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Conserved domains on  [gi|387510282|emb|CCH57670|]
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Menaquinone biosynthesis methyltransferase ubiE (plasmid) [Fibrisoma limi BUZ 3]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 34-162 4.85e-37

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: 126.26  E-value: 4.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  34 FRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQfpDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALPYPDGS 113
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 387510282 114 MDLVTCSLLLHHLSdaDKQQSIREMHRVLSPGGMLMLADWGKPANKLMR 162
Cdd:COG2226   88 FDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 34-162 4.85e-37

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: 126.26  E-value: 4.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  34 FRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQfpDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALPYPDGS 113
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 387510282 114 MDLVTCSLLLHHLSdaDKQQSIREMHRVLSPGGMLMLADWGKPANKLMR 162
Cdd:COG2226   88 FDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-146 2.12e-34

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 118.05  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   50 VLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALPYPDGSMDLVTCSLLLHHLSDA 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 387510282  130 DKQQSIREMHRVLSPGG 146
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 19-171 3.32e-26

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: 100.80  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   19 PFYD---RVMALTMrENYFRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPD-ASVFGLDGDEKALAIARQKHAVAG 94
Cdd:TIGR01934  10 PKYDllnDLLSFGL-HRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrGKVTGVDFSSEMLEVAKKKSELPL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282   95 wPIVLEQGLSTALPYPDGSMDLVTCSLLLHHLSDadKQQSIREMHRVLSPGGMLMLADWGKPANKLMRLLsYGLQLF 171
Cdd:TIGR01934  89 -NIEFIQADAEALPFEDNSFDAVTIAFGLRNVTD--IQKALREMYRVLKPGGRLVILEFSKPANALLKKF-YKFYLK 161
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-164 8.31e-25

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 97.53  E-value: 8.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQFPD-ASVFGLDGDEKALAIARQKHAVAGW--PIVLEQGLSTALPYPDGSMDLVTCSLLLHHL 126
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREKLRDLGLsgNVEFVQGDAEALPFPDNSFDAVTIAFGLRNV 134

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 387510282 127 SDadKQQSIREMHRVLSPGGMLMLADWGKPANKLMRLL 164
Cdd:PRK00216 135 PD--IDKALREMYRVLKPGGRLVILEFSKPTNPPLKKA 170
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-153 1.77e-18

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: 77.47  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLhRQFPDASVFGLDGDEKALAIARQKHAVAGWP--IVLEQGLSTALPYPDGSMDLVTCSLLLHHLS 127
Cdd:cd02440    2 VLDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKAAAALLADnvEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*.
gi 387510282 128 DaDKQQSIREMHRVLSPGGMLMLADW 153
Cdd:cd02440   81 E-DLARFLEEARRLLKPGGVLVLTLV 105
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 31-150 1.45e-09

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: 56.14  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282    31 ENYFRSLLLEPIRDRKPRYVLDVGCGTG----TLALLLHRQFPDA-----SVFGLDGDEKALAIARQ----KHAVAGWPI 97
Cdd:smart00138  84 EEKVLPLLIASRRHGRRVRIWSAGCSTGeepySLAMLLAETLPKGrepdvKILATDIDLKALEKARAgiypERELEDLPK 163

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282    98 -VLEQGLS-----------------------TALPYPDGSMDLVTCSLLLHHLSDADKQQSIREMHRVLSPGGMLML 150
Cdd:smart00138 164 aLLARYFKevedkyrvkpelkervrfakhnlLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
rhodoquin_RquA NF038261
rhodoquinone biosynthesis methyltransferase RquA;
104-157 1.66e-09

rhodoquinone biosynthesis methyltransferase RquA;


Pssm-ID: 468437  Cd Length: 217  Bit Score: 55.56  E-value: 1.66e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 387510282 104 STALPYPDGSMDLVTCSLLLHHLSDADKQQSIREMHRVLSPGGMLMLADWGKPA 157
Cdd:NF038261 107 AAALQFGDGSYDAVLCFFLLHEVPEDVKRRIVAEALRVVKPGGKVVFVDYHRPA 160
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 34-162 4.85e-37

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: 126.26  E-value: 4.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  34 FRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQfpDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALPYPDGS 113
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 387510282 114 MDLVTCSLLLHHLSdaDKQQSIREMHRVLSPGGMLMLADWGKPANKLMR 162
Cdd:COG2226   88 FDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-146 2.12e-34

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 118.05  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   50 VLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALPYPDGSMDLVTCSLLLHHLSDA 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 387510282  130 DKQQSIREMHRVLSPGG 146
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 19-171 3.32e-26

