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Conserved domains on  [gi|515743581|ref|WP_017176181|]
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MULTISPECIES: O-methyltransferase [Staphylococcus]

Protein Classification

O-methyltransferase( domain architecture ID 11467877)

O-methyltransferase of the class I-like SAM-binding methyltransferase superfamily, such as catechol O-methyltransferases that can use various catechol-like compounds

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
42-209 4.64e-56

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: 175.37  E-value: 4.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  42 IKQLIRIHHSKNILEIGTAIGYSSMQFAS-VSPDISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVSNH 120
Cdd:COG4122    8 LYLLARLLGAKRILEIGTGTGYSTLWLARaLPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581 121 LYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDidivrSRNVKQMVKKVQKYNTWLMKQKNYKTNFLNM 200
Cdd:COG4122   88 PFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHGRVAD-----PARRDPSTRAIREFNEYLREDPRLESVLLPI 162

                 ....*....
gi 515743581 201 DDGLAISIK 209
Cdd:COG4122  163 GDGLLLARK 171
 
Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
42-209 4.64e-56

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: 175.37  E-value: 4.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  42 IKQLIRIHHSKNILEIGTAIGYSSMQFAS-VSPDISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVSNH 120
Cdd:COG4122    8 LYLLARLLGAKRILEIGTGTGYSTLWLARaLPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581 121 LYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDidivrSRNVKQMVKKVQKYNTWLMKQKNYKTNFLNM 200
Cdd:COG4122   88 PFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHGRVAD-----PARRDPSTRAIREFNEYLREDPRLESVLLPI 162

                 ....*....
gi 515743581 201 DDGLAISIK 209
Cdd:COG4122  163 GDGLLLARK 171
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
19-209 4.85e-22

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 89.09  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   19 IEELRFYAEEHAVPI--VDKLTLDMIKQLIRIHHSKNILEIGTAIGYSSMQFA-SVSPDISITTIERNENMIKQAKLNFK 95
Cdd:pfam01596  10 LKELREETAKLPLAPmqVSPDEGQFLGMLVKLTGAKNVLEIGVFTGYSALAMAlALPEDGKITAIDIDPEAYEIAKKFIQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   96 KFEYENQIRLIEGDALSQYDKVSN----HLYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDIDIVRSR 171
Cdd:pfam01596  90 KAGVAHKISFILGPALKVLEQLTQdkplPEFDFIFIDADKSNYPNYYERLLELLKVGGLMAIDNTLWHGKVTEPDDQEAK 169
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 515743581  172 NVkqmvkKVQKYNTWLMKQKNYKTNFLNMDDGLAISIK 209
Cdd:pfam01596 170 TQ-----RLQEFNKDLAQDPRVEISVIPVGDGITLCRK 202
PLN02476 PLN02476
O-methyltransferase
41-209 8.77e-19

O-methyltransferase


Pssm-ID: 178094  Cd Length: 278  Bit Score: 82.03  E-value: 8.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  41 MIKQLIRIHHSKNILEIGTAIGYSSMQFASVSPDIS-ITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKV-- 117
Cdd:PLN02476 109 LLAMLVQILGAERCIEVGVYTGYSSLAVALVLPESGcLVACERDSNSLEVAKRYYELAGVSHKVNVKHGLAAESLKSMiq 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581 118 --SNHLYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDIDIVRSRNVkqmvkKVQKYNTWLMKQKNYKT 195
Cdd:PLN02476 189 ngEGSSYDFAFVDADKRMYQDYFELLLQLVRVGGVIVMDNVLWHGRVADPLVNDAKTI-----SIRNFNKKLMDDKRVSI 263
                        170
                 ....*....|....
gi 515743581 196 NFLNMDDGLAISIK 209
Cdd:PLN02476 264 SMVPIGDGMTICRK 277
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
53-153 1.79e-08

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: 50.51  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  53 NILEIGTAIGYSSMQFASvSPDISITTIERNENMIKQAKLNFKKFEYENqIRLIEGDALSQYDKVSNHlYDMIFIDAA-- 130
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADES-FDVIISDPPlh 77
                         90       100
                 ....*....|....*....|....*
gi 515743581 131 --KAQSQKFFEYYTPLLKKGGLVIT 153
Cdd:cd02440   78 hlVEDLARFLEEARRLLKPGGVLVL 102
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
54-159 3.00e-04

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 40.04  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   54 ILEIGTAIGYSSMQFASVSPDISITTIERNENMIKQAKLNFKKFEYENqIRLIEGDALSQYDK-VSNHLYDMIFI----- 127
Cdd:TIGR00091  20 HLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKN-LHVLCGDANELLDKfFPDGSLSKVFLnfpdp 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 515743581  128 ------DAAKAQSQKFFEYYTPLLKKGGLV--ITDNVLYH 159
Cdd:TIGR00091  99 wpkkrhNKRRITQPHFLKEYANVLKKGGVIhfKTDNEPLF 138
 
Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
42-209 4.64e-56

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: 175.37  E-value: 4.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  42 IKQLIRIHHSKNILEIGTAIGYSSMQFAS-VSPDISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVSNH 120
Cdd:COG4122    8 LYLLARLLGAKRILEIGTGTGYSTLWLARaLPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581 121 LYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDidivrSRNVKQMVKKVQKYNTWLMKQKNYKTNFLNM 200
Cdd:COG4122   88 PFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHGRVAD-----PARRDPSTRAIREFNEYLREDPRLESVLLPI 162

                 ....*....
gi 515743581 201 DDGLAISIK 209
Cdd:COG4122  163 GDGLLLARK 171
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
19-209 4.85e-22

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 89.09  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   19 IEELRFYAEEHAVPI--VDKLTLDMIKQLIRIHHSKNILEIGTAIGYSSMQFA-SVSPDISITTIERNENMIKQAKLNFK 95
Cdd:pfam01596  10 LKELREETAKLPLAPmqVSPDEGQFLGMLVKLTGAKNVLEIGVFTGYSALAMAlALPEDGKITAIDIDPEAYEIAKKFIQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   96 KFEYENQIRLIEGDALSQYDKVSN----HLYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDIDIVRSR 171
Cdd:pfam01596  90 KAGVAHKISFILGPALKVLEQLTQdkplPEFDFIFIDADKSNYPNYYERLLELLKVGGLMAIDNTLWHGKVTEPDDQEAK 169
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 515743581  172 NVkqmvkKVQKYNTWLMKQKNYKTNFLNMDDGLAISIK 209
Cdd:pfam01596 170 TQ-----RLQEFNKDLAQDPRVEISVIPVGDGITLCRK 202
PLN02476 PLN02476
O-methyltransferase
41-209 8.77e-19

O-methyltransferase


Pssm-ID: 178094  Cd Length: 278  Bit Score: 82.03  E-value: 8.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  41 MIKQLIRIHHSKNILEIGTAIGYSSMQFASVSPDIS-ITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKV-- 117
Cdd:PLN02476 109 LLAMLVQILGAERCIEVGVYTGYSSLAVALVLPESGcLVACERDSNSLEVAKRYYELAGVSHKVNVKHGLAAESLKSMiq 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581 118 --SNHLYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFVSDIDIVRSRNVkqmvkKVQKYNTWLMKQKNYKT 195
Cdd:PLN02476 189 ngEGSSYDFAFVDADKRMYQDYFELLLQLVRVGGVIVMDNVLWHGRVADPLVNDAKTI-----SIRNFNKKLMDDKRVSI 263
                        170
                 ....*....|....
gi 515743581 196 NFLNMDDGLAISIK 209
Cdd:PLN02476 264 SMVPIGDGMTICRK 277
PLN02781 PLN02781
Probable caffeoyl-CoA O-methyltransferase
12-163 7.28e-13

Probable caffeoyl-CoA O-methyltransferase


Pssm-ID: 215417  Cd Length: 234  Bit Score: 65.22  E-value: 7.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  12 HEQLdnniEELRFYA-------EEHAVPIVDKLTLDMikqLIRIHHSKNILEIGTAIGYSSMQFASVSP-DISITTIERN 83
Cdd:PLN02781  30 HELL----KELREATvqkygnlSEMEVPVDEGLFLSM---LVKIMNAKNTLEIGVFTGYSLLTTALALPeDGRITAIDID 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  84 ENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVSNHL----YDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYH 159
Cdd:PLN02781 103 KEAYEVGLEFIKKAGVDHKINFIQSDALSALDQLLNNDpkpeFDFAFVDADKPNYVHFHEQLLKLVKVGGIIAFDNTLWF 182

                 ....
gi 515743581 160 GFVS 163
Cdd:PLN02781 183 GFVA 186
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
55-156 1.62e-11

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 58.86  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   55 LEIGTAIGYSSMQFASVSPD---ISITTIERNEnMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVSNHLYDMIFIDA-- 129
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDnglGRLTAVDPDP-GAEEAGALLRKAGLDDRVRLIVGDSREALPSLADGPIDLLFIDGdh 79
                          90       100
                  ....*....|....*....|....*..
gi 515743581  130 AKAQSQKFFEYYTPLLKKGGLVITDNV 156
Cdd:pfam13578  80 TYEAVLNDLELWLPRLAPGGVILFHDI 106
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
45-126 1.55e-08

