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Conserved domains on  [gi|489502404|ref|WP_003407297|]
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MULTISPECIES: virulence-associated methyltransferase [Mycobacterium]

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]; ...
 41-153 2.71e-32

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: 115.86  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTVIS 120
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502404 121 AIGVMFAPDHQAAADELVRVCRPGGTIGVISWT 153
Cdd:COG2226   94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFS 126
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 41-153 2.71e-32

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: 115.86  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTVIS 120
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502404 121 AIGVMFAPDHQAAADELVRVCRPGGTIGVISWT 153
Cdd:COG2226   94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 53-145 2.84e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 90.70  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   53 VLDVAAGSGNISLPAAK-TGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTVISAIGVMF--APD 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpDPD 80

                          90
                  ....*....|....*.
gi 489502404  130 HQAAADELVRVCRPGG 145
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 41-150 1.87e-18

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: 81.54  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGAT---VISTDLTPELLQRSQARAAQQgLTLQYQEANAQALPFADDEFDT 117
Cdd:TIGR01934  31 AVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDFSSEMLEVAKKKSELP-LNIEFIQADAEALPFEDNSFDA 109

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489502404  118 VISAIGVMFAPDHQAAADELVRVCRPGGTIGVI 150
Cdd:TIGR01934 110 VTIAFGLRNVTDIQKALREMYRVLKPGGRLVIL 142
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 42-149 2.62e-17

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 78.66  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  42 VAAAGIGPGVRVLDVAAGSGNISLPAAKTG---ATVISTDLTPELLQRSQARAAQQGLT--LQYQEANAQALPFADDEFD 116
Cdd:PRK00216  44 IKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSgnVEFVQGDAEALPFPDNSFD 123

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502404 117 TVISAIGVMFAPDHQAAADELVRVCRPGGTIGV 149
Cdd:PRK00216 124 AVTIAFGLRNVPDIDKALREMYRVLKPGGRLVI 156
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 52-154 1.54e-09

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: 54.36  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  52 RVLDVAAGSGNISLPAAKT-GATVISTDLTPELLQRS-QARAAQQGLTLQYQEANA-QALPFADDEFDTVISAIGVM-FA 127
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELArKAAAALLADNVEVLKGDAeELPPEADESFDVIISDPPLHhLV 80

                         90       100
                 ....*....|....*....|....*..
gi 489502404 128 PDHQAAADELVRVCRPGGTIGVISWTC 154
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLVLA 107
rADc smart00650
Ribosomal RNA adenine dimethylases;
41-122 1.88e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.26  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404    41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQAR-AAQQGLTLQYQeaNAQALPFADDEFDTVI 119
Cdd:smart00650   5 IVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKfAAADNLTVIHG--DALKFDLPKLQPYKVV 82


                   ...
gi 489502404   120 SAI 122
Cdd:smart00650  83 GNL 85
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 41-153 2.71e-32

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: 115.86  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTVIS 120
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502404 121 AIGVMFAPDHQAAADELVRVCRPGGTIGVISWT 153
Cdd:COG2226   94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 53-145 2.84e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 90.70  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   53 VLDVAAGSGNISLPAAK-TGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTVISAIGVMF--APD 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpDPD 80

                          90
                  ....*....|....*.
gi 489502404  130 HQAAADELVRVCRPGG 145
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 54-147 1.73e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 88.88  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   54 LDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTlqYQEANAQALPFADDEFDTVISAIGVMFAPDHQAA 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT--FVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....
gi 489502404  134 ADELVRVCRPGGTI 147
Cdd:pfam08241  79 LREIARVLKPGGIL 92
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 47-147 7.13e-19

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 80.06  E-value: 7.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  47 IGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTlqYQEANAQALPFADDEFDTVISAIGVMF 126
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD--FVQGDLEDLPLEDGSFDLVICSEVLEH 99

                         90       100
                 ....*....|....*....|.
gi 489502404 127 APDHQAAADELVRVCRPGGTI 147
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLL 120
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 41-150 1.87e-18

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: 81.54  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGAT---VISTDLTPELLQRSQARAAQQgLTLQYQEANAQALPFADDEFDT 117
Cdd:TIGR01934  31 AVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDFSSEMLEVAKKKSELP-LNIEFIQADAEALPFEDNSFDA 109