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: 100.80  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   19 PFYD---RVMALTMrENYFRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPD-ASVFGLDGDEKALAIARQKHAVAG 94
Cdd:TIGR01934  10 PKYDllnDLLSFGL-HRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrGKVTGVDFSSEMLEVAKKKSELPL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282   95 wPIVLEQGLSTALPYPDGSMDLVTCSLLLHHLSDadKQQSIREMHRVLSPGGMLMLADWGKPANKLMRLLsYGLQLF 171
Cdd:TIGR01934  89 -NIEFIQADAEALPFEDNSFDAVTIAFGLRNVTD--IQKALREMYRVLKPGGRLVILEFSKPANALLKKF-YKFYLK 161
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 25-152 3.42e-26

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: 97.78  E-value: 3.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  25 MALTMRENYFRSLLLEPIRDR--KPRYVLDVGCGTGTLALLLHRQFpdASVFGLDGDEKALAIARQKHAVAGwpIVLEQG 102
Cdd:COG2227    1 MSDPDARDFWDRRLAALLARLlpAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELN--VDFVQG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 387510282 103 LSTALPYPDGSMDLVTCSLLLHHLSDADkqQSIREMHRVLSPGGMLMLAD 152
Cdd:COG2227   77 DLEDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-150 6.39e-26

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 96.19  E-value: 6.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   51 LDVGCGTGTLALLLHRQFPDasVFGLDGDEKALAIARQKHAVAGWPIVleQGLSTALPYPDGSMDLVTCSLLLHHLsdAD 130
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAPREGLTFV--VGDAEDLPFPDNSFDLVLSSEVLHHV--ED 74

                          90       100
                  ....*....|....*....|
gi 387510282  131 KQQSIREMHRVLSPGGMLML 150
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-164 8.31e-25

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 97.53  E-value: 8.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQFPD-ASVFGLDGDEKALAIARQKHAVAGW--PIVLEQGLSTALPYPDGSMDLVTCSLLLHHL 126
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREKLRDLGLsgNVEFVQGDAEALPFPDNSFDAVTIAFGLRNV 134

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 387510282 127 SDadKQQSIREMHRVLSPGGMLMLADWGKPANKLMRLL 164
Cdd:PRK00216 135 PD--IDKALREMYRVLKPGGRLVILEFSKPTNPPLKKA 170
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-214 3.93e-23

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 91.90  E-value: 3.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  45 RKPRYVLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQKHAVAGWPIV--LEQGLSTALPYPDGSMDLVTCSLL 122
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLGNVefLVADLAELDPLPAESFDLVVAFGV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282 123 LHHLSDADKQQSIREMHRVLSPGGMLMLADWgkPANKLMRLLSYGLQLFDGFDTTAANIQGRIPNMLYQGGFKDITQTGQ 202
Cdd:COG0500  104 LHHLPPEEREALLRELARALKPGGVLLLSAS--DAAAALSLARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDL 181

                        170
                 ....*....|..
gi 387510282 203 VNTLFGTLALYR 214
Cdd:COG0500  182 RSDALLESANAL 193
PRK08317 PRK08317
hypothetical protein; Provisional
 18-197 2.02e-22

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 91.15  E-value: 2.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  18 TPFYDRVmaltmRENYFRSLLLEPiRDRkpryVLDVGCGTGTLALLLHRQF-PDASVFGLDGDEKALAIARQKHAVAGWP 96
Cdd:PRK08317   1 LPDFRRY-----RARTFELLAVQP-GDR----VLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGLGPN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  97 IVLEQGLSTALPYPDGSMDLVTCSLLLHHLsdADKQQSIREMHRVLSPGGMLMLA--DWG----KPANK-LMRllsyglQ 169
Cdd:PRK08317  71 VEFVRGDADGLPFPDGSFDAVRSDRVLQHL--EDPARALAEIARVLRPGGRVVVLdtDWDtlvwHSGDRaLMR------K 142

                        170       180       190
                 ....*....|....*....|....*....|
gi 387510282 170 LFDGFDTTAAN--IQGRIPNMLYQGGFKDI 197
Cdd:PRK08317 143 ILNFWSDHFADpwLGRRLPGLFREAGLTDI 172
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-152 6.54e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 86.03  E-value: 6.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  46 KPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQKHAvagwPIVLEQGLSTALPyPDGSMDLVTCSLLLHH 125
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP----NVRFVVADLRDLD-PPEPFDLVVSNAALHW 75

                         90       100
                 ....*....|....*....|....*..
gi 387510282 126 LsdADKQQSIREMHRVLSPGGMLMLAD 152
Cdd:COG4106   76 L--PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 44-193 1.06e-20

