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Conserved domains on  [gi|1063694696|ref|NP_175866|]
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Methyltransferase family protein [Arabidopsis thaliana]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 18294757)

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; Drosophila melanogaster tRNA N(3)-methylcytidine methyltransferase Mettl2

CATH:  2.20.25.110
EC:  2.1.1.-
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
107-230 2.76e-14

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.59  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 107 LEIGCGNGSTVLPILRgSKNITVYACDCSSDALVRTKENIDRAISSVDnFHsfCCDFSTSEFPDwvacdrcrdkfmlnhs 186
Cdd:pfam13649   2 LDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEAGLNVE-FV--QGDAEDLPFPD---------------- 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063694696 187 ggseskhciGGVDFVTLIFTLSAVPKERMPRAIKECFAVLKPGG 230
Cdd:pfam13649  62 ---------GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
COG4627 super family cl44094
Predicted SAM-depedendent methyltransferase [General function prediction only];
210-278 2.90e-03

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


The actual alignment was detected with superfamily member COG4627:

Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 37.92  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 210 VPKERMPRAIKECFAVLKPGGLL---------LFRDY-GLYDMTMLRFEPEKR-----VGFREYVRSDGTLSYFFCLDTA 274
Cdd:COG4627    59 LDYEEAPLALKECYRVLKPGGILrivvpdlehVARLYlAEYDAALDVAELRLAgpidpLGIILGERLAGLAARHSVLFRT 138

                  ....
gi 1063694696 275 RKLF 278
Cdd:COG4627   139 GFTR 142
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
107-230 2.76e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.59  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 107 LEIGCGNGSTVLPILRgSKNITVYACDCSSDALVRTKENIDRAISSVDnFHsfCCDFSTSEFPDwvacdrcrdkfmlnhs 186
Cdd:pfam13649   2 LDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEAGLNVE-FV--QGDAEDLPFPD---------------- 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063694696 187 ggseskhciGGVDFVTLIFTLSAVPKERMPRAIKECFAVLKPGG 230
Cdd:pfam13649  62 ---------GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
87-256 6.55e-14

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: 67.71  E-value: 6.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696  87 RRY-LLKEFPELVSCGENSKLLEIGCGNGSTVLPILRgsKNITVYACDCSSDALVRTKENIDRAISSVDnFHsfCCDFST 165
Cdd:COG2226     6 ARYdGREALLAALGLRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARERAAEAGLNVE-FV--VGDAED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 166 SEFPDwvacdrcrdkfmlnhsggseskhciGGVDFVTLIFTLSAVPkeRMPRAIKECFAVLKPGGLLLFRDYGLYDMTML 245
Cdd:COG2226    81 LPFPD-------------------------GSFDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
                         170
                  ....*....|.
gi 1063694696 246 RfEPEKRVGFR 256
Cdd:COG2226   134 E-ELLAEAGFE 143
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
105-234 1.75e-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: 51.66  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 105 KLLEIGCGNGSTVLPILRGsKNITVYACDCSSDALVRTKENIDRAISsvDNFHSFCCDFSTSEFPDwvacdrcrdkfmln 184
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLA--DNVEVLKGDAEELPPEA-------------- 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063694696 185 hsggseskhcIGGVDFVTLIFTLSAVPkERMPRAIKECFAVLKPGGLLLF 234
Cdd:cd02440    64 ----------DESFDVIISDPPLHHLV-EDLARFLEEARRLLKPGGVLVL 102
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
210-278 2.90e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 37.92  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 210 VPKERMPRAIKECFAVLKPGGLL---------LFRDY-GLYDMTMLRFEPEKR-----VGFREYVRSDGTLSYFFCLDTA 274
Cdd:COG4627    59 LDYEEAPLALKECYRVLKPGGILrivvpdlehVARLYlAEYDAALDVAELRLAgpidpLGIILGERLAGLAARHSVLFRT 138

                  ....
gi 1063694696 275 RKLF 278
Cdd:COG4627   139 GFTR 142
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
92-148 5.28e-03

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: 38.10  E-value: 5.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063694696  92 KEFPELVSCGENSKLLEIGCGNGSTVLPILRGSKNITVYACDCSSDALVRTKENIDR 148
Cdd:TIGR00536 104 KALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEK 160
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
107-230 2.76e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.59  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 107 LEIGCGNGSTVLPILRgSKNITVYACDCSSDALVRTKENIDRAISSVDnFHsfCCDFSTSEFPDwvacdrcrdkfmlnhs 186
Cdd:pfam13649   2 LDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEAGLNVE-FV--QGDAEDLPFPD---------------- 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063694696 187 ggseskhciGGVDFVTLIFTLSAVPKERMPRAIKECFAVLKPGG 230
Cdd:pfam13649  62 ---------GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
87-256 6.55e-14

