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Conserved domains on  [gi|2473401067|gb|WEZ69580|]
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class I SAM-dependent methyltransferase [Bacillus subtilis]

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]; ...
 22-151 7.62e-35

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: 121.64  E-value: 7.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  22 YPLLGARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGVSslISFDLEDVHHLSYA 101
Cdd:COG2226     8 YDGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFP 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473401067 102 DQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPQGSHLE 151
Cdd:COG2226    85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 22-151 7.62e-35

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: 121.64  E-value: 7.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  22 YPLLGARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGVSslISFDLEDVHHLSYA 101
Cdd:COG2226     8 YDGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFP 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473401067 102 DQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPQGSHLE 151
Cdd:COG2226    85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-135 9.42e-31

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 109.58  E-value: 9.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSslISFDLEDVHHLSYADQYADFIVSYSCLHH--W 117
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpD 78

                          90
                  ....*....|....*...
gi 2473401067 118 EDVVKGLKECYRVLAPGG 135
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 30-166 8.86e-22

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 90.21  E-value: 8.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  30 SRMYSPKNKVIIDMGTGPGYLSIQLAKR--TNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLSYADQYADF 107
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAvgKTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDA 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 108 I-VSYsCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPQGSHLEIMRKqikepEYFRFV 166
Cdd:PRK00216  125 VtIAF-GLRNVPDIDKALREMYRVLKPGGRLVILEFSKPTNPPLKKAYD-----FYLFKV 178
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-145 4.49e-17

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: 77.30  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  30 SRMYSPKNKVIIDMGTGPGYLSIQLAKR--TNAHVHAVDINPAMHEIAQeeaKKSGVSSLISFDLEDVHHLSYADQYADF 107
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAKSapDRGKVTGVDFSSEMLEVAK---KKSELPLNIEFIQADAEALPFEDNSFDA 109

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2473401067 108 I-VSYScLHHWEDVVKGLKECYRVLAPGGKIVILDTFNP 145
Cdd:TIGR01934 110 VtIAFG-LRNVTDIQKALREMYRVLKPGGRLVILEFSKP 147
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-139 2.34e-16

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 72.46  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSS--LISFDLEDVHHlsYADQYADFIVSYSCLHHW 117
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNveVLKGDAEELPP--EADESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 2473401067 118 -EDVVKGLKECYRVLAPGGKIVI 139
Cdd:cd02440    80 vEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 22-151 7.62e-35

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: 121.64  E-value: 7.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  22 YPLLGARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGVSslISFDLEDVHHLSYA 101
Cdd:COG2226     8 YDGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFP 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473401067 102 DQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPQGSHLE 151
Cdd:COG2226    85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-135 9.42e-31

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 109.58  E-value: 9.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSslISFDLEDVHHLSYADQYADFIVSYSCLHH--W 117
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpD 78

                          90
                  ....*....|....*...
gi 2473401067 118 EDVVKGLKECYRVLAPGG 135
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-139 1.07e-26

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 98.89  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  41 IDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGVSSLisfdLEDVHHLSYADQYADFIVSYSCLHHWEDV 120
Cdd:pfam08241   1 LDVGCGTGLLTELLARL-GARVTGVDISPEMLELAREKAPREGLTFV----VGDAEDLPFPDNSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|....*....
gi 2473401067 121 VKGLKECYRVLAPGGKIVI 139
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 27-144 4.90e-24

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: 93.16  E-value: 4.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  27 ARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGvsslISFDLEDVHHLSYADQYAD 106
Cdd:COG2227    15 AALLARLLPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLEDGSFD 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2473401067 107 FIVSYSCLHHWEDVVKGLKECYRVLAPGGkIVILDTFN 144
Cdd:COG2227    90 LVICSEVLEHLPDPAALLRELARLLKPGG-LLLLSTPN 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-139 4.93e-22

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 88.83  E-value: 4.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLSYADQYaDFIVSYSCLHH--W 117
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQF-DAIVSIGMFEHvgP 133

                          90       100
                  ....*....|....*....|..
gi 2473401067 118 EDVVKGLKECYRVLAPGGKIVI 139
Cdd:COG2230   134 ENYPAYFAKVARLLKPGGRLLL 155
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 30-166 8.86e-22

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 90.21  E-value: 8.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  30 SRMYSPKNKVIIDMGTGPGYLSIQLAKR--TNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLSYADQYADF 107
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAvgKTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDA 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 108 I-VSYsCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPQGSHLEIMRKqikepEYFRFV 166
Cdd:PRK00216  125 VtIAF-GLRNVPDIDKALREMYRVLKPGGRLVILEFSKPTNPPLKKAYD-----FYLFKV 178
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 10-146 2.98e-21