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489502404  118 VISAIGVMFAPDHQAAADELVRVCRPGGTIGVI 150
Cdd:TIGR01934 110 VTIAFGLRNVTDIQKALREMYRVLKPGGRLVIL 142
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 42-149 2.62e-17

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 78.66  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  42 VAAAGIGPGVRVLDVAAGSGNISLPAAKTG---ATVISTDLTPELLQRSQARAAQQGLT--LQYQEANAQALPFADDEFD 116
Cdd:PRK00216  44 IKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSgnVEFVQGDAEALPFPDNSFD 123

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502404 117 TVISAIGVMFAPDHQAAADELVRVCRPGGTIGV 149
Cdd:PRK00216 124 AVTIAFGLRNVPDIDKALREMYRVLKPGGRLVI 156
PRK08317 PRK08317
hypothetical protein; Provisional
 43-147 5.92e-17

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 77.67  E-value: 5.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  43 AAAGIGPGVRVLDVAAGSGN--ISLpAAKTGAT--VISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTV 118
Cdd:PRK08317  13 ELLAVQPGDRVLDVGCGPGNdaREL-ARRVGPEgrVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAV 91

                         90       100
                 ....*....|....*....|....*....
gi 489502404 119 ISAIGVMFAPDHQAAADELVRVCRPGGTI 147
Cdd:PRK08317  92 RSDRVLQHLEDPARALAEIARVLRPGGRV 120
PLN02244 PLN02244
tocopherol O-methyltransferase
 29-152 9.96e-16

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 75.94  E-value: 9.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  29 MAEEVMAPLGpilVAAAGIGPGVRVLDVAAGSGNIS-LPAAKTGATVISTDLTPELLQRSQARAAQQGLT--LQYQEANA 105
Cdd:PLN02244 101 MIEESLAWAG---VPDDDEKRPKRIVDVGCGIGGSSrYLARKYGANVKGITLSPVQAARANALAAAQGLSdkVSFQVADA 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489502404 106 QALPFADDEFDTVISAIGVMFAPDHQAAADELVRVCRPGGTIGVISW 152
Cdd:PLN02244 178 LNQPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVTW 224
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
46-163 3.38e-15

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 72.86  E-value: 3.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   46 GIGPGVRVLDVAAGSGNIS---LPAAKTGATVISTDLTPELLQRSQARAAQQG-LTLQYQEANAQALPFADDEFDTVISA 121
Cdd:pfam01209  39 GVKRGNKFLDVAGGTGDWTfglSDSAGSSGKVVGLDINENMLKEGEKKAKEEGkYNIEFLQGNAEELPFEDDSFDIVTIS 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489502404  122 IGVMFAPDHQAAADELVRVCRPGGTIGVISW---TCEG--------------FFGRMLA 163
Cdd:pfam01209 119 FGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFskpENPLlsqayelyfkyvmpFMGKMFA 177
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 47-151 1.24e-13

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 66.67  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   47 IGPGVRVLDVAAGSGNISLPAAK---TGATVISTDLTPELLQRSQARAAQQGLT-LQYQEANAQALP--FADDEFDTVIS 120
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 489502404  121 AIGVMFAPDHQAAADELVRVCRPGGTIGVIS 151
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISD 111
arsM PRK11873
arsenite methyltransferase;
43-149 6.16e-13

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 66.90  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  43 AAAGIGPGVRVLDVAAGSGNISLPAA-KTGAT--VISTDLTPELLQRSQARAAQQGLT-LQYQEANAQALPFADDEFDTV 118
Cdd:PRK11873  71 ALAELKPGETVLDLGSGGGFDCFLAArRVGPTgkVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIEALPVADNSVDVI 150

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489502404 119 ISAIGVMFAPDHQAAADELVRVCRPGGTIGV 149
Cdd:PRK11873 151 ISNCVINLSPDKERVFKEAFRVLKPGGRFAI 181
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 41-149 2.02e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 60.71  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  41 LVAAAGIGPGVRVLDVAAGSGNISLPAAK-TGATVISTDLTPELLQRSQARAAQQGLT--LQYQEANAQALPfADDEFDT 117
Cdd:COG2230   43 ILRKLGLKPGMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLADYRDLP-ADGQFDA 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489502404 118 VISaIGVMFA---PDHQAAADELVRVCRPGGTIGV 149
Cdd:COG2230  122 IVS-IGMFEHvgpENYPAYFAKVARLLKPGGRLLL 155
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 53-147 3.21e-11

