|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
30-127 |
2.55e-24 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 91.57 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 30 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRQLQFERFVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQ 108
Cdd:pfam08241 1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75
|
90
....*....|....*....
gi 568993321 109 EKILREVCRVLKPGGAFYF 127
Cdd:pfam08241 76 ERALREIARVLKPGGILII 94
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
19-138 |
3.25e-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: 90.05 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 19 EFAGPSGKLTLLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKFLfKSVAENRQLQFErFVVAAGEDMHqVTDGSVDVVV 97
Cdd:COG2226 16 AALGLRPGARVLDLGCGTGRLaLALAERGARVTGVDISPEMLELA-RERAAEAGLNVE-FVVGDAEDLP-FPDGSFDLVI 92
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568993321 98 CTLVLCSVKNQEKILREVCRVLKPGGAFYFMEHVADERSTW 138
Cdd:COG2226 93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
28-128 |
9.83e-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: 72.08 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 28 TLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRQLQFERFVVAAGEDMHQVTDGSVDVVVCTLVL-CS 104
Cdd:cd02440 1 RVLDLGCGTGALALALasGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhHL 79
|
90 100
....*....|....*....|....
gi 568993321 105 VKNQEKILREVCRVLKPGGAFYFM 128
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
5-123 |
1.27e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 58.79 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 5 QMASQKRELFSNLQEFAGPSGkltlLEVGCGTGaNFKFY-----PPGCRVTCIDPNPNFEKFlfksvAENRQLQ---FER 76
Cdd:PRK08317 3 DFRRYRARTFELLAVQPGDRV----LDVGCGPG-NDARElarrvGPEGRVVGIDRSEAMLAL-----AKERAAGlgpNVE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568993321 77 FVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGG 123
Cdd:PRK08317 73 FVRGDADGL-PFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGG 118
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
10-129 |
2.83e-10 |
|
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273884 [Multi-domain] Cd Length: 223 Bit Score: 57.66 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 10 KRELFSNLQEFAGPsgklTLLEVGCGTG----ANFKFYPPGCRVTCIDPNPNFEKflfksVAENRQLQFER--FVVAAGE 83
Cdd:TIGR01934 28 RRRAVKLIGVFKGQ----KVLDVACGTGdlaiELAKSAPDRGKVTGVDFSSEMLE-----VAKKKSELPLNieFIQADAE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568993321 84 DMhQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFME 129
Cdd:TIGR01934 99 AL-PFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILE 143
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
30-127 |
2.55e-24 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 91.57 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 30 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRQLQFERFVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQ 108
Cdd:pfam08241 1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75
|
90
....*....|....*....
gi 568993321 109 EKILREVCRVLKPGGAFYF 127
Cdd:pfam08241 76 ERALREIARVLKPGGILII 94
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
19-138 |
3.25e-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: 90.05 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 19 EFAGPSGKLTLLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKFLfKSVAENRQLQFErFVVAAGEDMHqVTDGSVDVVV 97
Cdd:COG2226 16 AALGLRPGARVLDLGCGTGRLaLALAERGARVTGVDISPEMLELA-RERAAEAGLNVE-FVVGDAEDLP-FPDGSFDLVI 92
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568993321 98 CTLVLCSVKNQEKILREVCRVLKPGGAFYFMEHVADERSTW 138
Cdd:COG2226 93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
30-123 |
3.30e-19 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 78.37 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 30 LEVGCGTGANFKFYPP--GCRVTCIDPNPNFEKFLfKSVAENRQLQFErFVVAAGEDMHqVTDGSVDVVVCTLVL--CSV 105
Cdd:pfam13649 2 LDLGCGTGRLTLALARrgGARVTGVDLSPEMLERA-RERAAEAGLNVE-FVQGDAEDLP-FPDGSFDLVVSSGVLhhLPD 78
|
90
....*....|....*...