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 84.39  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   44 DRKPRYVLDVGCGTGTLALLLHRQF-PDASVFGLDGDEKALAIAR---QKHAVAGwpIVLEQGLSTALP--YPDGSMDLV 117
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARenaQKLGFDN--VEFEQGDIEELPelLEDDKFDVV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387510282  118 TCSLLLHHLsdADKQQSIREMHRVLSPGGMLMLAD---WGKPANKLMRLLSYGLQLFDGfdttaANIQGRIPNMLYQGG 193
Cdd:pfam13847  79 ISNCVLNHI--PDPDKVLQEILRVLKPGGRLIISDpdsLAELPAHVKEDSTYYAGCVGG-----AILKKKLYELLEEAG 150
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-153 1.77e-18

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: 77.47  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLhRQFPDASVFGLDGDEKALAIARQKHAVAGWP--IVLEQGLSTALPYPDGSMDLVTCSLLLHHLS 127
Cdd:cd02440    2 VLDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKAAAALLADnvEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*.
gi 387510282 128 DaDKQQSIREMHRVLSPGGMLMLADW 153
Cdd:cd02440   81 E-DLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-148 6.03e-18

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 75.48  E-value: 6.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   51 LDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALP--YPDGSMDLVTCSLLLHHLsd 128
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLgeLDPGSFDVVVASNVLHHL-- 78

                          90       100
                  ....*....|....*....|
gi 387510282  129 ADKQQSIREMHRVLSPGGML 148
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
34-150 6.14e-18

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 77.73  E-value: 6.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  34 FRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFpdASVFGLDGDEKALAIARQKHAvagwPIVLEQGLSTALPYPDGS 113
Cdd:COG4976   34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREKGV----YDRLLVADLADLAEPDGR 107

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 387510282 114 MDLVTCSLLLHHLsdADKQQSIREMHRVLSPGGMLML 150
Cdd:COG4976  108 FDLIVAADVLTYL--GDLAAVFAGVARALKPGGLFIF 142
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 50-152 2.40e-16

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 73.04  E-value: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQKHAVAG--WPIVLEQGLSTALPyPDGSMDLVTCSLLLHHLS 127
Cdd:COG2230   55 VLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGlaDRVEVRLADYRDLP-ADGQFDAIVSIGMFEHVG 132

                         90       100
                 ....*....|....*....|....*
gi 387510282 128 DADKQQSIREMHRVLSPGGMLMLAD 152
Cdd:COG2230  133 PENYPAYFAKVARLLKPGGRLLLHT 157
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 21-156 1.85e-15

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: 72.32  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   21 YDRVmALTMRENYFRSL-LLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQKhavAGWPIVL 99
Cdd:TIGR02072   9 YDRH-AKIQREMAKRLLaLLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK---LSENVQF 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282  100 EQGLSTALPYPDGSMDLVTCSLLLHHLSDADkqQSIREMHRVLSPGGMLMLADWGKP 156
Cdd:TIGR02072  85 ICGDAEKLPLEDSSFDLIVSNLALQWCDDLS--QALSELARVLKPGGLLAFSTFGPG 139
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
44-162 4.65e-15

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 71.32  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   44 DRKPRYVLDVGCGTGTLALLLHRQF-PDASVFGLDGDEKALAIARQKHAVAGW-PIVLEQGLSTALPYPDGSMDLVTCSL 121
Cdd:pfam01209  40 VKRGNKFLDVAGGTGDWTFGLSDSAgSSGKVVGLDINENMLKEGEKKAKEEGKyNIEFLQGNAEELPFEDDSFDIVTISF 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 387510282  122 LLHHLSDADKqqSIREMHRVLSPGGMLMLADWGKPANKLMR 162
Cdd:pfam01209 120 GLRNFPDYLK--VLKEAFRVLKPGGRVVCLEFSKPENPLLS 158
PRK06202 PRK06202
hypothetical protein; Provisional
 34-138 2.38e-14

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 69.26  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  34 FRSLLLEPIRDRKPRYVLDVGCGTGTLALLL----HRQFPDASVFGLDGDEKALAIARQKHAVAGwpIVLEQGLSTALPY 109
Cdd:PRK06202  48 YRRLLRPALSADRPLTLLDIGCGGGDLAIDLarwaRRDGLRLEVTAIDPDPRAVAFARANPRRPG--VTFRQAVSDELVA 125

                         90       100
                 ....*....|....*....|....*....
gi 387510282 110 PDGSMDLVTCSLLLHHLSDADKQQSIREM 138
Cdd:PRK06202 126 EGERFDVVTSNHFLHHLDDAEVVRLLADS 154
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 25-173 1.26e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 63.22  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   25 MALTMRENYFRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDasVFGLDGDEKALAIARQKHavagwpiVLEQGLS 104
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFS--VTGVDPSPIAIERALLNV-------RFDQFDE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387510282  105 TALPYPDGSMDLVTCSLLLHHLSDADKqqSIREMHRVLSPGGMLMLADWGKPANKLMRLLSYGLQLFDG 173
Cdd:pfam13489  72 QEAAVPAGKFDVIVAREVLEHVPDPPA--LLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRN 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 37-150 2.56e-12