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 62.08  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  53 VLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQgltlQYQEANAQALPFADDEFDTVISAIGVMFAPDHQA 132
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD----HYLAGDIESLPLATATFDLAWSNLAVQWCGNLST 121

                         90
                 ....*....|....*
gi 489502404 133 AADELVRVCRPGGTI 147
Cdd:PRK10258 122 ALRELYRVVRPGGVV 136
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
49-147 1.01e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.14  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  49 PGVRVLDVAAGSGNIS--LPAAKTGATVISTDLTPELLQRSQARAAQqgltLQYQEANAQALPFaDDEFDTVISAIGVMF 126
Cdd:COG4106    1 PPRRVLDLGCGTGRLTalLAERFPGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLDP-PEPFDLVVSNAALHW 75

                         90       100
                 ....*....|....*....|.
gi 489502404 127 APDHQAAADELVRVCRPGGTI 147
Cdd:COG4106   76 LPDHAALLARLAAALAPGGVL 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
25-145 1.39e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.86  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  25 DYALMAE---EVMAPLGPILVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLqrsqARAAQQGLTLQYQ 101
Cdd:COG4976   19 DAALVEDlgyEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEML----AKAREKGVYDRLL 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489502404 102 EANAQALPFADDEFDTVISAIGVMFAPDHQAAADELVRVCRPGG 145
Cdd:COG4976   95 VADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGG 138
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-191 5.31e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.62  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  49 PGVRVLDVAAGSGNISLP-AAKTGATVISTDLTPELLQRSQARAAQQGLT-LQYQEAN-AQALPFADDEFDTVIS--AIG 123
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLAlAARFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADlAELDPLPAESFDLVVAfgVLH 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502404 124 VMFAPDHQAAADELVRVCRPGGTIGVISWtcegFFGRMLATIRPYRPSVSADLPPSALWGREAYVTGL 191
Cdd:COG0500  106 HLPPEEREALLRELARALKPGGVLLLSAS----DAAAALSLARLLLLATASLLELLLLLRLLALELYL 169
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 52-154 1.54e-09

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: 54.36  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  52 RVLDVAAGSGNISLPAAKT-GATVISTDLTPELLQRS-QARAAQQGLTLQYQEANA-QALPFADDEFDTVISAIGVM-FA 127
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELArKAAAALLADNVEVLKGDAeELPPEADESFDVIISDPPLHhLV 80

                         90       100
                 ....*....|....*....|....*..
gi 489502404 128 PDHQAAADELVRVCRPGGTIGVISWTC 154
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLVLA 107
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 49-150 3.93e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 53.36  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  49 PGVRVLDVAAGSGNISLPAAKT--GATVISTDLTPELLQRSQARAAQQGLTLQyqEANAQALPFADDEFDTVISAIGVMF 126
Cdd:PLN02490 113 RNLKVVDVGGGTGFTTLGIVKHvdAKNVTILDQSPHQLAKAKQKEPLKECKII--EGDAEDLPFPTDYADRYVSAGSIEY 190

                         90       100
                 ....*....|....*....|....
gi 489502404 127 APDHQAAADELVRVCRPGGTIGVI 150
Cdd:PLN02490 191 WPDPQRGIKEAYRVLKIGGKACLI 214
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 52-145 5.49e-08

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: 52.29  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   52 RVLDVAAGSGNISLPAAKTG--ATVISTDLTPELLQRSQARAAQQgltLQYQEANAQALPFADDEFDTVISAIGVMFAPD 129
Cdd:TIGR02072  37 SVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSEN---VQFICGDAEKLPLEDSSFDLIVSNLALQWCDD 113

                          90
                  ....*....|....*.
gi 489502404  130 HQAAADELVRVCRPGG 145
Cdd:TIGR02072 114 LSQALSELARVLKPGG 129
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 40-150 3.38e-07

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 50.27  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  40 ILVAAAGIGPGVRVLDVAAGSGNIS-LPAAKTGAT--VISTDLTPELLQRSQARAAQQGLT----LQYQEANAQALPFAD 112
Cdd:PLN02233  64 MAVSWSGAKMGDRVLDLCCGSGDLAfLLSEKVGSDgkVMGLDFSSEQLAVAASRQELKAKScyknIEWIEGDATDLPFDD 143