gi 568993321 106 KNQEKILREVCRVLKPGG 123
Cdd:pfam13649 79 PDLEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
11-128 |
6.79e-18 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 75.82 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 11 RELFSNLQEFAGPSGKLtlLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKflfksVAENRQLQFE-RFVVAAGEDMhQV 88
Cdd:COG2227 12 RRLAALLARLLPAGGRV--LDVGCGTGRLaLALARRGADVTGVDISPEALE-----IARERAAELNvDFVQGDLEDL-PL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568993321 89 TDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFM 128
Cdd:COG2227 84 EDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLS 123
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
28-128 |
9.83e-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: 72.08 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 28 TLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRQLQFERFVVAAGEDMHQVTDGSVDVVVCTLVL-CS 104
Cdd:cd02440 1 RVLDLGCGTGALALALasGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhHL 79
|
90 100
....*....|....*....|....
gi 568993321 105 VKNQEKILREVCRVLKPGGAFYFM 128
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
30-123 |
1.02e-16 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 72.02 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 30 LEVGCGTGANFKF---YPPGCRVTCIDPNPNFEKFLFKSVAENRQLQFERfVVAAGEDMHQVTDGSVDVVVCTLVLCSVK 106
Cdd:pfam08242 1 LEIGCGTGTLLRAlleALPGLEYTGLDISPAALEAARERLAALGLLNAVR-VELFQLDLGELDPGSFDVVVASNVLHHLA 79
|
90
....*....|....*..
gi 568993321 107 NQEKILREVCRVLKPGG 123
Cdd:pfam08242 80 DPRAVLRNIRRLLKPGG 96
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
2-172 |
8.14e-15 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 68.61 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 2 YNEQMAsqkRELFSNLQEFAG--PSGKlTLLEVGCGTGANFK-FYPPGCRVTCIDPNPNfekflfksvAENRQLQFERFV 78
Cdd:pfam13489 1 YAHQRE---RLLADLLLRLLPklPSPG-RVLDFGCGTGIFLRlLRAQGFSVTGVDPSPI---------AIERALLNVRFD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 79 VAAgEDMHQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFMEHVADerstwnYFWQQVLDPVWFLFFDG-- 156
Cdd:pfam13489 68 QFD-EQEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAS------DEADRLLLEWPYLRPRNgh 140
|
170
....*....|....*...
gi 568993321 157 -CNLTRESWKTI-EQASF 172
Cdd:pfam13489 141 iSLFSARSLKRLlEEAGF 158
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
23-134 |
5.20e-14 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 66.29 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 23 PSGKLTLLEVGCGTGA-NFKFYP---PGCRVTCIDpnpnFEKFLFKSVAEN-RQLQFERFVVAAG--EDM-HQVTDGSVD 94
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHlSFELAEelgPNAEVVGID----ISEEAIEKARENaQKLGFDNVEFEQGdiEELpELLEDDKFD 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568993321 95 VVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFMEHVADE 134
Cdd:pfam13847 77 VVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLA 116
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
11-134 |
1.81e-13 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 65.40 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 11 RELFSNLQEFAGPSGKLTLLEVGCGTGANFKFYPP-GCRVTCIDPNPNFekfLfkSVAENRQLQfERFVVAageDMHQVT 89
Cdd:COG4976 32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPrGYRLTGVDLSEEM---L--AKAREKGVY-DRLLVA---DLADLA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568993321 90 --DGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYF-MEHVADE 134
Cdd:COG4976 103 epDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFsVEDADGS 150
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
28-127 |
4.95e-13 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 62.15 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 28 TLLEVGCGTGAN---FKFYPPGCRVTCIDPNPNFekflfksVAENRQLQFE-RFVVAageDMHQVT-DGSVDVVVCTLVL 102