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 88.05  E-value: 2.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  10 YKEFVDLYQSYLYPLLGARLSRMysPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSS--L 87
Cdd:COG0500     2 WDSYYSDELLPGLAALLALLERL--PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNveF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473401067  88 ISFDLEDVHHLSyaDQYADFIVSYSCLHHW--EDVVKGLKECYRVLAPGGKIVILDTFNPQ 146
Cdd:COG0500    80 LVADLAELDPLP--AESFDLVVAFGVLHHLppEEREALLRELARALKPGGVLLLSASDAAA 138
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 36-187 7.18e-21

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 85.55  E-value: 7.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  36 KNKVIIDMGTGPGYLSIQLAKR--TNAHVHAVDINPAMHEIAQEEAKKSGVSSlISFDLEDVHHL--SYADQYADFIVSY 111
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELpeLLEDDKFDVVISN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473401067 112 SCLHHWEDVVKGLKECYRVLAPGGKIVILDtFNPQGSHLEIMRkqikepEYFRFVREAFEESYSFEDIHQFVQDAG 187
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIISD-PDSLAELPAHVK------EDSTYYAGCVGGAILKKKLYELLEEAG 150
PRK08317 PRK08317
hypothetical protein; Provisional
 40-142 2.62e-20

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 86.14  E-value: 2.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNA--HVHAVDINPAMHEIAQEEAKKSGvsSLISFDLEDVHHLSYADQYADFIVSYSCLHHW 117
Cdd:PRK08317   23 VLDVGCGPGNDARELARRVGPegRVVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGLPFPDGSFDAVRSDRVLQHL 100

                          90       100
                  ....*....|....*....|....*
gi 2473401067 118 EDVVKGLKECYRVLAPGGKIVILDT 142
Cdd:PRK08317  101 EDPARALAEIARVLRPGGRVVVLDT 125
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
40-139 5.52e-19

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 79.10  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKR-TNAHVHAVDINPAMHEIAQEEAKKsgvsslISFDLEDVHHLSYADQYaDFIVSYSCLHHWE 118
Cdd:COG4106     5 VLDLGCGTGRLTALLAERfPGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEPF-DLVVSNAALHWLP 77

                          90       100
                  ....*....|....*....|.
gi 2473401067 119 DVVKGLKECYRVLAPGGKIVI 139
Cdd:COG4106    78 DHAALLARLAAALAPGGVLAV 98
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-145 4.49e-17

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: 77.30  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  30 SRMYSPKNKVIIDMGTGPGYLSIQLAKR--TNAHVHAVDINPAMHEIAQeeaKKSGVSSLISFDLEDVHHLSYADQYADF 107
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAKSapDRGKVTGVDFSSEMLEVAK---KKSELPLNIEFIQADAEALPFEDNSFDA 109

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2473401067 108 I-VSYScLHHWEDVVKGLKECYRVLAPGGKIVILDTFNP 145
Cdd:TIGR01934 110 VtIAFG-LRNVTDIQKALREMYRVLKPGGRLVILEFSKP 147
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 25-146 7.32e-17

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: 76.94  E-value: 7.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  25 LGARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRTN-AHVHAVDINPAMHEIAQEEakksgVSSLISFDLEDVHHLSYADQ 103
Cdd:TIGR02072  23 LLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPqAEFIALDISAGMLAQAKTK-----LSENVQFICGDAEKLPLEDS 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2473401067 104 YADFIVSYSCLHHWEDVVKGLKECYRVLAPGGkIVILDTFNPQ 146
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGG-LLAFSTFGPG 139
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-139 2.34e-16

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 72.46  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSS--LISFDLEDVHHlsYADQYADFIVSYSCLHHW 117
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNveVLKGDAEELPP--EADESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 2473401067 118 -EDVVKGLKECYRVLAPGGKIVI 139
Cdd:cd02440    80 vEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-137 3.25e-14

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 66.24  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  41 IDMGTGPGYLSIQLAKR-TNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLSYADQYADFIVSYSCLHHWED 119
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 2473401067 120 VVKGLKECYRVLAPGGKI 137
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
8-149 9.41e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 67.33  E-value: 9.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067   8 RTYKEFVDLYQSYLYPLLGAR---------LSRMYSPKNKVIIDMGTGPGYLSIQLAKRTnAHVHAVDINPAMheIAQee 78
Cdd:COG4976     9 ALFDQYADSYDAALVEDLGYEapallaeelLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEEM--LAK-- 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473401067  79 AKKSGVSslISFDLEDVHHLSYADQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGkIVILDTFNPQGSH 149
Cdd:COG4976    84 AREKGVY--DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGG-LFIFSVEDADGSG 151
arsM PRK11873
arsenite methyltransferase;
39-141 9.19e-12

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 63.04  E-value: 9.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  39 VIIDMGTGPGYLSIQLAKRTNA--HVHAVDINPAMHEIAQEEAKKSGVSSlISFDLEDVHHLSYADQYADFIVSYSCLHH 116
Cdd:PRK11873   80 TVLDLGSGGGFDCFLAARRVGPtgKVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVDVIISNCVINL 158

