|
Name |
Accession |
Description |
Interval |
E-value |
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
36-172 |
6.60e-22 |
|
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: 88.54 E-value: 6.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 36 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 113
Cdd:COG2227 2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_C 114 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2227 71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-168 |
1.82e-16 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 72.98 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 60 VLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLGn 138
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG- 71
|
90 100 110
....*....|....*....|....*....|
1D2H_C 139 SFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649 72 VLHHLPD-----PDLEAALREIARVLKPGG 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
59-172 |
2.57e-12 |
|
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: 62.06 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
|
90 100 110
....*....|....*....|....*....|....*
1D2H_C 138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440 74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
21-165 |
8.36e-09 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 54.84 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580 29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D2H_C 100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
58-172 |
5.56e-06 |
|
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: 46.49 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934 41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
1D2H_C 134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
36-172 |
6.60e-22 |
|
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: 88.54 E-value: 6.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 36 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 113
Cdd:COG2227 2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_C 114 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2227 71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
36-172 |
1.45e-18 |
|
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: 80.04 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 36 DTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWV-IEE 114
Cdd:COG2226 2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELA------RERAAEAGLNVeFVV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
1D2H_C 115 ANWLTLdkdvPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2226 76 GDAEDL----PFPDGsFDLVISS-FVLHHLPD-------PERALAEIARVLKPGGRLVV 122
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-168 |
1.82e-16 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 72.98 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 60 VLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLGn 138
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG- 71
|
90 100 110
....*....|....*....|....*....|
1D2H_C 139 SFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649 72 VLHHLPD-----PDLEAALREIARVLKPGG 96
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
46-172 |
5.72e-15 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 70.73 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 46 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlKERWNRRKEPafDKWVIEEANWLtldkDV 124
Cdd:COG2230 41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYA-RERAAEAGLA--DRVEVRLADYR----DL 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
1D2H_C 125 PAGDGFDAVICLGnSFAHLPDskgdqSEHRLALKNIASMVRPGGLLVI 172
Cdd:COG2230 114 PADGQFDAIVSIG-MFEHVGP-----ENYPAYFAKVARLLKPGGRLLL 155
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
19-178 |
8.13e-15 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 70.80 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 19 DQYADgeaarVWQLYIGDTR--SRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlk 96
Cdd:COG4976 12 DQYAD-----SYDAALVEDLgyEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 97 erwnrRKEPAFDKWVIEEanwltLDKDVPAGDGFDAVICLGnSFAHLPDskgdqseHRLALKNIASMVRPGGLLVIDHKN 176
Cdd:COG4976 85 -----REKGVYDRLLVAD-----LADLAEPDGRFDLIVAAD-VLTYLGD-------LAAVFAGVARALKPGGLFIFSVED 146
|
..
1D2H_C 177 YD 178
Cdd:COG4976 147 AD 148
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
59-174 |
1.31e-13 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 65.62 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvIEEANWLTLDKDVPagdgFDAVICl 136
Cdd:COG4106 4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARA------RARLPNVR---FVVADLRDLDPPEP----FDLVVS- 69
|
90 100 110
....*....|....*....|....*....|....*...
1D2H_C 137 GNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVIDH 174
Cdd:COG4106 70 NAALHWLPD-------HAALLARLAAALAPGGVLAVQV 100
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-172 |
8.67e-13 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 63.07 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 61 LDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwNRRKEPAFDKWVIEEANwltldkDVPAGDG-FDAVICLgNS 139
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA-----REKAPREGLTFVVGDAE------DLPFPDNsFDLVLSS-EV 68
|
90 100 110
....*....|....*....|....*....|...
1D2H_C 140 FAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam08241 69 LHHVED-------PERALREIARVLKPGGILII 94
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
59-172 |
2.57e-12 |
|
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: 62.06 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
|
90 100 110
....*....|....*....|....*....|....*
1D2H_C 138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440 74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-170 |
1.60e-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: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 61 LDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLgN 138
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA------RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS-N 73
|
90 100 110
....*....|....*....|....*....|..