Cdd:COG4106 4 RVLDLGCGTGRLtalLAERFPGARVTGVDLSPEM-------LARARARLPNvRFVVA---DLRDLDpPEPFDLVVSNAAL 73
|
90 100
....*....|....*....|....*
gi 568993321 103 CSVKNQEKILREVCRVLKPGGAFYF 127
Cdd:COG4106 74 HWLPDHAALLARLAAALAPGGVLAV 98
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
17-127 |
1.41e-11 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 60.70 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 17 LQEFAGPSGKLTLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRQLQFERFVVAAGEDMHQVTDGSVD 94
Cdd:COG0500 18 LALLERLPKGGRVLDLGCGTGRNLLALaaRFGGRVIGIDLSPEAIALA-RARAAKAGLGNVEFLVADLAELDPLPAESFD 96
|
90 100 110
....*....|....*....|....*....|....*
gi 568993321 95 VVVCTLVLCSV--KNQEKILREVCRVLKPGGAFYF 127
Cdd:COG0500 97 LVVAFGVLHHLppEEREALLRELARALKPGGVLLL 131
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
5-123 |
1.27e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 58.79 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 5 QMASQKRELFSNLQEFAGPSGkltlLEVGCGTGaNFKFY-----PPGCRVTCIDPNPNFEKFlfksvAENRQLQ---FER 76
Cdd:PRK08317 3 DFRRYRARTFELLAVQPGDRV----LDVGCGPG-NDARElarrvGPEGRVVGIDRSEAMLAL-----AKERAAGlgpNVE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568993321 77 FVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGG 123
Cdd:PRK08317 73 FVRGDADGL-PFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGG 118
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
10-129 |
2.83e-10 |
|
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273884 [Multi-domain] Cd Length: 223 Bit Score: 57.66 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 10 KRELFSNLQEFAGPsgklTLLEVGCGTG----ANFKFYPPGCRVTCIDPNPNFEKflfksVAENRQLQFER--FVVAAGE 83
Cdd:TIGR01934 28 RRRAVKLIGVFKGQ----KVLDVACGTGdlaiELAKSAPDRGKVTGVDFSSEMLE-----VAKKKSELPLNieFIQADAE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568993321 84 DMhQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFME 129
Cdd:TIGR01934 99 AL-PFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILE 143
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
28-127 |
4.19e-10 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 56.09 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 28 TLLEVGCGTGANFKF----YppGCRVTCIDPNPNfekflfksvaenrQLQF-ERFVVAAG---------EDMHQVT-DGS 92
Cdd:COG2230 54 RVLDIGCGWGGLALYlarrY--GVRVTGVTLSPE-------------QLEYaRERAAEAGladrvevrlADYRDLPaDGQ 118
|
90 100 110
....*....|....*....|....*....|....*..
gi 568993321 93 VDVVVCTLVLCSV--KNQEKILREVCRVLKPGGAFYF 127
Cdd:COG2230 119 FDAIVSIGMFEHVgpENYPAYFAKVARLLKPGGRLLL 155
|
|
| BioC |
TIGR02072 |
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
5-177 |
7.39e-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: 53.83 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 5 QMASQKRELFSNLQEFAGPSgkltLLEVGCGTG----ANFKFYPPGcRVTCIDPNPNFEKFLFKSVAENRQlqferFVVA 80
Cdd:TIGR02072 18 EMAKRLLALLKEKGIFIPAS----VLDIGCGTGyltrALLKRFPQA-EFIALDISAGMLAQAKTKLSENVQ-----FICG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 81 ageDMHQ--VTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFMEHVADERSTWNYFWQQVLDPVwflffdgcn 158
Cdd:TIGR02072 88 ---DAEKlpLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLRY--------- 155
|
170
....*....|....*....
gi 568993321 159 LTRESWKTIEQASFSKLKL 177
Cdd:TIGR02072 156 LSLDELKALLKNSFELLTL 174
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
22-129 |
5.08e-07 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 48.20 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 22 GPSGKLTLLEVGCGTGA-NFKFYP---PGCRVTCIDPNPNFEKFLFKSVAENRQLQFErFVVAAGEDMhQVTDGSVDVVV 97
Cdd:pfam01209 39 GVKRGNKFLDVAGGTGDwTFGLSDsagSSGKVVGLDINENMLKEGEKKAKEEGKYNIE-FLQGNAEEL-PFEDDSFDIVT 116
|
90 100 110
....*....|....*....|....*....|..
