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Conserved domains on  [gi|19112046|ref|NP_595254|]
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methyltransferase Efm4 [Schizosaccharomyces pombe]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11227116)

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 EEF1A lysine methyltransferase 2

CATH:  1.10.150.350|3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-209 2.43e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


:

Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 81.31  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    67 RVLDLGTGNGHLLFRLLEEedtlLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDkVKFQQLDI------IKDSKFcskdw 140
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEE----LGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIeelpelLEDDKF----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112046   141 DLILDKGTFDAISLSGELLdgrplnsvyvDRVRGMLSPNGIFLITSCNWtIQELEERFTKNGFIVHSTV 209
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVL----------QEILRVLKPGGRLIISDPDS-LAELPAHVKEDSTYYAGCV 133
 
Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-209 2.43e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 81.31  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    67 RVLDLGTGNGHLLFRLLEEedtlLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDkVKFQQLDI------IKDSKFcskdw 140
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEE----LGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIeelpelLEDDKF----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112046   141 DLILDKGTFDAISLSGELLdgrplnsvyvDRVRGMLSPNGIFLITSCNWtIQELEERFTKNGFIVHSTV 209
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVL----------QEILRVLKPGGRLIISDPDS-LAELPAHVKEDSTYYAGCV 133
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 42-188 7.36e-14

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: 66.19  E-value: 7.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  42 EERIVQWLEDHIstsfrevseAAPFRVLDLGTGNGHLLFRLLEEEdtllpspCQLVGVDYSEAAIvlakNIARHRQFSDK 121
Cdd:COG2227  11 DRRLAALLARLL---------PAGGRVLDVGCGTGRLALALARRG-------ADVTGVDISPEAL----EIARERAAELN 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112046 122 VKFQQLDIIkdskfcskdwDLILDKGTFDAIsLSGELLDGRPLNSVYVDRVRGMLSPNGIFLITSCN 188
Cdd:COG2227  71 VDFVQGDLE----------DLPLEDGSFDLV-ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 67-185 2.46e-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: 2.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  67 RVLDLGTGNGHLLFRLLEEEDtllpspCQLVGVDYSEAAIVLAKNIARHRQFsDKVKFQQLDIIKdskfcskdwDLILDK 146
Cdd:cd02440   1 RVLDLGCGTGALALALASGPG------ARVTGVDISPVALELARKAAAALLA-DNVEVLKGDAEE---------LPPEAD 64

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19112046 147 GTFDAISLSGELLDGRPLNSVYVDRVRGMLSPNGIFLIT 185
Cdd:cd02440  65 ESFDVIISDPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 43-152 6.75e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.92  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   43 ERIVQWLEDHISTSfrevseaAPFRVLDLGTGNGHLLFRLLEEedtlLPSpCQLVGVDYSEAAIVLAK-NIARHrqFSDK 121
Cdd:PRK09328  94 EELVEWALEALLLK-------EPLRVLDLGTGSGAIALALAKE----RPD-AEVTAVDISPEALAVARrNAKHG--LGAR 159

                         90       100       110
                 ....*....|....*....|....*....|.
gi 19112046  122 VKFQQldiikdskfcsKDWDLILDKGTFDAI 152
Cdd:PRK09328 160 VEFLQ-----------GDWFEPLPGGRFDLI 179
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 61-196 8.77e-04

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    61 SEAAPFRVLDLGTGNGHLLFRLLEEedtlLPsPCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIIKDskFCSKDW 140
Cdd:TIGR00536 111 SQPPILHILDLGTGSGCIALALAYE----FP-NAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEP--LAGQKI 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112046   141 DLI------LDKGtfDAISLSGELL-----------DGRPLNSVYVDRVRGMLSPNGIFLITSCNWTIQELEE 196
Cdd:TIGR00536 184 DIIvsnppyIDEE--DLADLPNVVRfepllalvggdDGLNILRQIIELAPDYLKPNGFLVCEIGNWQQKSLKE 254
 
Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-209 2.43e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 81.31  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    67 RVLDLGTGNGHLLFRLLEEedtlLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDkVKFQQLDI------IKDSKFcskdw 140
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEE----LGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIeelpelLEDDKF----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112046   141 DLILDKGTFDAISLSGELLdgrplnsvyvDRVRGMLSPNGIFLITSCNWtIQELEERFTKNGFIVHSTV 209
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVL----------QEILRVLKPGGRLIISDPDS-LAELPAHVKEDSTYYAGCV 133
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 42-188 7.36e-14