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: 62.90  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  37 LLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIAR---QKHAVAGWPIVLEQGLStalPYPDGS 113
Cdd:COG2813   40 LLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARanaAANGLENVEVLWSDGLS---GVPDGS 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 387510282 114 MDLVTCSLLLHHLSDADK---QQSIREMHRVLSPGGMLML 150
Cdd:COG2813  117 FDLILSNPPFHAGRAVDKevaHALIADAARHLRPGGELWL 156
arsM PRK11873
arsenite methyltransferase;
50-152 7.82e-12

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 62.66  E-value: 7.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQF-PDASVFGLDGDEKALAIARQKHAVAGWPIV-LEQGLSTALPYPDGSMDLV--TCSLllhH 125
Cdd:PRK11873  81 VLDLGSGGGFDCFLAARRVgPTGKVIGVDMTPEMLAKARANARKAGYTNVeFRLGEIEALPVADNSVDVIisNCVI---N 157

                         90       100
                 ....*....|....*....|....*..
gi 387510282 126 LSdADKQQSIREMHRVLSPGGMLMLAD 152
Cdd:PRK11873 158 LS-PDKERVFKEAFRVLKPGGRFAISD 183
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 39-162 9.45e-11

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 59.78  E-value: 9.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  39 LEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIAR---QKHAVAGWPIVLEQGLSTAL-------- 107
Cdd:COG2890  105 LALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARrnaERLGLEDRVRFLQGDLFEPLpgdgrfdl 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387510282 108 -----PY-PDGSMDLVTCSLLLH--HLS-DADK------QQSIREMHRVLSPGGMLML---ADWGKPANKLMR 162
Cdd:COG2890  185 ivsnpPYiPEDEIALLPPEVRDHepRLAlDGGEdgldfyRRIIAQAPRLLKPGGWLLLeigEDQGEAVRALLE 257
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 37-148 6.78e-10

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 57.08  E-value: 6.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  37 LLLEPIRDRKPRYVLDVGCGTGTLAllLHRQFPDASVFGLDGDEKALAIARQKHAVAGWpivlEQGLSTALPYPDGSMDL 116
Cdd:PRK10258  33 ALLAMLPQRKFTHVLDAGCGPGWMS--RYWRERGSQVTALDLSPPMLAQARQKDAADHY----LAGDIESLPLATATFDL 106

                         90       100       110
                 ....*....|....*....|....*....|..
gi 387510282 117 VTCSLLLHHLSDAdkQQSIREMHRVLSPGGML 148
Cdd:PRK10258 107 AWSNLAVQWCGNL--STALRELYRVVRPGGVV 136
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 45-119 7.18e-10

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: 56.69  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  45 RKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQkhAVAGWPI-----VLEQGLSTALPY-PDGSMDLVT 118
Cdd:COG4123   36 KKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARR--NVALNGLedritVIHGDLKEFAAElPPGSFDLVV 113


                 .
gi 387510282 119 C 119
Cdd:COG4123  114 S 114
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 44-158 9.89e-10

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: 56.89  E-value: 9.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  44 DRKPRYVLDVGCGTGTLALLLHRQFPD-ASVFGLDGDEKALAIARQ-----KHAVAGWPIVLEQGLSTALpyPDGSMDLV 117
Cdd:COG5459   78 DFAPLTVLDVGAGPGTAAWAAADAWPSlLDATLLERSAAALALGRRlaraaANPALETAEWRLADLAAAL--PAPPADLV 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 387510282 118 TCSLLLHHLSDADKQQSIREMHrvLSPGGMLMLADWGKPAN 158
Cdd:COG5459  156 VASYVLNELADAARAALVDRLW--LAPDGALLIVEPGTPAG 194
PLN02244 PLN02244
tocopherol O-methyltransferase
 44-153 1.05e-09

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 57.06  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  44 DRKPRYVLDVGCGTGTLALLLHRQFpDASVFGLdgdekALAIARQKHAVAgwpIVLEQGLS--------TAL--PYPDGS 113
Cdd:PLN02244 116 EKRPKRIVDVGCGIGGSSRYLARKY-GANVKGI-----TLSPVQAARANA---LAAAQGLSdkvsfqvaDALnqPFEDGQ 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 387510282 114 MDLVTCSLLLHHLsdADKQQSIREMHRVLSPGGMLMLADW 153
Cdd:PLN02244 187 FDLVWSMESGEHM--PDKRKFVQELARVAAPGGRIIIVTW 224
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 31-150 1.45e-09