1D2H_C 139 SFAHLPDSKGdqsehrlALKNIASMVRPGGLL 170
Cdd:pfam08242 74 VLHHLADPRA-------VLRNIRRLLKPGGVL 98
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
59-174 |
3.51e-10 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 57.43 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGVDSIMLVEEGFS---VTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDVpAGDGFDAVIC 135
Cdd:pfam13847 6 RVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARE----NAQKLGFDNVEFEQGDIEELPELL-EDDKFDVVIS 80
|
90 100 110
....*....|....*....|....*....|....*....
1D2H_C 136 LGnSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVIDH 174
Cdd:pfam13847 81 NC-VLNHIPDP-------DKVLQEILRVLKPGGRLIISD 111
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
33-172 |
2.12e-09 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 55.51 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 33 YIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMlkyalkerwnrrKEPAFDKWVI 112
Cdd:pfam13489 1 YAHQRERLLADLLLRLLPKLPSPG--RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA------------IERALLNVRF 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 113 EEANwltLDKDVPAGDGFDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam13489 67 DQFD---EQEAAVPAGKFDVIVAR-EVLEHVPD-------PPALLRQIAALLKPGGLLLL 115
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
30-173 |
3.21e-09 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 55.69 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 30 WQLYIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkerwnRRKEPAFD 108
Cdd:COG0500 2 WDSYYSDELLPGLAALLALLERLPKGG--RVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALA------RARAAKAG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1D2H_C 109 kwvIEEANWLTLD----KDVPAGDgFDAVICLGnSFAHLPDSKGDQsehrlALKNIASMVRPGGLLVID 173
Cdd:COG0500 74 ---LGNVEFLVADlaelDPLPAES-FDLVVAFG-VLHHLPPEEREA-----LLRELARALKPGGVLLLS 132
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
21-165 |
8.36e-09 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 54.84 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580 29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D2H_C 100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
42-178 |
8.43e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 54.94 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 42 AEYKAWLLGLLRQHGCHRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYAlKERwnRRKEPAFDKWVIEEANWL 118
Cdd:PRK08317 5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KER--AAGLGPNVEFVRGDADGL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_C 119 tldkdvPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVIDHKNYD 178
Cdd:PRK08317 82 ------PFPDGsFDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWD 128
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
58-172 |
3.57e-07 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 50.15 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 58 HRVLDVACGTGVDSIMLVEEG---FSVTSVDASDKMLKYAlKERWNRRKEPAFDKWVIEEANWLTLDKDVpagdgFDAV- 133
Cdd:PRK00216 53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS-----FDAVt 126
|
90 100 110 120
....*....|....*....|....*....|....*....|.
1D2H_C 134 ICLG--NsfahLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:PRK00216 127 IAFGlrN----VPD-------IDKALREMYRVLKPGGRLVI 156
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
46-174 |
1.58e-06 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 47.49 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 46 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVE---EGFSVTSVDASDKMLKYAlkeRWNRRKEPAFDKWVIEEANWLTLDK 122
Cdd:COG4122 6 RLLYLLARLLGAKRILEIGTGTGYSTLWLARalpDDGRLTTIEIDPERAAIA---RENFARAGLADRIRLILGDALEVLP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
1D2H_C 123 DVPAGDgFDAVIClgnsfahlpDskGDQSEHRLALKNIASMVRPGGLLVIDH 174
Cdd:COG4122 83 RLADGP-FDLVFI---------D--ADKSNYPDYLELALPLLRPGGLIVADN 122
|
|
| MenG_MenH_UbiE |
TIGR01934 |
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ... |
58-172 |
5.56e-06 |
|