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: 52.84  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  45 LIRIHHSKNILEIGTAIGYSSMQFASVSPDISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVSNHLYDM 124
Cdd:COG4123   32 FAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDL 111

                 ..
gi 515743581 125 IF 126
Cdd:COG4123  112 VV 113
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
53-153 1.79e-08

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: 50.51  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  53 NILEIGTAIGYSSMQFASvSPDISITTIERNENMIKQAKLNFKKFEYENqIRLIEGDALSQYDKVSNHlYDMIFIDAA-- 130
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADES-FDVIISDPPlh 77
                         90       100
                 ....*....|....*....|....*
gi 515743581 131 --KAQSQKFFEYYTPLLKKGGLVIT 153
Cdd:cd02440   78 hlVEDLARFLEEARRLLKPGGVLVL 102
PLN02589 PLN02589
caffeoyl-CoA O-methyltransferase
42-162 1.98e-08

caffeoyl-CoA O-methyltransferase


Pssm-ID: 166230  Cd Length: 247  Bit Score: 52.69  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  42 IKQLIRIHHSKNILEIGTAIGYSSMQFASVSP-DISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKV--- 117
Cdd:PLN02589  71 LNMLLKLINAKNTMEIGVYTGYSLLATALALPeDGKILAMDINRENYELGLPVIQKAGVAHKIDFREGPALPVLDQMied 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515743581 118 -SNH-LYDMIFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVLYHGFV 162
Cdd:PLN02589 151 gKYHgTFDFIFVDADKDNYINYHKRLIDLVKVGGVIGYDNTLWNGSV 197
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
48-200 2.71e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   48 IHHSKNILEIGTAIGYSSMQFAS-VSPDISITTIERNENMIKQAKLNFKKFEYENqIRLIEGDALSQYDKVSNHLYDMIF 126
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPELLEDDKFDVVI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743581  127 IDAAKAQS---QKFFEYYTPLLKKGGLVITDnvlyhgfvsdiDIVRSRNVKQMVKKVQKYNTWLMKQKNYKTNFLNM 200
Cdd:pfam13847  80 SNCVLNHIpdpDKVLQEILRVLKPGGRLIIS-----------DPDSLAELPAHVKEDSTYYAGCVGGAILKKKLYEL 145
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
20-110 3.36e-07

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 48.55  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  20 EELRFYA-EEHAVPIVDKLTL-------DMIkQLIRIHHSKNILEIGTAIGYS----SMQFASVspdisiTTIERNENMI 87
Cdd:COG2518   29 EALRELAyADRALPIGHGQTIsqpyivaRML-EALDLKPGDRVLEIGTGSGYQaavlARLAGRV------YSVERDPELA 101
                         90       100
                 ....*....|....*....|...
gi 515743581  88 KQAKLNFKKFEYENqIRLIEGDA 110
Cdd:COG2518  102 ERARERLAALGYDN-VTVRVGDG 123
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
29-153 6.78e-07

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 47.69  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  29 HAVPI----VDKLTLDmikqLIRIHHSKNILEIGTAIGYSSMQFASVSPDISITTIERNENMIKQAKLNFKKFEYENqIR 104
Cdd:PRK08287  10 EKVPMtkeeVRALALS----KLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGN-ID 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515743581 105 LIEGDA-LSQYDKVsnhlyDMIFIDAAKAQSQKFFEYYTPLLKKGG-LVIT 153
Cdd:PRK08287  85 IIPGEApIELPGKA-----DAIFIGGSGGNLTAIIDWSLAHLHPGGrLVLT 130
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
53-130 9.80e-06

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 44.62  E-value: 9.80e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743581  53 NILEIGTAIGYSSMQFAS-VSPDISITTIERNENMIKQAKLNFKKFEYENqIRLIEGDALSQYDKvsNHLYDMIFIDAA 130
Cdd:PRK13942  79 KVLEIGTGSGYHAAVVAEiVGKSGKVVTIERIPELAEKAKKTLKKLGYDN-VEVIVGDGTLGYEE--NAPYDRIYVTAA 154
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
46-157 1.24e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 44.40  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  46 IRIHHSKNILEIGTAIGYSSMQFASVSPDIS-ITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALSQYDKVsNHLYDM 124
Cdd:PRK00377  36 LRLRKGDMILDIGCGTGSVTVEASLLVGETGkVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTI-NEKFDR 114
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515743581 125 IFIDAAKAQSQKFFEYYTPLLKKGGLVITDNVL 157
Cdd:PRK00377 115 IFIGGGSEKLKEIISASWEIIKKGGRIVIDAIL 147
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
44-169 1.32e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.51  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  44 QLIRIHHSKNILEIGTAIGYSSMQFASVSPDiSITTIERNENMIKQAKLNFKKFEYENQ-IRLIEGDALSQYDKVSNHLY 122
Cdd:COG2521  126 KLVGVRRGDRVLDTCTGLGYTAIEALKRGAR-EVITVEKDPNVLELAELNPWSRELANErIKIILGDASEVIKTFPDESF 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515743581 123 DMIFIDA---AKAQ---SQKFFEYYTPLLKKGGlvitdnVLYH------GFVSDIDIVR 169
Cdd:COG2521  205 DAIIHDPprfSLAGelySLEFYRELYRVLKPGG------RLFHytgnpgKKKRGRDVPR 257
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
53-152 2.50e-05