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: 56.14  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282    31 ENYFRSLLLEPIRDRKPRYVLDVGCGTG----TLALLLHRQFPDA-----SVFGLDGDEKALAIARQ----KHAVAGWPI 97
Cdd:smart00138  84 EEKVLPLLIASRRHGRRVRIWSAGCSTGeepySLAMLLAETLPKGrepdvKILATDIDLKALEKARAgiypERELEDLPK 163

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282    98 -VLEQGLS-----------------------TALPYPDGSMDLVTCSLLLHHLSDADKQQSIREMHRVLSPGGMLML 150
Cdd:smart00138 164 aLLARYFKevedkyrvkpelkervrfakhnlLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
rhodoquin_RquA NF038261
rhodoquinone biosynthesis methyltransferase RquA;
104-157 1.66e-09

rhodoquinone biosynthesis methyltransferase RquA;


Pssm-ID: 468437  Cd Length: 217  Bit Score: 55.56  E-value: 1.66e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 387510282 104 STALPYPDGSMDLVTCSLLLHHLSDADKQQSIREMHRVLSPGGMLMLADWGKPA 157
Cdd:NF038261 107 AAALQFGDGSYDAVLCFFLLHEVPEDVKRRIVAEALRVVKPGGKVVFVDYHRPA 160
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 49-155 3.01e-09

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 55.28  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  49 YVLDVGCGTGTLALLLHRQF-PDASVFGLDGDEKALAIA-RQKHAVAG------WPIvleQGLSTALPYPDGSMDLVTCS 120
Cdd:PLN02233  76 RVLDLCCGSGDLAFLLSEKVgSDGKVMGLDFSSEQLAVAaSRQELKAKscykniEWI---EGDATDLPFDDCYFDAITMG 152

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 387510282 121 LLLHHLsdADKQQSIREMHRVLSPGGMLMLADWGK 155
Cdd:PLN02233 153 YGLRNV--VDRLKAMQEMYRVLKPGSRVSILDFNK 185
PRK05785 PRK05785
hypothetical protein; Provisional
 43-164 4.31e-09

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 54.69  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  43 RDRKPRYVLDVGCGTGTLALLLhRQFPDASVFGLDGDEKALAIArqkhAVAGWPIVleqGLSTALPYPDGSMDLVTCSLL 122
Cdd:PRK05785  48 YCGRPKKVLDVAAGKGELSYHF-KKVFKYYVVALDYAENMLKMN----LVADDKVV---GSFEALPFRDKSFDVVMSSFA 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 387510282 123 LHhlSDADKQQSIREMHRVlsPGGMLMLADWGKPANKLMRLL 164
Cdd:PRK05785 120 LH--ASDNIEKVIAEFTRV--SRKQVGFIAMGKPDNVIKRKY 157
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 37-148 8.75e-09

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: 52.98  E-value: 8.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   37 LLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIAR---QKHAVAGWPIVLEQGLSTAlpyPDGS 113
Cdd:pfam05175  22 LLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARenlAANGLENGEVVASDVYSGV---EDGK 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 387510282  114 MDLVTCSLLLH---HLSDADKQQSIREMHRVLSPGGML 148
Cdd:pfam05175  99 FDLIISNPPFHaglATTYNVAQRFIADAKRHLRPGGEL 136
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 39-88 1.29e-08

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 53.63  E-value: 1.29e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 387510282  39 LEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQ 88
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARR 150
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 43-148 1.33e-08

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: 52.26  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  43 RDRKPRYVLDVGCGTGTL---ALLLHRQfpdasVFGLDGDEKALAIARQ--KHAvAGWPIVLEQGLSTALPYPDGSMDLV 117
Cdd:COG1041   23 GAKEGDTVLDPFCGTGTIlieAGLLGRR-----VIGSDIDPKMVEGAREnlEHY-GYEDADVIRGDARDLPLADESVDAI 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 387510282 118 -------TCSLLLHHLSDADKQQSIREMHRVLSPGGML 148
Cdd:COG1041   97 vtdppygRSSKISGEELLELYEKALEEAARVLKPGGRV 134
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 38-162 2.57e-08

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 52.64  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  38 LLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQ--------KHAVAGWpivlEQGLSTALPY 109
Cdd:PRK01683  23 LLARVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSrlpdcqfvEADIASW----QPPQALDLIF 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282 110 PDGSMDLVTCSL-LLHHLSDAdkqqsiremhrvLSPGGML---MLADWGKPANKLMR 162
Cdd:PRK01683  99 ANASLQWLPDHLeLFPRLVSL------------LAPGGVLavqMPDNLDEPSHVLMR 143
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 51-151 5.58e-08