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: 66.19  E-value: 7.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  42 EERIVQWLEDHIstsfrevseAAPFRVLDLGTGNGHLLFRLLEEEdtllpspCQLVGVDYSEAAIvlakNIARHRQFSDK 121
Cdd:COG2227  11 DRRLAALLARLL---------PAGGRVLDVGCGTGRLALALARRG-------ADVTGVDISPEAL----EIARERAAELN 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112046 122 VKFQQLDIIkdskfcskdwDLILDKGTFDAIsLSGELLDGRPLNSVYVDRVRGMLSPNGIFLITSCN 188
Cdd:COG2227  71 VDFVQGDLE----------DLPLEDGSFDLV-ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 67-186 9.99e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.49  E-value: 9.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  67 RVLDLGTGNGHLLFRLLEEEDtllpspCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIikdskfcsKDWDLildK 146
Cdd:COG2230  54 RVLDIGCGWGGLALYLARRYG------VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY--------RDLPA---D 116

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19112046 147 GTFDAISLSG--ELLdGRPLNSVYVDRVRGMLSPNGIFLITS 186
Cdd:COG2230 117 GQFDAIVSIGmfEHV-GPENYPAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 64-186 2.83e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 66.09  E-value: 2.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  64 APFRVLDLGTGNGHLLFRLLEEEDTllpspcQLVGVDYSEAAIVLAKNIARHRQFSdKVKFQQLDIIKDSKFCSKDWDLI 143
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARFGG------RVIGIDLSPEAIALARARAAKAGLG-NVEFLVADLAELDPLPAESFDLV 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19112046 144 LDKGTFDAISLSgelldgrpLNSVYVDRVRGMLSPNGIFLITS 186
Cdd:COG0500  99 VAFGVLHHLPPE--------EREALLRELARALKPGGVLLLSA 133
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 51-203 2.87e-12

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: 62.32  E-value: 2.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  51 DHISTSFREVSEAAPFRVLDLGTGNGHLLFRLLEEEdtllpspCQLVGVDYSEAAIVLAKniARHRQFSDKVKFQQLDIi 130
Cdd:COG2226   9 DGREALLAALGLRPGARVLDLGCGTGRLALALAERG-------ARVTGVDISPEMLELAR--ERAAEAGLNVEFVVGDA- 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112046 131 kdskfcskdWDLILDKGTFDAISLSG--ELLDGRP--LNSVYvdRVrgmLSPNGIFLITSCNW-TIQELEERFTKNGF 203
Cdd:COG2226  79 ---------EDLPFPDGSFDLVISSFvlHHLPDPEraLAEIA--RV---LKPGGRLVVVDFSPpDLAELEELLAEAGF 142
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-182 2.24e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.53  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    69 LDLGTGNGHLLFRLLEEEdtllpSPCQLVGVDYSEAAIVLAKN--IARHRQFSDKVKFQQLDIIKdskfcskdwdliLDK 146
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL-----PGLEYTGLDISPAALEAARErlAALGLLNAVRVELFQLDLGE------------LDP 63

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19112046   147 GTFDAISLSGELLDGRPLNSVyVDRVRGMLSPNGIF 182
Cdd:pfam08242  64 GSFDVVVASNVLHHLADPRAV-LRNIRRLLKPGGVL 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
64-185 2.82e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.30  E-value: 2.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  64 APFRVLDLGTGNGHLLFRLLEEedtlLPSpCQLVGVDYSEAAivlaknIARHRQFSDKVKFQQLDIikdskfcsKDWDLi 143
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAER----FPG-ARVTGVDLSPEM------LARARARLPNVRFVVADL--------RDLDP- 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19112046 144 ldKGTFDAISLSGEL--LDGRPlnsVYVDRVRGMLSPNGIFLIT 185
Cdd:COG4106  61 --PEPFDLVVSNAALhwLPDHA---ALLARLAAALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-180 1.15e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.42  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    68 VLDLGTGNGHLLFRLLEEedtllpSPCQLVGVDYSEAAIVLAKniARHRQFSDKVKFQQLDIikdskfcskdWDLILDKG 147
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR------GGARVTGVDLSPEMLERAR--ERAAEAGLNVEFVQGDA----------EDLPFPDG 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 19112046   148 TFDAISLSG--ELLDGRPLNSVyVDRVRGMLSPNG 180
Cdd:pfam13649  63 SFDLVVSSGvlHHLPDPDLEAA-LREIARVLKPGG 96
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-152 4.50e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 55.54  E-value: 4.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  43 ERIVQWledhistSFREVSEAAPFRVLDLGTGNGHLLFRLLEEedtlLPSpCQLVGVDYSEAAIVLAK-NIARHrQFSDK 121
Cdd:COG2890  98 EELVEL-------ALALLPAGAPPRVLDLGTGSGAIALALAKE----RPD-ARVTAVDISPDALAVARrNAERL-GLEDR 164