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 43.65  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  53 NILEIGTAIGYSSMQFASVSPDIsiTTIERNENMIKQAKLNFKKFEYENqIRLIEGD------ALSQYDKVsnhlydmIF 126
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLVRRV--FSVERIKTLQWEAKRRLKQLGLHN-VSVRHGDgwkgwpAYAPFDRI-------LV 150
                         90       100
                 ....*....|....*....|....*..
gi 515743581 127 IDAAKAQSQKFFEyytpLLKKGG-LVI 152
Cdd:PRK00312 151 TAAAPEIPRALLE----QLKEGGiLVA 173
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
54-159 3.00e-04

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 40.04  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   54 ILEIGTAIGYSSMQFASVSPDISITTIERNENMIKQAKLNFKKFEYENqIRLIEGDALSQYDK-VSNHLYDMIFI----- 127
Cdd:TIGR00091  20 HLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKN-LHVLCGDANELLDKfFPDGSLSKVFLnfpdp 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 515743581  128 ------DAAKAQSQKFFEYYTPLLKKGGLV--ITDNVLYH 159
Cdd:TIGR00091  99 wpkkrhNKRRITQPHFLKEYANVLKKGGVIhfKTDNEPLF 138
PRK04457 PRK04457
polyamine aminopropyltransferase;
52-154 3.38e-04

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 40.41  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  52 KNILEIGTAIGYSSMQFASVSPDISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDALsQYDKVSNHLYDMIFIDAAK 131
Cdd:PRK04457  68 QHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENGERFEVIEADGA-EYIAVHRHSTDVILVDGFD 146
                         90       100       110
                 ....*....|....*....|....*....|
gi 515743581 132 AQ-------SQKFFEYYTPLLKKGGLVITD 154
Cdd:PRK04457 147 GEgiidalcTQPFFDDCRNALSSDGIFVVN 176
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
54-149 8.17e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.54  E-value: 8.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581   54 ILEIGTAIGYSSMQFASvSPDISITTIERNENMIKQAKLNFKkfEYENQIRLIEGDALsQYDKVSNHlYDMIFIDAA--- 130
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAA--EAGLNVEFVQGDAE-DLPFPDGS-FDLVVSSGVlhh 75
                          90       100
                  ....*....|....*....|.
gi 515743581  131 --KAQSQKFFEYYTPLLKKGG 149
Cdd:pfam13649  76 lpDPDLEAALREIARVLKPGG 96
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
35-111 2.33e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 37.71  E-value: 2.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743581  35 DKLTLDMIKQLIR--IHHSKNILEIGTAIGYSSMqFASVSPDISITTIERNENMIKQAKLNFKKFEYENQIRLIEGDAL 111
Cdd:COG4076   18 DVERNDAFKAAIErvVKPGDVVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADAT 95
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
44-180 2.97e-03

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: 36.51  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  44 QLIRIHHSKNILEIGTAIGYSSMQFAsvSPDISITTIERNENMIKQAKLNFKKFEYenQIRLIEGDALS------QYDKV 117
Cdd:COG2226   16 AALGLRPGARVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDlpfpdgSFDLV 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743581 118 -SNHLYdMIFIDAAKAqsqkFFEYYTpLLKKGGLVItdnvlyhgfVSDIDIVRSRNVKQMVKKV 180
Cdd:COG2226   92 iSSFVL-HHLPDPERA----LAEIAR-VLKPGGRLV---------VVDFSPPDLAELEELLAEA 140
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
50-130 6.20e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 34.80  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743581  50 HSKNILEIGTAIGYSSMQFASVSPDISITTIERNENMIKQAKLNFkkfeyeNQIRLIEGDALsQYDKVSNhlYDMIFIDA 129
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL------PNVRFVVADLR-DLDPPEP--FDLVVSNA 71

                 .
gi 515743581 130 A 130
Cdd:COG4106   72 A 72
 
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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