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 50.82  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   51 LDVGCGTGTLAL-----------LLHRQFPDASVFGLDGDEKALAIARQKHAVAGW--PIVLEQGLSTALPYPDGSMDLV 117
Cdd:pfam01170  33 LDPMCGSGTILIeaalmganiapGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVgdLIEFVQADAADLPLLEGSVDVI 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 387510282  118 TC------SLLLHHLSDADKQQSIREMHRVLSPGGMLMLA 151
Cdd:pfam01170 113 VTnppygiRLGSKGALEALYPEFLREAKRVLRGGGWLVLL 152
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
103-151 8.95e-08

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 49.86  E-value: 8.95e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 387510282 103 LSTALPYPDGSMDLVTCSLLLHHLSDADKQQSIREMHRVLSPGGMLMLA 151
Cdd:COG4627   36 LTDPLPFPDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRIV 84
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 19-124 2.62e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 49.69  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  19 PFYDrvmaltmrenyfrslLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQKHAVAGwpiv 98
Cdd:PRK14103  17 PFYD---------------LLARVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARERGVDAR---- 77

                         90       100
                 ....*....|....*....|....*.
gi 387510282  99 lEQGLSTALPYPDgsMDLVTCSLLLH 124
Cdd:PRK14103  78 -TGDVRDWKPKPD--TDVVVSNAALQ 100
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 14-146 2.30e-06

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 47.19  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  14 WKGLTPFYDRVMALTMRENYFRSLLLEP--IRDRKPRyVLDVGCGTG--TLALLLHRQFPDASVfgLDGDEKALAIARQK 89
Cdd:PLN02490  80 YRFLSIVYDHIINPGHWTEDMRDDALEPadLSDRNLK-VVDVGGGTGftTLGIVKHVDAKNVTI--LDQSPHQLAKAKQK 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282  90 HAVAGWPIVleQGLSTALPYPDGSMDLVTCSLLLHHLSDAdkQQSIREMHRVLSPGG 146
Cdd:PLN02490 157 EPLKECKII--EGDAEDLPFPTDYADRYVSAGSIEYWPDP--QRGIKEAYRVLKIGG 209
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 27-83 3.94e-06

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: 44.63  E-value: 3.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 387510282   27 LTMREnyFRSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKAL 83
Cdd:TIGR02469   2 MTKRE--VRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEAL 56
Methyltransf_29 pfam03141
Putative S-adenosyl-L-methionine-dependent methyltransferase; This family is a putative ...
 48-159 4.67e-06

Putative S-adenosyl-L-methionine-dependent methyltransferase; This family is a putative S-adenosyl-L-methionine (SAM)-dependent methyltransferase.


Pssm-ID: 335237 [Multi-domain]  Cd Length: 506  Bit Score: 46.53  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   48 RYVLDVGCGtgtlalllhrqfpDASvFG---LDGDEKALAIA-RQKHaVAGWPIVLEQGL--------STALPYPDGSMD 115
Cdd:pfam03141 119 RTALDVGCG-------------VAS-FGaylLSRDVLTMSFApKDVH-EAQVQFALERGIpamlgvlgTKRLPYPSRSFD 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 387510282  116 LVTCS-LLLHHLSDADKQqsIREMHRVLSPGGMLMLAdwGKPANK 159
Cdd:pfam03141 184 LAHCSrCRIPWTANDGIL--LLEVDRVLRPGGYFVLS--GPPVYA 224
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 12-88 7.00e-06

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 45.17  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  12 LRWKGLTP-----FYDRVMALTMRENYFRSLLLEPIRDRKPRYVLDVGCGTGTL----ALLLHRQfpdASVFGLDGDEKA 82
Cdd:PRK00377   1 MEWKYVIPgipdeEFERDEEIPMTKEEIRALALSKLRLRKGDMILDIGCGTGSVtveaSLLVGET---GKVYAVDKDEKA 77


                 ....*.
gi 387510282  83 LAIARQ 88
Cdd:PRK00377  78 INLTRR 83
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 50-153 9.15e-06

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 45.35  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQKHAVAGwPIVLEQGLSTALPYPDGSMDLVTCSLLLHHLSDA 129
Cdd:PTZ00098  56 VLDIGSGLGGGCKYINEKY-GAHVHGVDICEKMVNIAKLRNSDKN-KIEFEANDILKKDFPENTFDMIYSRDAILHLSYA 133

                         90       100
                 ....*....|....*....|....
gi 387510282 130 DKQQSIREMHRVLSPGGMLMLADW 153
Cdd:PTZ00098 134 DKKKLFEKCYKWLKPNGILLITDY 157
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
50-189 2.89e-05

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 44.09  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALP--YPDGSMDLVTCSLLLHHL- 126
Cdd:PRK06922 422 IVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKKKQNEGRSWNVIKGDAINLSssFEKESVDTIVYSSILHELf 501

