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Conserved domains on  [gi|488093829|ref|WP_002165226|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacillus]

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]; ...
 46-166 1.11e-18

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


:

Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 79.27  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  46 LLVIGAGGGQEILSIGKQNSnlSFTGVDPSESMLQLAKKRIESEGIqnQIHFVHGTVHSLltnPL----FDAATCMLVLH 121
Cdd:COG2226   26 VLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL---PFpdgsFDLVISSFVLH 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488093829 122 FIPtikEKKELLNEISSRLKPGAPFFLSTINgVPHTSMFSAQLNA 166
Cdd:COG2226   99 HLP---DPERALAEIARVLKPGGRLVVVDFS-PPDLAELEELLAE 139
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-166 1.11e-18

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 79.27  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  46 LLVIGAGGGQEILSIGKQNSnlSFTGVDPSESMLQLAKKRIESEGIqnQIHFVHGTVHSLltnPL----FDAATCMLVLH 121
Cdd:COG2226   26 VLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL---PFpdgsFDLVISSFVLH 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488093829 122 FIPtikEKKELLNEISSRLKPGAPFFLSTINgVPHTSMFSAQLNA 166
Cdd:COG2226   99 HLP---DPERALAEIARVLKPGGRLVVVDFS-PPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-143 1.57e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.52  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   49 IGAGGGQEILSIGKQnSNLSFTGVDPSESMLQLAKKRIESEGIqnQIHFVHGTVHSL-LTNPLFDAATCMLVLHFIPtIK 127
Cdd:pfam13649   4 LGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpFPDGSFDLVVSSGVLHHLP-DP 79

                          90
                  ....*....|....*.
gi 488093829  128 EKKELLNEISSRLKPG 143
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
45-167 1.30e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 53.57  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829    45 NLLVIGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNQIHFVHGTVHSLLTNPLFDAATCMLVLHFIp 124
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHI- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 488093829   125 tiKEKKELLNEISSRLKPGAPFFLSTI--NGV-----PHTSMFSAQLNAW 167
Cdd:smart00828  81 --KDKMDLFSNISRHLKDGGHLVLADFiaNLLsaiehEETTSYLVTREEW 128
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-149 7.37e-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: 48.97  E-value: 7.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  45 NLLVIGAGGGQEILSIGKQNsNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTNPL--FDAATCMLVLHF 122
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADesFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*..
gi 488093829 123 IPTikEKKELLNEISSRLKPGAPFFLS 149
Cdd:cd02440   79 LVE--DLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 47-143 2.54e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  47 LVIGAGGGQEILSIGKQNSNLS-FTGVDPSESMLQLAKKRIESEGiqNQIHFVHGTVHSLltnPL----FDAATCMLVLH 121
Cdd:PRK08317  24 LDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGL---PFpdgsFDAVRSDRVLQ 98

                         90       100
                 ....*....|....*....|..
gi 488093829 122 FIPtikEKKELLNEISSRLKPG 143
Cdd:PRK08317  99 HLE---DPARALAEIARVLRPG 117
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-166 1.11e-18

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 79.27  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  46 LLVIGAGGGQEILSIGKQNSnlSFTGVDPSESMLQLAKKRIESEGIqnQIHFVHGTVHSLltnPL----FDAATCMLVLH 121
Cdd:COG2226   26 VLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL---PFpdgsFDLVISSFVLH 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488093829 122 FIPtikEKKELLNEISSRLKPGAPFFLSTINgVPHTSMFSAQLNA 166
Cdd:COG2226   99 HLP---DPERALAEIARVLKPGGRLVVVDFS-PPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-143 1.57e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.52  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   49 IGAGGGQEILSIGKQnSNLSFTGVDPSESMLQLAKKRIESEGIqnQIHFVHGTVHSL-LTNPLFDAATCMLVLHFIPtIK 127
Cdd:pfam13649   4 LGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpFPDGSFDLVVSSGVLHHLP-DP 79

                          90
                  ....*....|....*.
gi 488093829  128 EKKELLNEISSRLKPG 143
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-146 8.31e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 70.09  E-value: 8.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   47 LVIGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTNPL--FDAATCMLVLHFIP 124
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLN-AVRVELFQLDLGELDPgsFDVVVASNVLHHLA 79

                          90       100
                  ....*....|....*....|..
gi 488093829  125 tikEKKELLNEISSRLKPGAPF 146
Cdd:pfam08242  80 ---DPRAVLRNIRRLLKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 45-152 1.00e-15

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: 70.82  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  45 NLLVIGAGGGQeiLSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGiqnqIHFVHGTVHSL-LTNPLFDAATCMLVLHFI 123
Cdd:COG2227   27 RVLDVGCGTGR--LALALARRGADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLpLEDGSFDLVICSEVLEHL 100