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: 67.71  E-value: 6.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696  87 RRY-LLKEFPELVSCGENSKLLEIGCGNGSTVLPILRgsKNITVYACDCSSDALVRTKENIDRAISSVDnFHsfCCDFST 165
Cdd:COG2226     6 ARYdGREALLAALGLRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARERAAEAGLNVE-FV--VGDAED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 166 SEFPDwvacdrcrdkfmlnhsggseskhciGGVDFVTLIFTLSAVPkeRMPRAIKECFAVLKPGGLLLFRDYGLYDMTML 245
Cdd:COG2226    81 LPFPD-------------------------GSFDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
                         170
                  ....*....|.
gi 1063694696 246 RfEPEKRVGFR 256
Cdd:COG2226   134 E-ELLAEAGFE 143
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
70-274 2.95e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.55  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696  70 PWQDFHSRhssgkffKERRYLLKEFPELVSCGENSKLLEIGCGNGSTVLPiLRGSKNITVYACDCSSDALVRTKENIDRA 149
Cdd:COG0500     1 PWDSYYSD-------ELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLA-LAARFGGRVIGIDLSPEAIALARARAAKA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 150 -ISSVDnFHsfCCDFSTS-EFPDwvacdrcrdkfmlnhsggseskhciGGVDFVTLIFTLSAVPKERMPRAIKECFAVLK 227
Cdd:COG0500    73 gLGNVE-FL--VADLAELdPLPA-------------------------ESFDLVVAFGVLHHLPPEEREALLRELARALK 124
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063694696 228 PGGLLLFrdyGLYDMTMLRFEPEKRVGFREYVRSDGTLSYFFCLDTA 274
Cdd:COG0500   125 PGGVLLL---SASDAAAALSLARLLLLATASLLELLLLLRLLALELY 168
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
107-232 6.58e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.15  E-value: 6.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 107 LEIGCGNGSTVLPILRGSKNITVYACDCSSDALVRTKENIDRAissvdnfhsfccDFSTSEFPDWVACDrcrdkfmlnhs 186
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAAL------------GLLNAVRVELFQLD----------- 57
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063694696 187 ggsESKHCIGGVDFVTLIFTLSAVPKerMPRAIKECFAVLKPGGLL 232
Cdd:pfam08242  58 ---LGELDPGSFDVVVASNVLHHLAD--PRAVLRNIRRLLKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
100-237 1.53e-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: 55.02  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 100 CGENSKLLEIGCGNGSTVLPILRgsKNITVYACDCSSDALVRTKENIDRAissvdNFHSFCCDFSTSEFPDwvacdrcrd 179
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALAR--RGADVTGVDISPEALEIARERAAEL-----NVDFVQGDLEDLPLED--------- 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694696 180 kfmlnhsggseskhciGGVDFVTLIFTLSAVPKERmpRAIKECFAVLKPGGLLLFRDY 237
Cdd:COG2227    86 ----------------GSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
107-234 4.73e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 52.67  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 107 LEIGCGNGSTVLPILRgsKNITVYACDCSSDALVRTKENIDRaissvDNFHSFCCDFSTSEFPDwvacdrcrdkfmlnhs 186
Cdd:pfam08241   1 LDVGCGTGLLTELLAR--LGARVTGVDISPEMLELAREKAPR-----EGLTFVVGDAEDLPFPD---------------- 57
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063694696 187 ggsESkhciggVDFVTLIFTLSAVpkERMPRAIKECFAVLKPGGLLLF 234
Cdd:pfam08241  58 ---NS------FDLVLSSEVLHHV--EDPERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
105-234 1.75e-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: 51.66  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 105 KLLEIGCGNGSTVLPILRGsKNITVYACDCSSDALVRTKENIDRAISsvDNFHSFCCDFSTSEFPDwvacdrcrdkfmln 184
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLA--DNVEVLKGDAEELPPEA-------------- 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063694696 185 hsggseskhcIGGVDFVTLIFTLSAVPkERMPRAIKECFAVLKPGGLLLF 234
Cdd:cd02440    64 ----------DESFDVIISDPPLHHLV-EDLARFLEEARRLLKPGGVLVL 102
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
71-236 1.70e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.93  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696  71 WQDFHSRHSSGKFFKERRYL-------LKEFPELVSCGENSKLLEIGCGNGSTVLPILRgSKNITVYACDCSSDALVRTK 143
Cdd:COG2230    13 FLDPTMTYSCAYFEDPDDTLeeaqeakLDLILRKLGLKPGMRVLDIGCGWGGLALYLAR-RYGVRVTGVTLSPEQLEYAR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 144 ENIDRAISSvDNFHSFCCDFSTSEFPdwvacdrcrdkfmlnhsggseskhciGGVDFVTLIFTLSAVPKERMPRAIKECF 223
Cdd:COG2230    92 ERAAEAGLA-DRVEVRLADYRDLPAD--------------------------GQFDAIVSIGMFEHVGPENYPAYFAKVA 144
                         170
                  ....*....|...
gi 1063694696 224 AVLKPGGLLLFRD 236
Cdd:COG2230   145 RLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
83-283 1.73e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 44.34  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696  83 FFKERRYLLKEFPELVS--CGENSKLLEIGCGNGsTVLPILRGSkNITVYACDCSSDALVRTKENIDRaissvDNFHSFC 160
Cdd:pfam13489   1 YAHQRERLLADLLLRLLpkLPSPGRVLDFGCGTG-IFLRLLRAQ-GFSVTGVDPSPIAIERALLNVRF-----DQFDEQE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 161 CDFSTSEFpdwvacdrcrdkfmlnhsggseskhciggvDFVTLIFTLSAVPKerMPRAIKECFAVLKPGGLLLFRDYGly 240
Cdd:pfam13489  74 AAVPAGKF------------------------------DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPL-- 119
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1063694696 241 dmtmLRFEPEKRVGFREYVRSDGTLSYFFCLDTARKLFTDAGF 283
Cdd:pfam13489 120 ----ASDEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGF 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
102-234 1.12e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.58  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 102 ENSKLLEIGCGNGSTVLPILRGSKNITVYACDcSSDALvrtkenIDRAISSVDNFHSFCCDFSTSEFPdwvacdrcrdkf 181
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVD-LSPEM------LARARARLPNVRFVVADLRDLDPP------------ 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063694696 182 mlnhsggseskhciGGVDFVTLIFTLSAVPkeRMPRAIKECFAVLKPGGLLLF 234
Cdd:COG4106    62 --------------EPFDLVVSNAALHWLP--DHAALLARLAAALAPGGVLAV 98
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
88-234 1.07e-03