                        90       100       110
                ....*....|....*....|....*....|.
gi 19112046 122 VKFQQLDIikdskfcskdWDLILDKGTFDAI 152
Cdd:COG2890 165 VRFLQGDL----------FEPLPGDGRFDLI 185
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 67-185 2.46e-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: 2.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  67 RVLDLGTGNGHLLFRLLEEEDtllpspCQLVGVDYSEAAIVLAKNIARHRQFsDKVKFQQLDIIKdskfcskdwDLILDK 146
Cdd:cd02440   1 RVLDLGCGTGALALALASGPG------ARVTGVDISPVALELARKAAAALLA-DNVEVLKGDAEE---------LPPEAD 64

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19112046 147 GTFDAISLSGELLDGRPLNSVYVDRVRGMLSPNGIFLIT 185
Cdd:cd02440  65 ESFDVIISDPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
67-209 5.75e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.15  E-value: 5.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  67 RVLDLGTGNGHLLFRlleeedtLLPSPCQLVGVDYSEAAIVLAKniARHRQfsdkVKFQQLDIIkdskfcskdwDLILDK 146
Cdd:COG4976  49 RVLDLGCGTGLLGEA-------LRPRGYRLTGVDLSEEMLAKAR--EKGVY----DRLLVADLA----------DLAEPD 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112046 147 GTFDAISLSGELLDGRPLNSVyVDRVRGMLSPNGIFLITSCN--------WTIQELEERFTKNGFIVHSTV 209
Cdd:COG4976 106 GRFDLIVAADVLTYLGDLAAV-FAGVARALKPGGLFIFSVEDadgsgryaHSLDYVRDLLAAAGFEVPGLL 175
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 60-152 1.59e-06

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: 47.45  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  60 VSEAAPFRVLDLGTGNGHLLFRLLeeedTLLPSpCQLVGVDYSEAAIVLAK-NIARHrQFSDKVKFQQLDIikdskfcsK 138
Cdd:COG4123  33 APVKKGGRVLDLGTGTGVIALMLA----QRSPG-ARITGVEIQPEAAELARrNVALN-GLEDRITVIHGDL--------K 98

                        90
                ....*....|....
gi 19112046 139 DWDLILDKGTFDAI 152
Cdd:COG4123  99 EFAAELPPGSFDLV 112
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-184 2.63e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.58  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    69 LDLGTGNGHLLFRLLEeedtllpSPCQLVGVDYSEAAIvlakNIARHRQFSDKVKFQQLDIIkdskfcskdwDLILDKGT 148
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-------LGARVTGVDISPEML----ELAREKAPREGLTFVVGDAE----------DLPFPDNS 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19112046   149 FDAIsLSGELLDGRPLNSVYVDRVRGMLSPNGIFLI 184
Cdd:pfam08241  60 FDLV-LSSEVLHHVEDPERALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 67-207 3.75e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.50  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    67 RVLDLGTGNGHLLfrlleeeDTLLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDkvkfqqldiikdskfcSKDWDLildK 146
Cdd:pfam13489  25 RVLDFGCGTGIFL-------RLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDE----------------QEAAVP---A 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   147 GTFDAISLSgELLDGRPLNSVYVDRVRGMLSPNGIFLIT------------------------SCNWTIQELEERFTKNG 202
Cdd:pfam13489  79 GKFDVIVAR-EVLEHVPDPPALLRQIAALLKPGGLLLLStplasdeadrlllewpylrprnghISLFSARSLKRLLEEAG 157


                  ....*
gi 19112046   203 FIVHS 207
Cdd:pfam13489 158 FEVVS 162
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 43-129 4.59e-06

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 44.87  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    43 ERIVQWLEDHISTSFREVseaAPFRVLDLGTGNGHLLFRLLeeedtLLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDKV 122
Cdd:pfam13679   7 EHLAEFIAPLLKELLDEN---GPITIVDHGAGKGYLGFILY-----YLKYGVRVYGIDTRAELVEKANALAQKLGFNKRM 78


                  ....*..
gi 19112046   123 KFQQLDI 129
Cdd:pfam13679  79 SFLEGTI 85
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 43-152 6.75e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.92  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   43 ERIVQWLEDHISTSfrevseaAPFRVLDLGTGNGHLLFRLLEEedtlLPSpCQLVGVDYSEAAIVLAK-NIARHrqFSDK 121
Cdd:PRK09328  94 EELVEWALEALLLK-------EPLRVLDLGTGSGAIALALAKE----RPD-AEVTAVDISPEALAVARrNAKHG--LGAR 159