                         90       100
                 ....*....|....*....|....*....
gi 488093829 124 PtikEKKELLNEISSRLKPGAPFFLSTIN 152
Cdd:COG2227  101 P---DPAALLRELARLLKPGGLLLLSTPN 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 32-149 1.15e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 69.95  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  32 FLFTTLPKENMNPNLLVIGAGGGQEILSIGKQNsNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTNPL- 110
Cdd:COG0500   16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELDPLPAe 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488093829 111 -FDAATCMLVLHFIPTIKEKKeLLNEISSRLKPGAPFFLS 149
Cdd:COG0500   94 sFDLVVAFGVLHHLPPEEREA-LLRELARALKPGGVLLLS 132
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-148 6.51e-14

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.99  E-value: 6.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   47 LVIGAGGGQEILSIGKQNSNLsfTGVDPSESMLQLAKKRIESEGiqnqIHFVHGTVHSLltnPL----FDAATCMLVLHF 122
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARV--TGVDISPEMLELAREKAPREG----LTFVVGDAEDL---PFpdnsFDLVLSSEVLHH 71

                          90       100
                  ....*....|....*....|....*.
gi 488093829  123 IPtikEKKELLNEISSRLKPGAPFFL 148
Cdd:pfam08241  72 VE---DPERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
49-150 1.87e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 61.38  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  49 IGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIEsegiqnQIHFVHGTVHSLLTNPLFDAATCMLVLHFIPtikE 128
Cdd:COG4106    8 LGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP------NVRFVVADLRDLDPPEPFDLVVSNAALHWLP---D 78

                         90       100
                 ....*....|....*....|..
gi 488093829 129 KKELLNEISSRLKPGAPFFLST 150
Cdd:COG4106   79 HAALLARLAAALAPGGVLAVQV 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 46-150 1.65e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 60.33  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  46 LLVIGAGGGQEILSIGKQNsNLSFTGVDPSESMLQLAKKRIESEGIQNQIHFVHGTVHSLLTNPLFDAATCMLVLHFIPT 125
Cdd:COG2230   55 VLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGP 133

                         90       100
                 ....*....|....*....|....*
gi 488093829 126 iKEKKELLNEISSRLKPGAPFFLST 150
Cdd:COG2230  134 -ENYPAYFAKVARLLKPGGRLLLHT 157
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
45-167 1.30e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 53.57  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829    45 NLLVIGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNQIHFVHGTVHSLLTNPLFDAATCMLVLHFIp 124
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHI- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 488093829   125 tiKEKKELLNEISSRLKPGAPFFLSTI--NGV-----PHTSMFSAQLNAW 167
Cdd:smart00828  81 --KDKMDLFSNISRHLKDGGHLVLADFiaNLLsaiehEETTSYLVTREEW 128
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 45-189 4.16e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   45 NLLVIGAGGGQ-EILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTN---PLFDAATCMLVL 120
Cdd:pfam13847   6 RVLDLGCGTGHlSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPELledDKFDVVISNCVL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488093829  121 HFIPtikEKKELLNEISSRLKPGAPFFLSTINGVphtSMFSAQLNAWRNHMMQNQIPLEDWNRFENSFE 189
Cdd:pfam13847  85 NHIP---DPDKVLQEILRVLKPGGRLIISDPDSL---AELPAHVKEDSTYYAGCVGGAILKKKLYELLE 147
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 31-210 4.35e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 50.89  E-value: 4.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   31 HFLFTTLPKenmNPNLLVIGAGGGQEILSIGKQNSnlSFTGVDPSESMLQLAKKriesegiqNQIHFVHGTVHSLLTNPL 110
Cdd:pfam13489  14 LRLLPKLPS---PGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALL--------NVRFDQFDEQEAAVPAGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  111 FDAATCMLVLHfipTIKEKKELLNEISSRLKPGAPFFLSTINgvphtsmfsaqlNAWRNHMMqnqipLEDWnRFENSFET 190
Cdd:pfam13489  81 FDVIVAREVLE---HVPDPPALLRQIAALLKPGGLLLLSTPL------------ASDEADRL-----LLEW-PYLRPRNG 139

                         170       180
                  ....*....|....*....|
gi 488093829  191 EIFPISETNLLAIMEECGFT 210
Cdd:pfam13489 140 HISLFSARSLKRLLEEAGFE 159
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
70-174 4.71e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.15  E-value: 4.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  70 TGVDPSESMLQLAKKRiesegiQNQIHFVHGTVHSLLTNP-LFDAATCMLVLHFIPtikEKKELLNEISSRLKPGApFFL 148
Cdd:COG4976   72 TGVDLSEEMLAKAREK------GVYDRLLVADLADLAEPDgRFDLIVAADVLTYLG---DLAAVFAGVARALKPGG-LFI 141