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: 39.40  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696  88 RYLLKEFPELVScgenSKLLEIGCGNG--STVLpiLRGSKNITVYACDCSSDALVRTKENIDRA-ISSVDNFHSFCCD-F 163
Cdd:COG2813    39 RLLLEHLPEPLG----GRVLDLGCGYGviGLAL--AKRNPEARVTLVDVNARAVELARANAAANgLENVEVLWSDGLSgV 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063694696 164 STSEFpDWVACdrcrdkfmlN---HSGGSESKHciggvdfVTLIFtlsavpkermpraIKECFAVLKPGGLLLF 234
Cdd:COG2813   113 PDGSF-DLILS---------NppfHAGRAVDKE-------VAHAL-------------IADAARHLRPGGELWL 156
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
210-278 2.90e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 37.92  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694696 210 VPKERMPRAIKECFAVLKPGGLL---------LFRDY-GLYDMTMLRFEPEKR-----VGFREYVRSDGTLSYFFCLDTA 274
Cdd:COG4627    59 LDYEEAPLALKECYRVLKPGGILrivvpdlehVARLYlAEYDAALDVAELRLAgpidpLGIILGERLAGLAARHSVLFRT 138

                  ....
gi 1063694696 275 RKLF 278
Cdd:COG4627   139 GFTR 142
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
92-148 5.28e-03

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: 38.10  E-value: 5.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063694696  92 KEFPELVSCGENSKLLEIGCGNGSTVLPILRGSKNITVYACDCSSDALVRTKENIDR 148
Cdd:TIGR00536 104 KALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEK 160
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
96-148 6.79e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 37.44  E-value: 6.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063694696  96 ELVSCGENSKLLEIGCGNGSTVLPILRGSKNITVYACDCSSDALVRTKENIDR 148
Cdd:COG2890   106 ALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAER 158
 
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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