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489502404 113 DEFDTVISAIGVMFAPDHQAAADELVRVCRPGGTIGVI 150
Cdd:PLN02233 144 CYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSIL 181
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 40-151 3.68e-07

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: 49.18  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  40 ILVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTL-QYQEANAQALPFADDEFDTV 118
Cdd:COG1041   17 ALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDaDVIRGDARDLPLADESVDAI 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489502404 119 I--------SAIGVMfAPDH--QAAADELVRVCRPGGTIGVIS 151
Cdd:COG1041   97 VtdppygrsSKISGE-ELLElyEKALEEAARVLKPGGRVVIVT 138
PRK14968 PRK14968
putative methyltransferase; Provisional
 40-119 2.15e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 47.20  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  40 ILVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQAL--PFADDEFDT 117
Cdd:PRK14968  14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLfePFRGDKFDV 93


                 ..
gi 489502404 118 VI 119
Cdd:PRK14968  94 IL 95
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
52-149 2.38e-06

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 47.65  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  52 RVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQYQ--EANAQAL-PFADDEFDTVISAIGVMFAP 128
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQfiHCAAQDIaQHLETPVDLILFHAVLEWVA 126

                         90       100
                 ....*....|....*....|.
gi 489502404 129 DHQAAADELVRVCRPGGTIGV 149
Cdd:PRK11036 127 DPKSVLQTLWSVLRPGGALSL 147
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 54-147 3.06e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   54 LDVAAGSGNISLPAAK--TGATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDE--FDtVISAIGVM-FAP 128
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPgsFD-VVVASNVLhHLA 79

                          90
                  ....*....|....*....
gi 489502404  129 DHQAAADELVRVCRPGGTI 147
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 49-119 1.13e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 45.21  E-value: 1.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502404  49 PGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLT--LQYQEANAQALpfaDDEFDTVI 119
Cdd:PRK07580  63 TGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDLESL---LGRFDTVV 132
PRK14967 PRK14967
putative methyltransferase; Provisional
 24-120 1.14e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.43  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  24 GDYALMAEEVMAP-----LGPILVAAAGIGPGVRVLDVAAGSGNISLPAAKTGA-TVISTDLTPELLQRSQARAAQQGLT 97
Cdd:PRK14967   6 PDALLRAPGVYRPqedtqLLADALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAgSVTAVDISRRAVRSARLNALLAGVD 85

                         90       100
                 ....*....|....*....|....
gi 489502404  98 LQYQEAN-AQALPFadDEFDTVIS 120
Cdd:PRK14967  86 VDVRRGDwARAVEF--RPFDVVVS 107
PRK05785 PRK05785
hypothetical protein; Provisional
 51-151 1.49e-05

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 45.06  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  51 VRVLDVAAGSGNISLPAAK-TGATVISTDLTPELLQRS-QARAAQQGLTlqyqeanaQALPFADDEFDTVISAIGVMFAP 128
Cdd:PRK05785  53 KKVLDVAAGKGELSYHFKKvFKYYVVALDYAENMLKMNlVADDKVVGSF--------EALPFRDKSFDVVMSSFALHASD 124

                         90       100
                 ....*....|....*....|...
gi 489502404 129 DHQAAADELVRVCRpgGTIGVIS 151
Cdd:PRK05785 125 NIEKVIAEFTRVSR--KQVGFIA 145
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 42-151 1.66e-05

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 45.26  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  42 VAAAGIGPGVRVLDVAAGS-G-NISLPAAKTGATVISTDLTPELLQRSQARAAQQglTLQYQEANAQALP---FADDEFD 116
Cdd:cd08261  152 VRRAGVTAGDTVLVVGAGPiGlGVIQVAKARGARVIVVDIDDERLEFARELGADD--TINVGDEDVAARLrelTDGEGAD 229

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489502404 117 TVISAIGvmfapdHQAAADELVRVCRPGGTIGVIS 151
Cdd:cd08261  230 VVIDATG------NPASMEEAVELVAHGGRVVLVG 258
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-166 3.06e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.19  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   40 ILVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSqaraaqqGLTLQYQEANAQALPFADDEFDtVI 119
Cdd:pfam13489  13 LLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERA-------LLNVRFDQFDEQEAAVPAGKFD-VI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 489502404  120 SAIGVMFA-PDHQAAADELVRVCRPGGTIGVISWTCEGFFGRMLATIR 166
Cdd:pfam13489  85 VAREVLEHvPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWP 132
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 42-214 7.64e-05

