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Conserved domains on  [gi|491149914|ref|WP_005008309|]
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methyltransferase [Acinetobacter bouvetii]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 64-182 5.00e-37

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


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 128.85  E-value: 5.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  64 PYWIFCWASGLAMAQWLLAEPHhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLEY--- 140
Cdd:COG3897   47 PFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTrlg 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491149914 141 -LDDLYKAEQVDILLAADVLYDQcnRF------FLDEFLKFAPEVWVAD 182
Cdd:COG3897  126 dWRDPPAAGGFDLILGGDVLYER--DLaepllpFLDRLAAPGGEVLIGD 172
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 64-182 5.00e-37

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


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 128.85  E-value: 5.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  64 PYWIFCWASGLAMAQWLLAEPHhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLEY--- 140
Cdd:COG3897   47 PFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTrlg 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491149914 141 -LDDLYKAEQVDILLAADVLYDQcnRF------FLDEFLKFAPEVWVAD 182
Cdd:COG3897  126 dWRDPPAAGGFDLILGGDVLYER--DLaepllpFLDRLAAPGGEVLIGD 172
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
76-159 1.03e-18

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 81.35  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  76 MAQWLLAEPhhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLE-YLDDlyKAEQVDILL 154
Cdd:PRK00517 109 CLEALEKLV--LPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNvYLPQ--GDLKADVIV 184


                 ....*...
gi 491149914 155 A---ADVL 159
Cdd:PRK00517 185 AnilANPL 192
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 78-161 8.01e-14

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 68.71  E-value: 8.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDV------KLEYLDDLyKAEQVD 151
Cdd:TIGR00406 151 EWL--EDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVsdrlqvKLIYLEQP-IEGKAD 227

                          90
                  ....*....|...
gi 491149914  152 ILLA---ADVLYD 161
Cdd:TIGR00406 228 VIVAnilAEVIKE 240
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 78-159 2.21e-12

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: 64.59  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDV----KLEYLDDLYKaEQVDIL 153
Cdd:pfam06325 153 EAL--ERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVearlEVYLPGDLPK-EKADVV 229


                  ....*....
gi 491149914  154 LA---ADVL 159
Cdd:pfam06325 230 VAnilADPL 238
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 92-185 2.52e-05

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: 42.03  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  92 VLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACR-ANADLNDVKLEYL------DDLYKAEQVDILLAADVLydQCN 164
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARkAAAALLADNVEVLkgdaeeLPPEADESFDVIISDPPL--HHL 79

                         90       100
                 ....*....|....*....|.
gi 491149914 165 RFFLDEFLKFAPEVWVADSRV 185
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVL 100
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 64-182 5.00e-37

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


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 128.85  E-value: 5.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  64 PYWIFCWASGLAMAQWLLAEPHhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLEY--- 140
Cdd:COG3897   47 PFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTrlg 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491149914 141 -LDDLYKAEQVDILLAADVLYDQcnRF------FLDEFLKFAPEVWVAD 182
Cdd:COG3897  126 dWRDPPAAGGFDLILGGDVLYER--DLaepllpFLDRLAAPGGEVLIGD 172
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
76-159 1.71e-22

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 92.16  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  76 MAQWLLAEPHhvKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDV--KLE-YLDDLYKAEQVDI 152
Cdd:COG2264  138 CLEALEKLLK--PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVedRIEvVLGDLLEDGPYDL 215

                         90
                 ....*....|
gi 491149914 153 LLA---ADVL 159
Cdd:COG2264  216 VVAnilANPL 225
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
76-159 1.03e-18

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 81.35  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  76 MAQWLLAEPhhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLE-YLDDlyKAEQVDILL 154
Cdd:PRK00517 109 CLEALEKLV--LPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNvYLPQ--GDLKADVIV 184


                 ....*...
gi 491149914 155 A---ADVL 159
Cdd:PRK00517 185 AnilANPL 192
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 78-161 8.01e-14

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 68.71  E-value: 8.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDV------KLEYLDDLyKAEQVD 151
Cdd:TIGR00406 151 EWL--EDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVsdrlqvKLIYLEQP-IEGKAD 227