                         90       100       110
                 ....*....|....*....|....*....|.
gi 19112046  122 VKFQQldiikdskfcsKDWDLILDKGTFDAI 152
Cdd:PRK09328 160 VEFLQ-----------GDWFEPLPGGRFDLI 179
PRK14968 PRK14968
putative methyltransferase; Provisional
 67-205 6.17e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.58  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   67 RVLDLGTGNGHLLFRLLEEEdtllpspCQLVGVDYSEAAIVLAKNIARHRQFSD-KVKFQQLDI---IKDSKFcskdwDL 142
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNG-------KKVVGVDINPYAVECAKCNAKLNNIRNnGVEVIRSDLfepFRGDKF-----DV 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112046  143 IL----------DKGTFDAI--SLSGElLDGRPLNSVYVDRVRGMLSPNG-IFLITSCNWTIQELEERFTKNGFIV 205
Cdd:PRK14968  94 ILfnppylpteeEEEWDDWLnyALSGG-KDGREVIDRFLDEVGRYLKPGGrILLLQSSLTGEDEVLEYLEKLGFEA 168
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 67-184 7.74e-05

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: 42.09  E-value: 7.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046  67 RVLDLGTGNGHLLFRLLEeedtLLPSPCQLVGVDYSEAAIVLAK-NIARHRqFSDKVKFQQ---LDIIKDskfcskdwdl 142
Cdd:COG4122  19 RILEIGTGTGYSTLWLAR----ALPDDGRLTTIEIDPERAAIAReNFARAG-LADRIRLILgdaLEVLPR---------- 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19112046 143 iLDKGTFDAIslsgeLLDG-RPLNSVYVDRVRGMLSPNGIFLI 184
Cdd:COG4122  84 -LADGPFDLV-----FIDAdKSNYPDYLELALPLLRPGGLIVA 120
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 61-196 8.77e-04

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    61 SEAAPFRVLDLGTGNGHLLFRLLEEedtlLPsPCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIIKDskFCSKDW 140
Cdd:TIGR00536 111 SQPPILHILDLGTGSGCIALALAYE----FP-NAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEP--LAGQKI 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112046   141 DLI------LDKGtfDAISLSGELL-----------DGRPLNSVYVDRVRGMLSPNGIFLITSCNWTIQELEE 196
Cdd:TIGR00536 184 DIIvsnppyIDEE--DLADLPNVVRfepllalvggdDGLNILRQIIELAPDYLKPNGFLVCEIGNWQQKSLKE 254
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 65-155 1.57e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.60  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   65 PFRVLDLGTGNGHLLFRLLEEedtlLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIIkdskfcskdwDLIL 144
Cdd:PRK00216  52 GDKVLDLACGTGDLAIALAKA----VGKTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAE----------ALPF 117

                         90
                 ....*....|.
gi 19112046  145 DKGTFDAISLS 155
Cdd:PRK00216 118 PDNSFDAVTIA 128
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 29-144 3.41e-03

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: 37.31  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046    29 FNDEGE-----VWfgeEAEERIVQWLEdHISTSFREVSEAAPFRVLDLGTGNGhlLFRLLEEedtLLPSPCQLVGVDYSE 103
Cdd:pfam10294  10 EEDTGNgigghVW---DAAVVLSKYLE-MKIFKELGANNLSGLNVLELGSGTG--LVGIAVA---LLLPGASVTITDLEE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19112046   104 AAIVLAKNIARHrQFSDKVKFQQLD---IIKDSKFCSKDWDLIL 144
Cdd:pfam10294  81 ALELLKKNIELN-ALSSKVVVKVLDwgeNLPPDLFDGHPVDLIL 123
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
67-129 5.15e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 36.81  E-value: 5.15e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112046  67 RVLDLGTGNGHLLFRLleeedtLLPSPCQLVGVDYSEAAIVLAKNIArhRQFSDKVKFQQLDI 129
Cdd:COG2263  48 TVLDLGCGTGMLAIGA------ALLGAKKVVGVDIDPEALEIARENA--ERLGVRVDFIRADV 102
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 28-198 5.62e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 37.26  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   28 EFNDEG----EVWFGEeaeerivqwleDHISTS--------FREVSEAAPFRVLDLGTGNGHLLFRLLEEEDTllpspcQ 95
Cdd:PTZ00098  15 QYSDEGikayEFIFGE-----------DYISSGgieattkiLSDIELNENSKVLDIGSGLGGGCKYINEKYGA------H 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112046   96 LVGVDYSEAAIvlakNIARHR-QFSDKVKFQQLDIIKdSKFCSKDWDLILDKgtfDAIsLSGELLDGRPLnsvyVDRVRG 174
Cdd:PTZ00098  78 VHGVDICEKMV----NIAKLRnSDKNKIEFEANDILK-KDFPENTFDMIYSR---DAI-LHLSYADKKKL----FEKCYK 144

                        170       180
                 ....*....|....*....|....*
gi 19112046  175 MLSPNGIFLITS-CNWTIQELEERF 198
Cdd:PTZ00098 145 WLKPNGILLITDyCADKIENWDEEF 169
 
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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