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 43.59  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  42 VAAAGIGPGVRVLDVAAGS-GNISLPAAKT-GA-TVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFAD-DEFDT 117
Cdd:COG1063  154 VERAGVKPGDTVLVIGAGPiGLLAALAARLaGAaRVIVVDRNPERLELARELGADAVVNPREEDLVEAVRELTGgRGADV 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404 118 VISAIGvmfapdHQAAADELVRVCRPGGTIGVIswtceGFFGRMlatirpyrpsvsADLPPSALWGREAYVTGLLGDGVT 197
Cdd:COG1063  234 VIEAVG------APAALEQALDLVRPGGTVVLV-----GVPGGP------------VPIDLNALVRKELTLRGSRNYTRE 290

                        170
                 ....*....|....*..
gi 489502404 198 GLKTARGLLEVKRFDTA 214
Cdd:COG1063  291 DFPEALELLASGRIDLE 307
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 42-119 1.32e-04

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: 42.86  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  42 VAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLT-LQYQEANA-QALP--FADDEFDT 117
Cdd:COG2265  226 LEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKnVEFVAGDLeEVLPelLWGGRPDV 305


                 ..
gi 489502404 118 VI 119
Cdd:COG2265  306 VV 307
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 40-150 2.92e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 41.28  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  40 ILVAAAGIGPGVRVLDVAAGSGNISLPAAK--TGATVISTDLTPELLQRSQARAAQQGLT--LQYQEANAQALP--FADD 113
Cdd:COG4123   28 LLAAFAPVKKGGRVLDLGTGTGVIALMLAQrsPGARITGVEIQPEAAELARRNVALNGLEdrITVIHGDLKEFAaeLPPG 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489502404 114 EFDTVIS-------AIGVMFAPDHQAAA--------DELVRVC----RPGGTIGVI 150
Cdd:COG4123  108 SFDLVVSnppyfkaGSGRKSPDEARAIArhedaltlEDLIRAAarllKPGGRFALI 163
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 49-148 3.60e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 41.10  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404   49 PGVRVLDVAAGSGNISLPAAKTGAT-VISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPfaDDEFDTVISAIG---- 123
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLP--KEKADVVVANILadpl 238

                          90       100
                  ....*....|....*....|....*
gi 489502404  124 VMFAPDhqaaadeLVRVCRPGGTIG 148
Cdd:pfam06325 239 IELAPD-------IYALVKPGGYLI 256
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 45-163 5.85e-04

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 40.72  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  45 AGIGPGVRVldVAAGSGNISLPAAKTG-----ATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFAD-DEFDTV 118
Cdd:cd05278  163 AGIKPGSTV--AVIGAGPVGLCAVAGArllgaARIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELTGgRGVDCV 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489502404 119 ISAIGVmfapdhQAAADELVRVCRPGGTIGVISWTCEGFFGRMLA 163
Cdd:cd05278  241 IEAVGF------EETFEQAVKVVRPGGTIANVGVYGKPDPLPLLG 279
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 49-147 7.15e-04

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: 39.87  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  49 PGVRVLDVAAGSGNISLPAAKTGA-TVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPfADDEFDTVISAiGVMFA 127
Cdd:COG3897   70 AGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPP-AAGGFDLILGG-DVLYE 147

                         90       100
                 ....*....|....*....|.
gi 489502404 128 PDHQAA-ADELVRVCRPGGTI 147
Cdd:COG3897  148 RDLAEPlLPFLDRLAAPGGEV 168
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 40-126 7.70e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 40.31  E-value: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  40 ILVAAAGIGPGvRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQ--YQEANAQALPfadDEFDT 117
Cdd:PRK12335 112 VLEAVQTVKPG-KALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRtgLYDINSASIQ---EEYDF 187


                 ....*....
gi 489502404 118 VISAIGVMF 126
Cdd:PRK12335 188 ILSTVVLMF 196
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 41-151 1.00e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.61  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  41 LVAAAGIGPGVRVLDVAAGS-GNISLPAAKT-GATVISTDLTPELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTV 118
Cdd:cd05188  126 LRRAGVLKPGDTVLVLGAGGvGLLAAQLAKAaGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGGADVV 205

