKRNPEARVTLVDVNARAVELARANAAAN------GLENVEVLWSD----GL 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2074188857 142 AGIQKESYDIVISNCVI--NLVPDK---QKVLREVYQVLKYGGELYF 183
Cdd:COG2813 110 SGVPDGSFDLILSNPPFhaGRAVDKevaHALIADAARHLRPGGELWL 156
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
73-183 |
7.22e-04 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 40.51 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 73 RILDLGSGSGrdcyVLSQLVGQK---GHITGidmtkvqVEVAKAYLEYHTEKF---GFQtPNVTFLHGQIEMLAEAgIQK 146
Cdd:COG4123 40 RVLDLGTGTG----VIALMLAQRspgARITG-------VEIQPEAAELARRNValnGLE-DRITVIHGDLKEFAAE-LPP 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 147 ESYDIVISN--------CVINlvPDKQK-------------VLREVYQVLKYGGELYF 183
Cdd:COG4123 107 GSFDLVVSNppyfkagsGRKS--PDEARaiarhedaltledLIRAAARLLKPGGRFAL 162
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
63-155 |
2.06e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 39.37 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 63 LVVPEHLENCRILDLGSGSG----------RDCYVlsqlvgqkghiTGIDMTKVQVEVAKAYLEYHTEKfgfqtpNVTFL 132
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGaialalakerPDAEV-----------TAVDISPEALAVARRNAKHGLGA------RVEFL 163
|
90 100
....*....|....*....|...
gi 2074188857 133 HGqiEMLaeAGIQKESYDIVISN 155
Cdd:PRK09328 164 QG--DWF--EPLPGGRFDLIVSN 182
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
70-189 |
2.59e-03 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 39.18 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 70 ENCRILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKaylEYHTEKfgfqtpnvtflhGQIEMLAEAGIQKE-- 147
Cdd:PTZ00098 52 ENSKVLDIGSGLGGGCKYINEKYG--AHVHGVDICEKMVNIAK---LRNSDK------------NKIEFEANDILKKDfp 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2074188857 148 --SYDIVISNCVINLVP--DKQKVLREVYQVLKYGGELYFSDVYAS 189
Cdd:PTZ00098 115 enTFDMIYSRDAILHLSyaDKKKLFEKCYKWLKPNGILLITDYCAD 160
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
67-155 |
3.80e-03 |
|
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]
Pssm-ID: 274634 [Multi-domain] Cd Length: 250 Bit Score: 38.60 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 67 EHLENC-RILDLGSGSGrdCYVLSQLVGQKG-HITGIDMTKVQVEVAKAYLEYHtekfgfQTPNVTFLHGQiemLAEAgI 144
Cdd:TIGR03534 82 ERLKKGpRVLDLGTGSG--AIALALAKERPDaRVTAVDISPEALAVARKNARRL------GLENVEFLQGD---WFEP-L 149
|
90
....*....|.
gi 2074188857 145 QKESYDIVISN 155
Cdd:TIGR03534 150 PSGKFDLIVSN 160
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
69-184 |
3.87e-03 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 38.62 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 69 LENCRILDLGSGSGrdcyVLS---QLVGQKgHITGIDMTKVQVEVAKAyleyhtekfgfqtpNVTF--LHGQIEMLAEAG 143
Cdd:COG2264 147 KPGKTVLDVGCGSG----ILAiaaAKLGAK-RVLAVDIDPVAVEAARE--------------NAELngVEDRIEVVLGDL 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2074188857 144 IQKESYDIVISNcvIN------LVPDkqkvlreVYQVLKYGGELYFS 184
Cdd:COG2264 208 LEDGPYDLVVAN--ILanplieLAPD-------LAALLKPGGYLILS 245
|
|
| PRK12335 |
PRK12335 |
tellurite resistance protein TehB; Provisional |
50-157 |
6.15e-03 |
|
tellurite resistance protein TehB; Provisional
Pssm-ID: 183450 [Multi-domain] Cd Length: 287 Bit Score: 38.00 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 50 VHEEVtsryygcgLVVPEHLENCRILDLGSGSGRDCYVLSqlvgQKGH-ITGIDmtkvQVEVAKAYLEYHTEKFGFQTPn 128
Cdd:PRK12335 108 THSEV--------LEAVQTVKPGKALDLGCGQGRNSLYLA----LLGFdVTAVD----INQQSLENLQEIAEKENLNIR- 170
|
90 100
....*....|....*....|....*....
gi 2074188857 129 vTFLHGqiemLAEAGIQkESYDIVISNCV 157
Cdd:PRK12335 171 -TGLYD----INSASIQ-EEYDFILSTVV 193
|
|
|