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387510282 127 ----SDADK------QQSIREMHRVLSPGGMLMLADWGKPANK-LMRLLSY----GLQLFDGFdttAANIQGRIPNML 189
Cdd:PRK06922 502 syieYEGKKfnheviKKGLQSAYEVLKPGGRIIIRDGIMTEDKrLMRVIRFkdagGMKFLEQY---VQEFKGRIIQYE 576
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
44-151 3.65e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.62  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  44 DRKPRYVLDVGCGTGTLALLLHRQFPdASVFGLDGDEKALAIAR---QKHAVAGWPIVLEQGLSTALPYpdgsmDLVTCS 120
Cdd:COG2264  146 LKPGKTVLDVGCGSGILAIAAAKLGA-KRVLAVDIDPVAVEAARenaELNGVEDRIEVVLGDLLEDGPY-----DLVVAN 219

                         90       100       110
                 ....*....|....*....|....*....|..
gi 387510282 121 LLLH-HLSDADkqqsirEMHRVLSPGGMLMLA 151
Cdd:COG2264  220 ILANpLIELAP------DLAALLKPGGYLILS 245
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 31-92 4.72e-05

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 43.11  E-value: 4.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387510282   31 ENYFRSLLLEPIRDRkpryVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIAR---QKHAV 92
Cdd:TIGR00536 103 EKALASLISQPPILH----ILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEenaEKNQL 163
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 42-152 8.10e-05

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: 41.71  E-value: 8.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  42 IRDRKPRYVLDVGCGTGTLALLLHRQFP-DASVFGLDGDEKALAIARQKHAVAGWP----IVLEQGLSTALPYPDGSMDL 116
Cdd:COG4122   12 ARLLGAKRILEIGTGTGYSTLWLARALPdDGRLTTIEIDPERAAIARENFARAGLAdrirLILGDALEVLPRLADGPFDL 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 387510282 117 VtcslllhhLSDADKQQSIREMHRV---LSPGGMLmLAD 152
Cdd:COG4122   92 V--------FIDADKSNYPDYLELAlplLRPGGLI-VAD 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
44-88 1.75e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 41.04  E-value: 1.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 387510282  44 DRKPRYVLDVGCGTGTLALLLhrQFPDAS-VFGLDGDEKALAIARQ 88
Cdd:COG2263   43 DIEGKTVLDLGCGTGMLAIGA--ALLGAKkVVGVDIDPEALEIARE 86
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 44-159 3.06e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.89  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  44 DRKP-RYVLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQKHAVAGWPIVLEQGLSTALPYPDGSMDLVTCSLL 122
Cdd:PLN02336 263 DLKPgQKVLDVGCGIGGGDFYMAENF-DVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDT 341

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 387510282 123 LHHLSdaDKQQSIREMHRVLSPGGMLMLADWGKPANK 159
Cdd:PLN02336 342 ILHIQ--DKPALFRSFFKWLKPGGKVLISDYCRSPGT 376
PRK14968 PRK14968
putative methyltransferase; Provisional
 37-87 8.80e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.73  E-value: 8.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 387510282  37 LLLEPIRDRKPRYVLDVGCGTGTLALLLHRQfpDASVFGLDGDEKALAIAR 87
Cdd:PRK14968  14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAK 62
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-88 1.09e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 37.93  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 387510282   35 RSLLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGD----EKALAIARQ 88
Cdd:pfam13679  14 APLLKELLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRaelvEKANALAQK 71
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 75-155 1.23e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 38.13  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  75 GLDGDEKALAIARQKHAVAGWP----IVLEQGLSTALPYPDGSMDLVTCSLLLHHLsdADKQQSIREMHRVLSPGGMLML 150
Cdd:PLN02232   2 GLDFSSEQLAVAATRQSLKARScykcIEWIEGDAIDLPFDDCEFDAVTMGYGLRNV--VDRLRAMKEMYRVLKPGSRVSI 79


                 ....*
gi 387510282 151 ADWGK 155
Cdd:PLN02232  80 LDFNK 84
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 43-150 1.45e-03

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: 38.79  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   43 RDRKPRYVLDVGCGTGTLALLLHRqFPDASVFGLDGDEKALAIAR----QKHAVAGWPIVLEQGLstalpyPDGSMDLVT 118
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALK-LGAKKVVGVDIDPVAVRAAKenaeLNGVEARLEVYLPGDL------PKEKADVVV 230

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 387510282  119 CSLLLHhlsdadkqqSIREM----HRVLSPGGMLML 150
Cdd:pfam06325 231 ANILAD---------PLIELapdiYALVKPGGYLIL 257
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 37-141 2.18e-03