gi 568993321 98 CTLVLCSVKNQEKILREVCRVLKPGGAFYFME 129
Cdd:pfam01209 117 ISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLE 148
|
|
| arsM |
PRK11873 |
arsenite methyltransferase; |
88-126 |
7.00e-07 |
|
arsenite methyltransferase;
Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 48.02 E-value: 7.00e-07
10 20 30
....*....|....*....|....*....|....*....
gi 568993321 88 VTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFY 126
Cdd:PRK11873 142 VADNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFA 180
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
4-145 |
9.10e-07 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 47.83 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 4 EQMASQKRELFSNLQEFAGPSGKLTLLEVGCGTGANFKFY-PPGCRVTCIDPNPNFekflfksVAENRQLQFERFVVAAG 82
Cdd:PRK10258 21 EQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWrERGSQVTALDLSPPM-------LAQARQKDAADHYLAGD 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568993321 83 EDMHQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKPGGAFYFMEHVADERSTWNYFWQQV 145
Cdd:PRK10258 94 IESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAV 156
|
|
| COG4627 |
COG4627 |
Predicted SAM-depedendent methyltransferase [General function prediction only]; |
24-180 |
3.37e-06 |
|
Predicted SAM-depedendent methyltransferase [General function prediction only];
Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 45.24 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 24 SGKLTLLEVGCGTganfkFYPPGCRVTCIDPNPNfekflfksvaenrqlqferfVVAAGE--DMHQVTDGSVDVVVCTLV 101
Cdd:COG4627 1 SLSPLKLNIGCGP-----KRLPGWLNVDIVPAPG--------------------VDIVGDltDPLPFPDNSVDAIYSSHV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 102 L--CSVKNQEKILREVCRVLKPGG---------AFYFMEHVADERSTWNYFWQQVLDPVWFLFF-DGCNLTRESWKTIEQ 169
Cdd:COG4627 56 LehLDYEEAPLALKECYRVLKPGGilrivvpdlEHVARLYLAEYDAALDVAELRLAGPIDPLGIiLGERLAGLAARHSVL 135
|
170
....*....|.
gi 568993321 170 ASFSKLKLQHI 180
Cdd:COG4627 136 FRTGFTRLALT 146
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
21-123 |
3.57e-05 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 42.83 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 21 AGPSGKLTLLEVGCGTG--ANF--KFYPPGCRVTCIDPNPNF-----EKFLfksvAENRQLQFErFVVAAGEDMhQVTDG 91
Cdd:PRK00216 47 LGVRPGDKVLDLACGTGdlAIAlaKAVGKTGEVVGLDFSEGMlavgrEKLR----DLGLSGNVE-FVQGDAEAL-PFPDN 120
|
90 100 110
....*....|....*....|....*....|..
gi 568993321 92 SVDVVVCTLVLCSVKNQEKILREVCRVLKPGG 123
Cdd:PRK00216 121 SFDAVTIAFGLRNVPDIDKALREMYRVLKPGG 152
|
|
| PRK06202 |
PRK06202 |
hypothetical protein; Provisional |
23-191 |
6.15e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 180466 [Multi-domain] Cd Length: 232 Bit Score: 42.29 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 23 PSGKLTLLEVGCGTG------------ANFKFyppgcRVTCIDPNPnfEKFLF-KSVAENRQLQFERFVVAAgedmhQVT 89
Cdd:PRK06202 58 ADRPLTLLDIGCGGGdlaidlarwarrDGLRL-----EVTAIDPDP--RAVAFaRANPRRPGVTFRQAVSDE-----LVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 90 DGS-VDVVVCTLVLCSVKNQE-KILREVCRVLKPGGAFyfmehVAD-ERSTWNY--FW--QQVLDPVWFLFFDGCNLTRE 162
Cdd:PRK06202 126 EGErFDVVTSNHFLHHLDDAEvVRLLADSAALARRLVL-----HNDlIRSRLAYalFWagTRLLSRSSFVHTDGLLSVRR 200
|
170 180
....*....|....*....|....*....