                          90       100
                  ....*....|....*....|....*
gi 2473401067 117 WEDVVKGLKECYRVLAPGGKIVILD 141
Cdd:PRK11873  159 SPDKERVFKEAFRVLKPGGRFAISD 183
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 35-96 9.34e-12

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 62.55  E-value: 9.34e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473401067  35 PKNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGVSSLISF---DLEDVH 96
Cdd:PRK07580   62 LTGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERAPEAGLAGNITFevgDLESLL 125
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 17-187 2.56e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 60.13  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  17 YQSYLYPLLGARLSRM--YSPKNKVIIDMGTGPGYLSIqLAKRTNAHVHAVDINPAMHEIAQEEAKksgvsslisFDLED 94
Cdd:pfam13489   1 YAHQRERLLADLLLRLlpKLPSPGRVLDFGCGTGIFLR-LLRAQGFSVTGVDPSPIAIERALLNVR---------FDQFD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  95 VHHLSYADQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPqgSHLEIMRKQIkepeYFRFVREAFEESY 174
Cdd:pfam13489  71 EQEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAS--DEADRLLLEW----PYLRPRNGHISLF 144

                         170
                  ....*....|...
gi 2473401067 175 SFEDIHQFVQDAG 187
Cdd:pfam13489 145 SARSLKRLLEEAG 157
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 35-167 2.65e-11

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: 61.31  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  35 PKNKVIIDMGTGPGYLSIQLAKRT-NAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLS--YADQYADFIVS- 110
Cdd:COG4123    36 KKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaeLPPGSFDLVVSn 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 111 ---------YSCL-------HH-----WEDVVKGlkeCYRVLAPGGKIVI------LDTFnpqgshLEIMRKQIKEPEYF 163
Cdd:COG4123   116 ppyfkagsgRKSPdearaiaRHedaltLEDLIRA---AARLLKPGGRFALihpaerLAEI------LAALRKYGLGPKRL 186


                  ....
gi 2473401067 164 RFVR 167
Cdd:COG4123   187 RPVH 190
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 24-189 4.95e-11

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 61.32  E-value: 4.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  24 LLGARLSRMYSPKNKVIIDMGTGPGYLSIQLAK-RTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISF---DL-EDVHhl 98
Cdd:COG2890   100 LVELALALLPAGAPPRVLDLGTGSGAIALALAKeRPDARVTAVDISPDALAVARRNAERLGLEDRVRFlqgDLfEPLP-- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  99 syADQYADFIVS---YSCLHHWEDV---VK-------------GLkECYR--------VLAPGGKIVildtfnpqgshLE 151
Cdd:COG2890   178 --GDGRFDLIVSnppYIPEDEIALLppeVRdheprlaldggedGL-DFYRriiaqaprLLKPGGWLL-----------LE 243

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2473401067 152 IMRKQIKEpeyfrfVREAFEEsYSFEDIhQFVQD-AGIP 189
Cdd:COG2890   244 IGEDQGEA------VRALLEA-AGFADV-ETHKDlAGRD 274
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 27-168 5.99e-11

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: 59.43  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  27 ARLSRMYSPKNkvIIDMGTGPGYLSIQLAK--RTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHL--SYAD 102
Cdd:COG4122     9 YLLARLLGAKR--ILEIGTGTGYSTLWLARalPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVlpRLAD 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2473401067 103 QYADFIVSysclhhweDVVKG-----LKECYRVLAPGGkIVILDTFNPQGSHLEIMRKQ---IKEPEYFRFVRE 168
Cdd:COG4122    87 GPFDLVFI--------DADKSnypdyLELALPLLRPGG-LIVADNVLWHGRVADPARRDpstRAIREFNEYLRE 151
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 34-145 4.06e-10

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 58.75  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  34 SPKNKVIIDMGTGPGYLSIQLAKRTNA-HVHAVDINPamHEIAQEEAKKS--GVSsLISFDLEDvhhLSYADQYADFIVS 110
Cdd:PLN02490  111 SDRNLKVVDVGGGTGFTTLGIVKHVDAkNVTILDQSP--HQLAKAKQKEPlkECK-IIEGDAED---LPFPTDYADRYVS 184

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2473401067 111 YSCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNP 145
Cdd:PLN02490  185 AGSIEYWPDPQRGIKEAYRVLKIGGKACLIGPVHP 219
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
40-198 6.11e-10