                         90       100
                 ....*....|....*....|....*.
gi 488093829 149 STINGVPHTSMFSAQLNAWRNHMMQN 174
Cdd:COG4976  142 FSVEDADGSGRYAHSLDYVRDLLAAA 167
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-149 7.37e-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: 48.97  E-value: 7.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  45 NLLVIGAGGGQEILSIGKQNsNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTNPL--FDAATCMLVLHF 122
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADesFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*..
gi 488093829 123 IPTikEKKELLNEISSRLKPGAPFFLS 149
Cdd:cd02440   79 LVE--DLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 47-143 2.54e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  47 LVIGAGGGQEILSIGKQNSNLS-FTGVDPSESMLQLAKKRIESEGiqNQIHFVHGTVHSLltnPL----FDAATCMLVLH 121
Cdd:PRK08317  24 LDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGL---PFpdgsFDAVRSDRVLQ 98

                         90       100
                 ....*....|....*....|..
gi 488093829 122 FIPtikEKKELLNEISSRLKPG 143
Cdd:PRK08317  99 HLE---DPARALAEIARVLRPG 117
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 49-150 1.07e-06

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 47.46  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  49 IGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTNPLFDAATCMLVLHFI-PTIK 127
Cdd:PRK00121  47 IGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGLTN-LRLLCGDAVEVLLDMFPDGSLDRIYLNFPdPWPK 125

                         90       100       110
                 ....*....|....*....|....*....|.
gi 488093829 128 EK--------KELLNEISSRLKPGAPFFLST 150
Cdd:PRK00121 126 KRhhkrrlvqPEFLALYARKLKPGGEIHFAT 156
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 70-144 1.09e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 47.84  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  70 TGVDPSESMLQLAKKRIESEGIQNQIHFVHGTVHSLltnPL----FDAATcmlvLHF-IPTIKEKKELLNEISSRLKPGA 144
Cdd:PRK00216  80 VGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL---PFpdnsFDAVT----IAFgLRNVPDIDKALREMYRVLKPGG 152
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 43-150 1.72e-06

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 46.51  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   43 NPNLLVIGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLLTNPLFDAATCMLVLHF 122
Cdd:pfam02390   2 APVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQN-LRILCGNALDVLPNYFPPGSLQKIFINF 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488093829  123 -IPTIKEKK--------ELLNEISSRLKPGAPFFLST 150
Cdd:pfam02390  81 pDPWPKKRHhkrrllqpEFLKEYARVLKPGGVLHLAT 117
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
33-143 1.67e-05

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 44.57  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  33 LFTTLPKENmnpnLLVIGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNQIHFVHGTV---HSLLTNP 109
Cdd:PRK11036  37 LLAELPPRP----LRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAqdiAQHLETP 112

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488093829 110 ----LFDAatcmlVLHFiptIKEKKELLNEISSRLKPG 143
Cdd:PRK11036 113 vdliLFHA-----VLEW---VADPKSVLQTLWSVLRPG 142
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 70-221 9.26e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 42.13  E-value: 9.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  70 TGVDPSESMLQLAKKRIESEGIQNQIHFVHGTVHSLLTNplFDAATCMLVL-HFiPTiKEKKELLNEISSRLKpgAPFFL 148
Cdd:PRK07580  89 VASDISPQMVEEARERAPEAGLAGNITFEVGDLESLLGR--FDTVVCLDVLiHY-PQ-EDAARMLAHLASLTR--GSLIF 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829 149 STingVPHTSMFSAQlnawrnHMMQNQIPledwnrfENSFETEIFPISETNLLAIMEECGFtQINR-------FFTSFLI 221
Cdd:PRK07580 163 TF---APYTPLLALL------HWIGGLFP-------GPSRTTRIYPHREKGIRRALAAAGF-KVVRterissgFYFSRLL 225
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 49-150 1.73e-04

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 41.28  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829  49 IGAGGGQEILSIGKQNSNLSFTGVDPSESMLQLAKKRIESEGIQNqIHFVHGtvhslltnplfDAAtcmLVLHFIP--TI 126
Cdd:COG0220   39 IGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTN-VRLLRG-----------DAV---ELLELFPdgSL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488093829 127 KE----------KK----------ELLNEISSRLKPGAPFFLST 150
Cdd:COG0220  104 DRiylnfpdpwpKKrhhkrrlvqpEFLALLARVLKPGGELHLAT 147
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
71-209 9.74e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.96  E-value: 9.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488093829   71 GVDPSESMLQLAKKRIESEGIQNqIHFVHGTVHSLltnPLFDAATCMLVLHF-IPTIKEKKELLNEISSRLKPGAPFF-L 148
Cdd:pfam01209  72 GLDINENMLKEGEKKAKEEGKYN-IEFLQGNAEEL---PFEDDSFDIVTISFgLRNFPDYLKVLKEAFRVLKPGGRVVcL 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488093829  149 STINgvPHTSMFSAQLNAWRNHMMQNQIPLedwnrFENSFET--------EIFPISETnLLAIMEECGF 209
Cdd:pfam01209 148 EFSK--PENPLLSQAYELYFKYVMPFMGKM-----FAKSYKSyqylqesiRDFPDQKT-LASMFEKAGF 208
 
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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