                          90
                  ....*....|...
gi 491149914  152 ILLA---ADVLYD 161
Cdd:TIGR00406 228 VIVAnilAEVIKE 240
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 78-159 2.21e-12

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: 64.59  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDV----KLEYLDDLYKaEQVDIL 153
Cdd:pfam06325 153 EAL--ERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVearlEVYLPGDLPK-EKADVV 229


                  ....*....
gi 491149914  154 LA---ADVL 159
Cdd:pfam06325 230 VAnilADPL 238
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
87-141 7.25e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 59.15  E-value: 7.25e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491149914  87 VKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLEYL 141
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGVRVDFI 98
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 80-136 6.30e-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: 53.66  E-value: 6.30e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  80 LLAE--PHHVKDKVvLDFGAGSGVVAIA-AKMAGAKRVICCDIDQVSLDACRANADLNDV 136
Cdd:COG2813   40 LLLEhlPEPLGGRV-LDLGCGYGVIGLAlAKRNPEARVTLVDVNARAVELARANAAANGL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 75-160 6.64e-09

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: 52.33  E-value: 6.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  75 AMAQWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAkRVICCDIDQVSLDACRANADLNDVKLEYLD--DL-YKAEQVD 151
Cdd:COG2227   13 RLAALL--ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQGDleDLpLEDGSFD 89


                 ....*....
gi 491149914 152 ILLAADVLY 160
Cdd:COG2227   90 LVICSEVLE 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 92-159 1.37e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.64  E-value: 1.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491149914   92 VLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLEYL----DDL-YKAEQVDILLAADVL 159
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVqgdaEDLpFPDGSFDLVVSSGVL 73
PRK14968 PRK14968
putative methyltransferase; Provisional
 80-137 5.26e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 5.26e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491149914  80 LLAEPHHVKD-KVVLDFGAGSGVVAIAAKMAGaKRVICCDIDQVSLDACRANADLNDVK 137
Cdd:PRK14968  14 LLAENAVDKKgDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVECAKCNAKLNNIR 71
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 53-161 3.76e-07

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 48.48  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   53 DEVIRRIWNDTPYWIFC--WASGLAMAQWLL------AEPHHVKDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDQVs 123
Cdd:pfam10294   3 DNPGLRIEEDTGNGIGGhvWDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAvALLLPGASVTITDLEEA- 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 491149914  124 LDACRANADLN----DVKLEYLD-------DLYKAEQVDILLAADVLYD 161
Cdd:pfam10294  82 LELLKKNIELNalssKVVVKVLDwgenlppDLFDGHPVDLILAADCVYN 130
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 88-137 7.14e-07

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 49.10  E-value: 7.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491149914  88 KDKVVLDFGAGSGVVAI-AAKMAGAKrVICCDIDQVSLDACRANADLNDVK 137
Cdd:COG1867   57 REISYLDALAASGIRGLrYALEVGIK-VTLNDIDPEAVELIRENLELNGLE 106
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 76-155 7.66e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 48.62  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  76 MAQWLLAEPHHVKDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDQVSLDACRANADLN---DVKLeYLDDLYKA---E 148
Cdd:PRK09328  96 LVEWALEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEALAVARRNAKHGlgaRVEF-LQGDWFEPlpgG 174


                 ....*..
gi 491149914 149 QVDILLA 155
Cdd:PRK09328 175 RFDLIVS 181
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
85-155 8.18e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.11  E-value: 8.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  85 HHVK-DKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVK----------LEYLDDlykaEQVDIL 153
Cdd:COG4076   31 RVVKpGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSdritvinadaTDLDLP----EKADVI 106


                 ..
gi 491149914 154 LA 155
Cdd:COG4076  107 IS 108
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 70-160 2.84e-06

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: 45.37  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  70 WASGLAMAQWLLAEPHHVKDKVVLDFGAGSGVVAIAAKMAGAkRVICCDIDQVSLDACRANADLNDVKLEYL----DDL- 144
Cdd:COG2226    4 VAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGLNVEFVvgdaEDLp 82