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 57.45  E-value: 6.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAK--RTNAHVHAVDINPAMHEIAQEEAKKSGVSSlISFDLEDVHHLSYADQYADFI-VSYScLHH 116
Cdd:pfam01209  46 FLDVAGGTGDWTFGLSDsaGSSGKVVGLDINENMLKEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVtISFG-LRN 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 117 WEDVVKGLKECYRVLAPGGKIVILDTFNPQgshLEIMRKQI----------------KEPEYFRFVREAFEESYSFEDIH 180
Cdd:pfam01209 124 FPDYLKVLKEAFRVLKPGGRVVCLEFSKPE---NPLLSQAYelyfkyvmpfmgkmfaKSYKSYQYLQESIRDFPDQKTLA 200

                         170
                  ....*....|....*...
gi 2473401067 181 QFVQDAGIPNYSLETFHF 198
Cdd:pfam01209 201 SMFEKAGFKSVGYESLTG 218
PLN02244 PLN02244
tocopherol O-methyltransferase
 35-139 1.47e-09

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 57.06  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  35 PKNkvIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLSYADQYADFIVSYSCL 114
Cdd:PLN02244  119 PKR--IVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESG 196

                          90       100
                  ....*....|....*....|....*
gi 2473401067 115 HHWEDVVKGLKECYRVLAPGGKIVI 139
Cdd:PLN02244  197 EHMPDKRKFVQELARVAAPGGRIII 221
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 26-139 6.76e-09

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: 54.04  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  26 GAR--LSRMYSPKNKVIIDMGTGPGYLSIQLAKRT-NAHVHAVDINPAMHEIAQEEAKKSGVSS---LISFDLEDVHHLS 99
Cdd:COG2813    37 GTRllLEHLPEPLGGRVLDLGCGYGVIGLALAKRNpEARVTLVDVNARAVELARANAAANGLENvevLWSDGLSGVPDGS 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473401067 100 YadqyaDFIVS-----------YSCLHHWedvvkgLKECYRVLAPGGKIVI 139
Cdd:COG2813   117 F-----DLILSnppfhagravdKEVAHAL------IADAARHLRPGGELWL 156
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 9-188 1.94e-08

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: 53.71  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067   9 TYKEF-----VDLYQSYLYPLLG---ARLSRMYSPkNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAK 80
Cdd:COG2520   146 IHRENgcrfkLDVAKVYFSPRLAterLRIAELVKP-GERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIR 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  81 KSGVSSLISFDLEDVHHL-SYADQYADFIVsyscLHHWEDVVKGLKECYRVLAPGGkIVILDTFNPQGSHLEIMRKQIK- 158
Cdd:COG2520   225 LNKVEDRVTPILGDAREVaPELEGKADRII----MNLPHSADEFLDAALRALKPGG-VIHYYEIVPEEDPFERAEERIEe 299

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2473401067 159 ---------EPEYFRFVReafeeSYSfEDIHQFVQDAGI 188
Cdd:COG2520   300 aaeeagyevEILEKRRVK-----SYS-PGVYHVVVDVRV 332
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 29-189 3.02e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 52.86  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  29 LSRMYSPKNKVIIDMGTGPGYLSIQLAK-RTNAHVHAVDINPAMHEIAQEEAKKsGVSSLISFDLEDVHHLSYADQYaDF 107
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALALAKeRPDAEVTAVDISPEALAVARRNAKH-GLGARVEFLQGDWFEPLPGGRF-DL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 108 IVS---Y---SCLHHWEDVVK-------------GLkECYR--------VLAPGGKIVildtfnpqgshLEIMRKQIKEp 160
Cdd:PRK09328  179 IVSnppYipeADIHLLQPEVRdhephlalfggedGL-DFYRriieqaprYLKPGGWLL-----------LEIGYDQGEA- 245

                         170       180       190
                  ....*....|....*....|....*....|
gi 2473401067 161 eyfrfVREAFEEsYSFEDIhQFVQD-AGIP 189
Cdd:PRK09328  246 -----VRALLAA-AGFADV-ETRKDlAGRD 268
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
36-138 6.77e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 51.58  E-value: 6.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  36 KNKVIIDMGTGPGYLSIqLAKRTNA-HVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLsYADQYADFIVSySCL 114
Cdd:COG4076    35 PGDVVLDIGTGSGLLSM-LAARAGAkKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDL-DLPEKADVIIS-EML 111

                          90       100       110
                  ....*....|....*....|....*....|
gi 2473401067 115 HHW---EDVVKGL---KEcyRVLAPGGKIV 138
Cdd:COG4076   112 DTAlldEGQVPILnhaRK--RLLKPGGRII 139
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
 25-94 8.11e-08

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 50.12  E-value: 8.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473401067  25 LGARLSRMYS--PKNKVIIDMGTGPGYLSIQLAKRTNA-HVHAVDINPAMHEIAQEEAKKSGVSSLISFDLED 94
Cdd:pfam12847   1 LSKRLQAIASlvPPGSRVADIGTDHAYLPIYLVKNGIApKAIASDINEGPLEKARENIEKYGLEDRIEVRLGD 73
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
32-142 9.94e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 51.33  E-value: 9.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  32 MYSPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVhhlsYADQYADFIVS- 110
Cdd:COG2264   144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDL----LEDGPYDLVVAn 219