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 37.82  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   37 LLLEPIRDRKPryVLDVGCGTGTLALLLhRQFPDASVFGLDGDEKALAIARQKhAVAgwpiVLEQGLSTALP-YPDGSMD 115
Cdd:pfam07021   6 YILEWIPPGSR--VLDLGCGDGTLLYLL-KEEKGVDGYGIELDAAGVAECVAK-GLY----VIQGDLDEGLEhFPDKSFD 77

                          90       100
                  ....*....|....*....|....*.
gi 387510282  116 LVTCSLLLHHLSDADkqQSIREMHRV 141
Cdd:pfam07021  78 YVILSQTLQATRNPR--EVLDEMLRI 101
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 50-141 2.97e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 37.35  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   50 VLDVGCGTGT-LALLLHRQFPDASVFGLDGDEKALAIARQKHavagwpiVLEQGLSTALP-YPDGSMDLVTCSLLLHHLS 127
Cdd:TIGR02081  17 VLDLGCGDGElLALLRDEKQVRGYGIEIDQDGVLACVARGVN-------VIQGDLDEGLEaFPDKSFDYVILSQTLQATR 89

                          90
                  ....*....|....
gi 387510282  128 DADkqQSIREMHRV 141
Cdd:TIGR02081  90 NPE--EILDEMLRV 101
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 39-88 3.58e-03

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 37.85  E-value: 3.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 387510282  39 LEPIRDRKPRYVLDVGCGTGTLALLLHRQFpdASVFGLDGDEKALAIARQ 88
Cdd:COG2265  226 LEWLDLTGGERVLDLYCGVGTFALPLARRA--KKVIGVEIVPEAVEDARE 273
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 50-111 3.72e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 37.84  E-value: 3.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387510282  50 VLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQ---KHAV------AGW-PIVLEQglstaLPYPD 111
Cdd:COG2242  251 LWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRAnarRFGVpnvevvEGEaPEALAD-----LPDPD 317
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 35-185 3.92e-03

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 37.17  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  35 RSLLLEP-IRDRKpryVLDVGCGTGTLALLLHRQFpDASVFGLDGDEKALAIARQkHAVA-GWPIVLEQGLSTALPyPDG 112
Cdd:COG3897   61 RYLLDHPeVAGKR---VLELGCGLGLVGIAAAKAG-AADVTATDYDPEALAALRL-NAALnGVAITTRLGDWRDPP-AAG 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387510282 113 SMDLVTCSLLLHHLSDADkqQSIREMHRVLSPGGMLMLADWGKP-----ANKLMRLLSYGLQLFDGFDTTAAnIQGRI 185
Cdd:COG3897  135 GFDLILGGDVLYERDLAE--PLLPFLDRLAAPGGEVLIGDPGRGylpafRERLEALAGYEVVTRELEDTEKV-KRGRV 209
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
50-149 5.57e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 36.55  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282  50 VLDVGCGTGTLALLLHRQFPDaSVFGLDGDEKALAIARQKHAVAGWP--IVLEQGLSTALpYPDGSMDLVTCSLLLHHLS 127
Cdd:COG4076   39 VLDIGTGSGLLSMLAARAGAK-KVYAVEVNPDIAAVARRIIAANGLSdrITVINADATDL-DLPEKADVIISEMLDTALL 116

                         90       100
                 ....*....|....*....|...
gi 387510282 128 DADKQQSIRE-MHRVLSPGGMLM 149
Cdd:COG4076  117 DEGQVPILNHaRKRLLKPGGRII 139
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
50-196 5.89e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 36.63  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282    50 VLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQKHAVAGWP--IVLEQGLSTALPYPDgSMDLVTCSLLLHHLs 127
Cdd:smart00828   3 VLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQgrIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387510282   128 dADKQQSIREMHRVLSPGGMLMLAD----------------WGKPANKLMRLLS-YGLQLFDGFDTTAaniqgRIPNMLY 190
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVLADfianllsaieheettsYLVTREEWAELLArNNLRVVEGVDASL-----EIANFLY 154


                   ....*.
gi 387510282   191 QGGFKD 196
Cdd:smart00828 155 DPGFED 160
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
43-88 5.96e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 36.67  E-value: 5.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 387510282  43 RDRKPRYVLDVGCGTGTLALLLhRQFPDASVFGLDGDEKALAIARQ 88
Cdd:PRK00517 116 LVLPGKTVLDVGCGSGILAIAA-AKLGAKKVLAVDIDPQAVEAARE 160
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
37-88 8.47e-03

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 36.45  E-value: 8.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 387510282  37 LLLEPIRDRKPRYVLDVGCGTGTLALLLHRQFPDASVFGLDGDEKALAIARQ 88
Cdd:PRK09489 187 LLLSTLTPHTKGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRA 238
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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