                         90
                 ....*....|....*.
gi 491149914 145 YKAEQVDILLAADVLY 160
Cdd:COG2226   83 FPDGSFDLVISSFVLH 98
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 76-155 3.82e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 46.30  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  76 MAQWLLAEPHHVKDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDQVSLDACRANADLNDVKLE---YLDDLYKA---- 147
Cdd:COG2890  100 LVELALALLPAGAPPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDALAVARRNAERLGLEDRvrfLQGDLFEPlpgd 179


                 ....*...
gi 491149914 148 EQVDILLA 155
Cdd:COG2890  180 GRFDLIVS 187
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 77-162 9.31e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.91  E-value: 9.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  77 AQWLLAEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANAD---LNDVKLeYLDDLYK-----AE 148
Cdd:COG0500   15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAkagLGNVEF-LVADLAEldplpAE 93

                         90
                 ....*....|....
gi 491149914 149 QVDILLAADVLYDQ 162
Cdd:COG0500   94 SFDLVVAFGVLHHL 107
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 88-132 9.74e-06

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: 44.55  E-value: 9.74e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 491149914  88 KDKVVLDFGAGSGVVAIAAKMAGAkRVICCDIDQVSLDACRANAD 132
Cdd:COG1041   26 EGDTVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENLE 69
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 88-137 1.40e-05

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: 43.73  E-value: 1.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491149914   88 KDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDQVSLDACRANADLNDVK 137
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAAlAKESPDAELTMVDINARALESARENLAANGLE 81
PRK14967 PRK14967
putative methyltransferase; Provisional
 79-139 1.61e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 44.27  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491149914  79 WLLAEPHHVKDKV----VLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLE 139
Cdd:PRK14967  23 QLLADALAAEGLGpgrrVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVD 87
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
85-201 2.11e-05

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 43.38  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   85 HHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADL---------NDVKLEYLDDLYKAEQVDILLA 155
Cdd:pfam03602  38 PYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQLlglpgavlvMDALLALLRLAGKGPVFDIVFL 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 491149914  156 ----ADVLYDQCnrffLDEFLK---FAPEVWVA---DSRVKNFSHPKY-EKLDERSA 201
Cdd:pfam03602 118 dppyAKGLIEEV----LDLLAEkgwLKPNALIYvetEKRGELPEQPGNlELVREKKY 170
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 92-185 2.52e-05

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: 42.03  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  92 VLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACR-ANADLNDVKLEYL------DDLYKAEQVDILLAADVLydQCN 164
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARkAAAALLADNVEVLkgdaeeLPPEADESFDVIISDPPL--HHL 79

                         90       100
                 ....*....|....*....|.
gi 491149914 165 RFFLDEFLKFAPEVWVADSRV 185
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVL 100
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
92-160 1.75e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.42  E-value: 1.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491149914  92 VLDFGAGSGVV--AIAAKMAGAkRVICCDIDQVSLDACRAN--------ADLNDVKLEylddlykaEQVDILLAADVLY 160
Cdd:COG4106    5 VLDLGCGTGRLtaLLAERFPGA-RVTGVDLSPEMLARARARlpnvrfvvADLRDLDPP--------EPFDLVVSNAALH 74
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
76-159 2.73e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.37  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  76 MAQWLLAEPHHVKDKVVLDFGAGSGVVAIAAKMAGaKRVICCDIDQVSLDACRANADLNDVKLEYLDDL-YKAEQVDILL 154
Cdd:COG4976   34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEEMLAKAREKGVYDRLLVADLADLaEPDGRFDLIV 112


                 ....*
gi 491149914 155 AADVL 159
Cdd:COG4976  113 AADVL 117
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 92-134 5.35e-04

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 39.74  E-value: 5.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 491149914  92 VLDFGAGSGVVAI--AAKMAGAkRVICCDIDQVSLDACRANADLN 134
Cdd:COG4123   41 VLDLGTGTGVIALmlAQRSPGA-RITGVEIQPEAAELARRNVALN 84
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 91-137 5.82e-04

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 40.28  E-value: 5.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 491149914  91 VVLDFGAGSGVVAI-AAKMAGAKRVICCDIDQVSLDACRANADLNDVK 137
Cdd:PRK04338  60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLE 107
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-179 6.19e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   93 LDFGAGSGVVAIAAKMAGAkRVICCDIDQVSLDACRANADLNDVKL--EYLDDL-YKAEQVDILLAADVLydqcnrFFLD 169
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREGLTFvvGDAEDLpFPDNSFDLVLSSEVL------HHVE 73