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2473401067 111 -YSclhhweDVVKGL-KECYRVLAPGGKIV---ILDT 142
Cdd:COG2264   220 iLA------NPLIELaPDLAALLKPGGYLIlsgILEE 250
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 29-141 1.22e-07

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 51.12  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  29 LSRMYSPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKsgvSSLISFDLEDVHHLSYADQYADFI 108
Cdd:PTZ00098   45 LSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSD---KNKIEFEANDILKKDFPENTFDMI 121

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2473401067 109 VSYSCLHH--WEDVVKGLKECYRVLAPGGKIVILD 141
Cdd:PTZ00098  122 YSRDAILHlsYADKKKLFEKCYKWLKPNGILLITD 156
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 28-140 1.25e-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: 49.95  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  28 RLSRMY-----SPKNKVIID--MGTGpgylSIQL-AKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSlISFDLEDVHHLS 99
Cdd:COG1041    13 RLARALvnlagAKEGDTVLDpfCGTG----TILIeAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473401067 100 YADQYADFIV--------SYSCLHHWEDVVKG-LKECYRVLAPGGKIVIL 140
Cdd:COG1041    88 LADESVDAIVtdppygrsSKISGEELLELYEKaLEEAARVLKPGGRVVIV 137
PRK14968 PRK14968
putative methyltransferase; Provisional
 36-86 1.64e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 49.90  E-value: 1.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473401067  36 KNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSGVSS 86
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKN-GKKVVGVDINPYAVECAKCNAKLNNIRN 72
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
32-156 1.92e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 50.54  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  32 MYSPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLIsfdledvhHLSYADQYADFIVS- 110
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNV--------YLPQGDLKADVIVAn 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 111 -YSclhhweDVVKGL-KECYRVLAPGGKIV-----------ILDTFNPQG-SHLEIMRKQ 156
Cdd:PRK00517  187 iLA------NPLLELaPDLARLLKPGGRLIlsgileeqadeVLEAYEEAGfTLDEVLERG 240
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
98-139 4.20e-07

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 48.32  E-value: 4.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2473401067  98 LSYADQYADFIVSYSCLHH--WEDVVKGLKECYRVLAPGGKIVI 139
Cdd:COG4627    40 LPFPDNSVDAIYSSHVLEHldYEEAPLALKECYRVLKPGGILRI 83
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 40-161 1.68e-06

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 47.46  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRT--NAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHlSYADQYADFIVsYSCLHHW 117
Cdd:COG2519    95 VLEAGTGSGALTLALARAVgpEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAVF-LDMPDPW 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2473401067 118 EdvvkGLKECYRVLAPGGKIVI-LDTFNpQGSHL-EIMRKQ-IKEPE 161
Cdd:COG2519   173 E----ALEAVAKALKPGGVLVAyVPTVN-QVSKLvEALRESgFTDIE 214
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 38-139 4.71e-06

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 46.64  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  38 KVIIdMGTGP-GYLSIQLAKRTNAHVHAVDINPAmheiAQEEAKKSGVSSLISFDLEDVHHLSYADQYADFIVsySCLHH 116
Cdd:COG1064   165 RVAV-IGAGGlGHLAVQIAKALGAEVIAVDRSPE----KLELARELGADHVVNSSDEDPVEAVRELTGADVVI--DTVGA 237

                          90       100
                  ....*....|....*....|...
gi 2473401067 117 WEDVVKGLkecyRVLAPGGKIVI 139
Cdd:COG1064   238 PATVNAAL----ALLRRGGRLVL 256
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 29-139 4.72e-06

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: 45.66  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  29 LSRMYSPKNKVIIDMGTGPGYLSIQLAKRT-NAHVHAVDINPAMHEIAQEEAKKSGVS--SLISFD-LEDVHHLSYadqy 104
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESpDAELTMVDINARALESARENLAANGLEngEVVASDvYSGVEDGKF---- 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2473401067 105 aDFIVS----YSCLHHWEDVVKGL-KECYRVLAPGGKIVI 139
Cdd:pfam05175 100 -DLIISnppfHAGLATTYNVAQRFiADAKRHLRPGGELWI 138
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 36-167 4.78e-06

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 45.66  E-value: 4.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  36 KNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEiaqEEAKKSGVSSLIS--FDLEDVHHLS-YADQYADFIVS-- 110
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLW---KPRNDPGVTFIQGdiRDPETLDLLEeLLGRKVDLVLSdg 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473401067 111 --YSCLHHWEDVVK--GLKE-----CYRVLAPGGkIVILDTFnpQGSHLEIMRKQIKepEYFRFVR 167
Cdd:pfam01728  98 spFISGNKVLDHLRslDLVKaalevALELLRKGG-NFVCKVF--QGEDFSELLYLLK--LGFEKVG 158
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 14-95 7.90e-06