gi 568993321 163 SWKTIEQASFsklklqhiqAPLSWTLVRP 191
Cdd:PRK06202 201 SYTPAELAAL---------APQGWRVERQ 220
|
|
| Rsm22 |
COG5459 |
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ... |
11-102 |
1.43e-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: 41.48 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 11 RELFSNLQEfAGPSGK-LTLLEVGCGTG----ANFKFYPPGCRVTCIDPNP---NFEKFLFKSVAEN--RQLQFERFVVA 80
Cdd:COG5459 66 RAALAELAE-AGPDFApLTVLDVGAGPGtaawAAADAWPSLLDATLLERSAaalALGRRLARAAANPalETAEWRLADLA 144
|
90 100
....*....|....*....|..
gi 568993321 81 AGEDmhqvtDGSVDVVVCTLVL 102
Cdd:COG5459 145 AALP-----APPADLVVASYVL 161
|
|
| PRK11036 |
PRK11036 |
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
23-128 |
4.48e-04 |
|
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
Pssm-ID: 182918 Cd Length: 255 Bit Score: 39.95 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 23 PSGKLTLLEVGCGTGA-NFKFYPPGCRVTCIDPNPNFEKFLFKSVAENRQLQFERFVVAAGEDMHQVTDGSVDVVVCTLV 101
Cdd:PRK11036 42 PPRPLRVLDAGGGEGQtAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIAQHLETPVDLILFHAV 121
|
90 100
....*....|....*....|....*..
gi 568993321 102 LCSVKNQEKILREVCRVLKPGGAFYFM 128
Cdd:PRK11036 122 LEWVADPKSVLQTLWSVLRPGGALSLM 148
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
30-148 |
7.09e-04 |
|
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: 38.63 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 30 LEVGCGTGanfkfY---------PPGCRVTCIDPNP--------NFEKFLFKSVAenrqlqfeRFVVA-AGEDMHQVTDG 91
Cdd:COG4122 21 LEIGTGTG-----YstlwlaralPDDGRLTTIEIDPeraaiareNFARAGLADRI--------RLILGdALEVLPRLADG 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 92 SVDvvvctLVLC-SVKNQ-EKILREVCRVLKPGGAFyfmehVADerstwNYFWQ-QVLDP 148
Cdd:COG4122 88 PFD-----LVFIdADKSNyPDYLELALPLLRPGGLI-----VAD-----NVLWHgRVADP 132
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
28-127 |
1.07e-03 |
|
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: 38.25 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 28 TLLEVGCGTG---ANFKFYPPGCRVTCIDPNpnfekflFKSVA---EN-RQLQFERFVVAAGEDMHQVTDGSVDVVVC-- 98
Cdd:COG2813 52 RVLDLGCGYGvigLALAKRNPEARVTLVDVN-------ARAVElarANaAANGLENVEVLWSDGLSGVPDGSFDLILSnp 124
|
90 100 110
....*....|....*....|....*....|....*....
gi 568993321 99 ----------TLVlcsvknqEKILREVCRVLKPGGAFYF 127
Cdd:COG2813 125 pfhagravdkEVA-------HALIADAARHLRPGGELWL 156
|
|
| CbiT |
TIGR02469 |
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ... |
28-124 |
8.13e-03 |
|
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274148 [Multi-domain] Cd Length: 124 Bit Score: 35.00 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568993321 28 TLLEVGCGTG------ANFKfypPGCRVTCIDPNPNFekflFKSVAENRQLQFERFVVAAGEDMHQVTDGSVDVVVCTLV 101
Cdd:TIGR02469 22 VLWDIGAGTGsvtieaARLV---PNGRVYAIERNPEA----LDLIERNLRRFGVSNIVIVEGDAPEAPEALLPDPDAVFV 94
|
90 100
....*....|....*....|...
gi 568993321 102 LCSVKNQEKILREVCRVLKPGGA 124
Cdd:TIGR02469 95 GGSGGLLQEILEAVERRLRPGGR 117
|
|
|