                          90
                  ....*....|
gi 491149914  170 EFLKFAPEVW 179
Cdd:pfam08241  74 DPERALREIA 83
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 86-164 1.06e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.17  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914   86 HVKDKVVLDFGAGSGVVA--IAAKMAGAKRVICCDIDQVSLDACRANADLNDVK--------LEYLDDLYKAEQVDILLA 155
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSfeLAEELGPNAEVVGIDISEEAIEKARENAQKLGFDnvefeqgdIEELPELLEDDKFDVVIS 80


                  ....*....
gi 491149914  156 ADVLYDQCN 164
Cdd:pfam13847  81 NCVLNHIPD 89
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 71-129 1.28e-03

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. 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: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 39.14  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491149914  71 ASGLAMAQWLLAEP-----HHVK------DKVVLDFGAGS-GVVAI-AAKMAGAKRVICCDIDQVSLDACRA 129
Cdd:cd08232  137 PDGLSLRRAALAEPlavalHAVNragdlaGKRVLVTGAGPiGALVVaAARRAGAAEIVATDLADAPLAVARA 208
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 85-133 1.73e-03

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 37.75  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491149914  85 HHVKDKVVLDFGAGSGVVAIAAkmA--GAKRVICCDIDQVSLDACRANADL 133
Cdd:COG0742   38 PDIEGARVLDLFAGSGALGLEA--LsrGAASVVFVEKDRKAAAVIRKNLEK 86
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 88-182 1.79e-03

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 38.62  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  88 KDKVVLDFGAGSGV--VAIAAKmagAKRVICCDIDQVSLDACRANADLNDVKleylddlykaeQVDIlLAADVlydqcNR 165
Cdd:COG2265  233 GGERVLDLYCGVGTfaLPLARR---AKKVIGVEIVPEAVEDARENARLNGLK-----------NVEF-VAGDL-----EE 292

                         90
                 ....*....|....*..
gi 491149914 166 FFLDEFLKFAPEVWVAD 182
Cdd:COG2265  293 VLPELLWGGRPDVVVLD 309
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 90-161 1.90e-03

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


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 38.63  E-value: 1.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491149914  90 KVVLDFGAGS-G-VVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKLEYLDDLYKAEQVDILLA---ADVLYD 161
Cdd:cd05285  164 DTVLVFGAGPiGlLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPESAEKIAELLGgkgPDVVIE 240
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 87-175 1.98e-03

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


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 38.30  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491149914  87 VKD-KVVLDFGAGSGVVAIAAKMAGAKRVICCDIDQVSLDACRANADLNDVKleylddlykaEQVDILL--AADVLYDQC 163
Cdd:COG2520  178 VKPgERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIRLNKVE----------DRVTPILgdAREVAPELE 247

                         90       100
                 ....*....|....*....|.
gi 491149914 164 NRF---------FLDEFLKFA 175
Cdd:COG2520  248 GKAdriimnlphSADEFLDAA 268
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 88-144 5.39e-03

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


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 37.45  E-value: 5.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491149914  88 KDKVVLDFGAGSGVVAI-AAKMAGAKRVICCDIDQVSLDACRANAD---LNDVKL------EYLDDL 144
Cdd:COG2242  247 PGDVLWDIGAGSGSVSIeAARLAPGGRVYAIERDPERAALIRANARrfgVPNVEVvegeapEALADL 313
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 89-129 5.78e-03

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, 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. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 37.24  E-value: 5.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491149914  89 DKVVLDFGAGS-GVVAIA-AKMAGAKRVICCDIDQVSLDACRA 129
Cdd:cd08231  178 GDTVVVQGAGPlGLYAVAaAKLAGARRVIVIDGSPERLELARE 220
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 89-129 6.18e-03

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: 37.04  E-value: 6.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491149914  89 DKVVLDFGAGS-GV-VAIAAKMAGAKRVICCDIDQVSLDACRA 129
Cdd:COG1063  162 GDTVLVIGAGPiGLlAALAARLAGAARVIVVDRNPERLELARE 204
 
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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