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 45.42  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  14 VDLYQSYLYPLLGA---RLSRMYSPkNKVIIDMGTGPGYLSIQLAKRTNA-HVHAVDINPAMHEIAQEEAKKSGVSSLIS 89
Cdd:pfam02475  75 VDVAKVYWSPRLIAereRIAKLVEP-GEVVVDMFAGIGPFSIPIAKHSKArRVYAIELNPESYKYLKENIKLNKVEDVVK 153


                  ....*.
gi 2473401067  90 FDLEDV 95
Cdd:pfam02475 154 PILGDV 159
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 34-138 1.45e-05

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and 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. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 45.32  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  34 SPKNKVIIdMGTGP-GYLSIQLAKRTNAHVHAVDINPAmheiAQEEAKKSGVSSLISFDLEDVHHLSYADQ--YADFIVs 110
Cdd:cd08254   164 KPGETVLV-IGLGGlGLNAVQIAKAMGAAVIAVDIKEE----KLELAKELGADEVLNSLDDSPKDKKAAGLggGFDVIF- 237

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2473401067 111 ysclhhweDVVkGLKE----CYRVLAPGGKIV 138
Cdd:cd08254   238 --------DFV-GTQPtfedAQKAVKPGGRIV 260
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
48-140 1.73e-05

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 42.98  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  48 GYLSIQLAKRTNAHVHAVDINPAmheiAQEEAKKSGVSSLIS---FDLEDVHHLSYADQYADFIVSYSCLHhwedvvKGL 124
Cdd:pfam00107   3 GLAAIQLAKAAGAKVIAVDGSEE----KLELAKELGADHVINpkeTDLVEEIKELTGGKGVDVVFDCVGSP------ATL 72

                          90
                  ....*....|....*.
gi 2473401067 125 KECYRVLAPGGKIVIL 140
Cdd:pfam00107  73 EQALKLLRPGGRVVVV 88
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
36-96 2.37e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.74  E-value: 2.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2473401067  36 KNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVS-SLISFDLEDVH 96
Cdd:COG2263    45 EGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGVRvDFIRADVTRIP 106
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 9-141 3.15e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 44.36  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067   9 TYKEFVDLYQsylypllgarlsrmYSPKNKVIiDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAkkSGVSSLI 88
Cdd:PLN02336  254 TTKEFVDKLD--------------LKPGQKVL-DVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERA--IGRKCSV 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2473401067  89 SFDLEDVHHLSYADQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKIVILD 141
Cdd:PLN02336  317 EFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISD 369
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 24-90 1.01e-04

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: 42.73  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2473401067  24 LLGARLSRMYS-PKNKVIIDMGTGPGYLSIQLA-KRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISF 90
Cdd:TIGR00536 101 LVEKALASLISqPPILHILDLGTGSGCIALALAyEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEF 169
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
40-135 1.01e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 42.26  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNaHVHAVDINPAMHEIAQEEAKKSGVSS---LISFDLEDVH-HLsyaDQYADFIVSYSCLH 115
Cdd:PRK11036   48 VLDAGGGEGQTAIKLAELGH-QVILCDLSAEMIQRAKQAAEAKGVSDnmqFIHCAAQDIAqHL---ETPVDLILFHAVLE 123

                          90       100
                  ....*....|....*....|
gi 2473401067 116 HWEDVVKGLKECYRVLAPGG 135
Cdd:PRK11036  124 WVADPKSVLQTLWSVLRPGG 143
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 8-137 1.57e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 41.67  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067   8 RTYKEFVDLYQ---SYLYPLLGARlsrmyspKNKVIIDMGTGPGYLSIQLAKRtNAHVHAVDINPAMHEIAQEEAKKSgv 84
Cdd:PRK10258   18 AHYEQHAELQRqsaDALLAMLPQR-------KFTHVLDAGCGPGWMSRYWRER-GSQVTALDLSPPMLAQARQKDAAD-- 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2473401067  85 ssliSFDLEDVHHLSYADQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKI 137
Cdd:PRK10258   88 ----HYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 29-139 1.74e-04

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: 42.08  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  29 LSRMYSPKNKVIIDMGTGPGYLSIQLAKRT-NAHVHAVDINPAMHEIAQEEAKKSGVSslisfDLEDVHHLSYAdqyadf 107
Cdd:COG2242   240 LAKLALRPGDVLWDIGAGSGSVSIEAARLApGGRVYAIERDPERAALIRANARRFGVP-----NVEVVEGEAPE------ 308