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502404 119 ISAIGvmfapdHQAAADELVRVCRPGGTIGVIS 151
Cdd:cd05188  206 IDAVG------GPETLAQALRLLRPGGRIVVVG 232
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 45-150 1.22e-03

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 39.78  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  45 AGIGPGVRVLDVAAGS-GNISLPAAKT-GAT-VISTDLTPELLQrsqaRAAQQGLTLQYQ------EANAQALP--FADD 113
Cdd:cd05285  158 AGVRPGDTVLVFGAGPiGLLTAAVAKAfGATkVVVTDIDPSRLE----FAKELGATHTVNvrtedtPESAEKIAelLGGK 233

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489502404 114 EFDTVISAIGVmfAPDHQAAadelVRVCRPGGTIGVI 150
Cdd:cd05285  234 GPDVVIECTGA--ESCIQTA----IYATRPGGTVVLV 264
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 78-152 1.54e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 38.52  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502404  78 DLTPELLQRSQARAAQQGLT----LQYQEANAQALPFADDEFDTVISAIGVMFAPDHQAAADELVRVCRPGGTIGVISW 152
Cdd:PLN02232   4 DFSSEQLAVAATRQSLKARScykcIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDF 82
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 50-145 1.75e-03

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 39.33  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  50 GVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQ--RSQARAAQQGLTLQYQEANAQALPFADDEFDTVISaigvMFA 127
Cdd:PLN02396 132 GLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKiaRLHADMDPVTSTIEYLCTTAEKLADEGRKFDAVLS----LEV 207

                         90       100
                 ....*....|....*....|..
gi 489502404 128 PDHQAAADE----LVRVCRPGG 145
Cdd:PLN02396 208 IEHVANPAEfcksLSALTIPNG 229
rADc smart00650
Ribosomal RNA adenine dimethylases;
41-122 1.88e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.26  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404    41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQAR-AAQQGLTLQYQeaNAQALPFADDEFDTVI 119
Cdd:smart00650   5 IVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKfAAADNLTVIHG--DALKFDLPKLQPYKVV 82


                   ...
gi 489502404   120 SAI 122
Cdd:smart00650  83 GNL 85
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
49-96 2.00e-03

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 39.37  E-value: 2.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489502404  49 PGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGL 96
Cdd:PRK13168 297 PGDRVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGL 344
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 47-147 3.88e-03

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 38.30  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  47 IGPGVRVLDVAAGSGNISLPAAK-TGATVISTDLTP---ELLQRSQARAAQQGLTLQYQEANAQALPFADDEFDTVIsai 122
Cdd:COG2520  178 VKPGERVLDMFAGVGPFSIPIAKrSGAKVVAIDINPdavEYLKENIRLNKVEDRVTPILGDAREVAPELEGKADRII--- 254

                         90       100
                 ....*....|....*....|....*..
gi 489502404 123 gvMFAPdHQAAA--DELVRVCRPGGTI 147
Cdd:COG2520  255 --MNLP-HSADEflDAALRALKPGGVI 278
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
41-126 5.47e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 37.02  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  41 LVAAAGIGPGVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLT-LQYQEANAQALPFaDDEFDTVI 119
Cdd:PRK11207  22 VLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDnLHTAVVDLNNLTF-DGEYDFIL 100


                 ....*..
gi 489502404 120 SAIGVMF 126
Cdd:PRK11207 101 STVVLMF 107
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 50-118 8.49e-03

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 37.14  E-value: 8.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502404  50 GVRVLDVAAGSGNISLPAAKTGATVISTDLTPELLQRSQARAAQQGLTLQYQEA---NAQALPFADDEFDTV 118
Cdd:PLN02585 145 GVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAERRAKEALAALPPEVLpkfEANDLESLSGKYDTV 216
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 45-150 9.67e-03

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 37.19  E-value: 9.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502404  45 AGIGPGVRVldVAAGSGNISLPAA-----KTGATVISTDLTPELLqrsqARAAQQGLT---LQYQEANAQALPFADDEFD 116
Cdd:cd08282  172 AGVQPGDTV--AVFGAGPVGLMAAysailRGASRVYVVDHVPERL----DLAESIGAIpidFSDGDPVEQILGLEPGGVD 245

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489502404 117 TVISAIGvMFAPDHQAAAD------ELVRVCRPGGTIGVI 150
Cdd:cd08282  246 RAVDCVG-YEARDRGGEAQpnlvlnQLIRVTRPGGGIGIV 284
 
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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