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: 46.49 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934 41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
1D2H_C 134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
58-184 |
2.36e-04 |
|
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: 41.09 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 58 HRVLDVACGTGVdsiMLVEE---GFSVTSVDASDKM-------LKYALKERWNRRKEPAFDkwvieeanwLTLdkdvpAG 127
Cdd:COG1041 28 DTVLDPFCGTGT---ILIEAgllGRRVIGSDIDPKMvegarenLEHYGYEDADVIRGDARD---------LPL-----AD 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
1D2H_C 128 DGFDAVIC---LGNSFahlpDSKGDQSEHRL--ALKNIASMVRPGGLLVI--DHKNYDYILSTG 184
Cdd:COG1041 91 ESVDAIVTdppYGRSS----KISGEELLELYekALEEAARVLKPGGRVVIvtPRDIDELLEEAG 150
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
59-171 |
4.98e-04 |
|
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440709 [Multi-domain] Cd Length: 392 Bit Score: 41.32 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGvdsimlveeGFS----------VTSVDASDKMLKYA--------LKERWNRRKEPAFDkwvieeanwlTL 120
Cdd:COG1092 219 RVLNLFSYTG---------GFSvhaaaggaksVTSVDLSATALEWAkenaalngLDDRHEFVQADAFD----------WL 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
1D2H_C 121 DKDVPAGDGFDAVIC----LGNSFAHLPDSKGDQSE-HRLALKniasMVRPGGLLV 171
Cdd:COG1092 280 RELAREGERFDLIILdppaFAKSKKDLFDAQRDYKDlNRLALK----LLAPGGILV 331
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
38-135 |
7.30e-04 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 40.52 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 38 RSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkeRWNRRKEPAFDKWVIEEA 115
Cdd:COG2890 94 RPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVA---RRNAERLGLEDRVRFLQG 170
|
90 100
....*....|....*....|
1D2H_C 116 NWLTldkDVPAGDGFDAVIC 135
Cdd:COG2890 171 DLFE---PLPGDGRFDLIVS 187
|
|
| Rsm22 |
COG5459 |
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ... |
59-172 |
7.34e-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: 40.32 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGVDSI---MLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLD-KDVPAGDGFDAVI 134
Cdd:COG5459 83 TVLDVGAGPGTAAWaaaDAWPSLLDATLLERSAAALALG------RRLARAAANPALETAEWRLADlAAALPAPPADLVV 156
|
90 100 110
....*....|....*....|....*....|....*....
1D2H_C 135 ClGNSFAHLPDSKgdqsehRLALknIASM-VRPGGLLVI 172
Cdd:COG5459 157 A-SYVLNELADAA------RAAL--VDRLwLAPDGALLI 186
|
|
| PLN02396 |
PLN02396 |
hexaprenyldihydroxybenzoate methyltransferase |
59-176 |
8.24e-04 |
|
hexaprenyldihydroxybenzoate methyltransferase
Pssm-ID: 178018 [Multi-domain] Cd Length: 322 Bit Score: 40.49 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 59 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkeRWNRRKEPafdkwVIEEANWL--TLDKDVPAGDGFDAVICL 136
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIA---RLHADMDP-----VTSTIEYLctTAEKLADEGRKFDAVLSL 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1D2H_C 137 gnsfahlpdskgDQSEHRLA----LKNIASMVRPGGLLVIDHKN 176
Cdd:PLN02396 206 ------------EVIEHVANpaefCKSLSALTIPNGATVLSTIN 237
|
|
| PRK10258 |
PRK10258 |
biotin biosynthesis protein BioC; Provisional |
48-106 |
1.10e-03 |
|
biotin biosynthesis protein BioC; Provisional
Pssm-ID: 182340 [Multi-domain] Cd Length: 251 Bit Score: 39.74 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
1D2H_C 48 LLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPA 106
Cdd:PRK10258 34 LLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA------RQKDAA 86
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
47-174 |
5.97e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 37.45 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 47 WLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYALKerwNRRKEPAfDKWVIEEANWLTldkDV 124
Cdd:PRK09328 99 WALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARR---NAKHGLG-ARVEFLQGDWFE---PL 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_C 125 PAGDgFDAVIClgN----SFAHLPDSKGDQSEH--RLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:PRK09328 172 PGGR-FDLIVS--NppyiPEADIHLLQPEVRDHepHLALfggedgldfyrriiEQAPRYLKPGGWLLLEI 238
|
|
|