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401067 108 ivsysCLHHWEDV----VKG--------LKECYRVLAPGGKIVI 139
Cdd:COG2242   309 -----ALADLPDPdavfIGGsggnlpeiLEACWARLRPGGRLVA 347
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 33-157 2.51e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 41.44  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  33 YSPKNKVIIDMGTGPGYLSIQLA----KRTNAHVHAVDINPAMHEIAqeeAKKSgvsSLISFDLEDVHHLSYADQYADFI 108
Cdd:PRK11088   82 LDEKATALLDIGCGEGYYTHALAdalpEITTMQLFGLDISKVAIKYA---AKRY---PQVTFCVASSHRLPFADQSLDAI 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473401067 109 VS-YS-CLHhwedvvkglKECYRVLAPGGkIVIldTFNPQGSHLEIMRKQI 157
Cdd:PRK11088  156 IRiYApCKA---------EELARVVKPGG-IVI--TVTPGPRHLFELKGLI 194
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 43-181 4.50e-04

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: 40.89  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  43 MGTGP-GYLSIQLAKRTNA-HVHAVDINPAMHEIAqeeaKKSGVSSLISFDLEDVhhlsyADQYADFIVSYSClhhweDV 120
Cdd:COG1063   168 IGAGPiGLLAALAARLAGAaRVIVVDRNPERLELA----RELGADAVVNPREEDL-----VEAVRELTGGRGA-----DV 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 121 V-------KGLKECYRVLAPGGKIVIL------DTFNPQgshlEIMRKQIK-------EPEYFRFVREAFEE-------- 172
Cdd:COG1063   234 VieavgapAALEQALDLVRPGGTVVLVgvpggpVPIDLN----ALVRKELTlrgsrnyTREDFPEALELLASgridlepl 309

                         170
                  ....*....|..
gi 2473401067 173 ---SYSFEDIHQ 181
Cdd:COG1063   310 ithRFPLDDAPE 321
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
35-137 5.00e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 40.28  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  35 PKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQE-------EAKKsgvsslISFDLEDVHHL--SYADQYA 105
Cdd:COG2521   131 RRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDPNVLELAELnpwsrelANER------IKIILGDASEVikTFPDESF 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2473401067 106 DFIVS-----------YSclhhwEDVvkgLKECYRVLAPGGKI 137
Cdd:COG2521   205 DAIIHdpprfslagelYS-----LEF---YRELYRVLKPGGRL 239
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 40-139 6.49e-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: 39.94  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDL-EDVHHLSY----ADQYADFIVSYScl 114
Cdd:pfam06325 165 VLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLpGDLPKEKAdvvvANILADPLIELA-- 242

                          90       100
                  ....*....|....*....|....*
gi 2473401067 115 hhwEDVvkglkecYRVLAPGGKIVI 139
Cdd:pfam06325 243 ---PDI-------YALVKPGGYLIL 257
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 105-149 7.05e-04

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 39.70  E-value: 7.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2473401067 105 ADFIVSYSCLHHWED--VVKGLKECYRVLAPGGKIVILDTFNPQGSH 149
Cdd:pfam00891 126 ADAYILKRVLHDWSDekCVKLLKRCYKACPAGGKVILVESLLGADPS 172
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 26-158 8.09e-04

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: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  26 GARLSRMYSPKNKVIIdMGTGP-GYLSIQLAKRTNAHVHAVDINPAMHEIaqeeAKKSGVSSLISFDLEDVHH--LSYAD 102
Cdd:cd05188   125 ALRRAGVLKPGDTVLV-LGAGGvGLLAAQLAKAAGARVIVTDRSDEKLEL----AKELGADHVIDYKEEDLEEelRLTGG 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2473401067 103 QYADFIVsysclhhweDVV---KGLKECYRVLAPGGKIVIL---DTFNPQGSHLEIMRKQIK 158
Cdd:cd05188   200 GGADVVI---------DAVggpETLAQALRLLRPGGRIVVVggtSGGPPLDDLRRLLFKELT 252
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 43-214 8.16e-04

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: 39.86  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  43 MGTGP-GYLSIQLAKRTNAHVHAVDINPAMHEIAQEEakksGVSSLISFDLEDVHHL---SYADQYADFIVSYSCLHHwe 118
Cdd:cd08261   166 VGAGPiGLGVIQVAKARGARVIVVDIDDERLEFAREL----GADDTINVGDEDVAARlreLTDGEGADVVIDATGNPA-- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067 119 dvvkGLKECYRVLAPGGKIVILD------TFNPQGSH---LEIM--RKQIKEpeyfrfvreafeesySFEDIHQFVQDAG 187
Cdd:cd08261   240 ----SMEEAVELVAHGGRVVLVGlskgpvTFPDPEFHkkeLTILgsRNATRE---------------DFPDVIDLLESGK 300

                         170       180
                  ....*....|....*....|....*..
gi 2473401067 188 IPNYSLETFHFLPEDFIESLDELEDAP 214
Cdd:cd08261   301 VDPEALITHRFPFEDVPEAFDLWEAPP 327
PRK05785 PRK05785
hypothetical protein; Provisional
 33-130 1.41e-03

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 38.90  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  33 YSPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKsgvsSLISFDledvhHLSYADQYADFIVSYS 112
Cdd:PRK05785   48 YCGRPKKVLDVAAGKGELSYHFKKVFKYYVVALDYAENMLKMNLVADDK----VVGSFE-----ALPFRDKSFDVVMSSF 118

                          90
                  ....*....|....*...
gi 2473401067 113 CLHHWEDVVKGLKECYRV 130
Cdd:PRK05785  119 ALHASDNIEKVIAEFTRV 136
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-90 1.59e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 37.55  E-value: 1.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2473401067  40 IIDMGTGPGYLSIQLA-KRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISF 90
Cdd:pfam13679  29 IVDHGAGKGYLGFILYyLKYGVRVYGIDTRAELVEKANALAQKLGFNKRMSF 80
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 29-137 1.68e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 38.90  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  29 LSRMYSPKNKVIIDMGTGPGYLSIQLAKR-TNAHVHAVDINPAMHEIAQEEakksgvssLISFDLEDVHHLSYADQYaDF 107
Cdd:PRK14103   22 LARVGAERARRVVDLGCGPGNLTRYLARRwPGAVIEALDSSPEMVAAARER--------GVDARTGDVRDWKPKPDT-DV 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2473401067 108 IVSYSCLH----HWEDVVKGLKEcyrvLAPGGKI 137
Cdd:PRK14103   93 VVSNAALQwvpeHADLLVRWVDE----LAPGSWI 122
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
30-88 2.18e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 38.34  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2473401067  30 SRMYSPKNKVIIDMGTGPGYLSIQLAKRTnAHVHAVDINPAMHEIAQEEAKKSGVSSLI 88
Cdd:PRK14896   23 EYAEDTDGDPVLEIGPGKGALTDELAKRA-KKVYAIELDPRLAEFLRDDEIAAGNVEII 80
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 40-144 2.90e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 37.95  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  40 IIDMGTGPGYLSIQLAKR--TNAHVHAVDINPAMHEIA--QEEAKKSGVSSLISFDLEDVHHLSYADQYADFIVSYSCLH 115
Cdd:PLN02233   77 VLDLCCGSGDLAFLLSEKvgSDGKVMGLDFSSEQLAVAasRQELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLR 156

                          90       100
                  ....*....|....*....|....*....
gi 2473401067 116 HWEDVVKGLKECYRVLAPGGKIVILDtFN 144
Cdd:PLN02233  157 NVVDRLKAMQEMYRVLKPGSRVSILD-FN 184
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 24-83 3.45e-03

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 38.14  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473401067  24 LLGARLSRMysPKNKVIIDMGTGPGYLSIQLA-KRTNAHVHAVDINPAMHEIAQEEAKKSG 83
Cdd:PRK14966  241 LVEAVLARL--PENGRVWDLGTGSGAVAVTVAlERPDAFVRASDISPPALETARKNAADLG 299
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 53-141 3.76e-03

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 36.13  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  53 QLAKRTNA-HVHAVDINPAMHEiAQEEAKKSGVSSLISFDLEDVHHL--SYADQYADFIVSYSClHHWEDVVKGLKECYR 129
Cdd:pfam13578  16 AALRDNGLgRLTAVDPDPGAEE-AGALLRKAGLDDRVRLIVGDSREAlpSLADGPIDLLFIDGD-HTYEAVLNDLELWLP 93

                          90
                  ....*....|..
gi 2473401067 130 VLAPGGkIVILD 141
Cdd:pfam13578  94 RLAPGG-VILFH 104
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
36-141 6.86e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 37.54  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401067  36 KNKVIIDMGTGPGYLSIQLAKRT-NAHVHAVDIN----PAMHEIAQEEAKKSGVSSLISFDLEDvhhlSYADQYADFIVS 110
Cdd:PRK06922  418 KGDTIVDVGAGGGVMLDMIEEETeDKRIYGIDISenviDTLKKKKQNEGRSWNVIKGDAINLSS----SFEKESVDTIVY 493

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401067 111 YSCLHHW-------------EDVVKGLKECYRVLAPGGKIVILD 141
Cdd:PRK06922  494 SSILHELfsyieyegkkfnhEVIKKGLQSAYEVLKPGGRIIIRD 537
PLN02781 PLN02781
Probable caffeoyl-CoA O-methyltransferase
 27-90 8.30e-03

Probable caffeoyl-CoA O-methyltransferase


Pssm-ID: 215417  Cd Length: 234  Bit Score: 36.72  E-value: 8.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2473401067  27 ARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISF 90
Cdd:PLN02781   61 SMLVKIMNAKNTLEIGVFTGYSLLTTALALPEDGRITAIDIDKEAYEVGLEFIKKAGVDHKINF 124
 
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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