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Conserved domains on  [gi|922467209|ref|XP_013633856|]
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PREDICTED: thiocyanate methyltransferase 1 isoform X1 [Brassica oleracea var. oleracea]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-185 2.33e-59

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.).


The actual alignment was detected with superfamily member pfam05724:

Pssm-ID: 473071  Cd Length: 218  Bit Score: 184.94  E-value: 2.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   48 DVVAMASPERFVVGLDISESALEKAAETYASSPKAKYFTFVKE-----------DFFTWRPNEL--FDLIFDYVVFCAIE 114
Cdd:pfam05724  51 DMVWLAEQGHFVVGVEISELAVEKFFAEAGLSPPITELSGFKEyssgnislycgDFFTLPREELgkFDLIYDRAALCALP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  115 PEMRPAWAKSMYELLKPDGE--LITLMYPITDHDGGPPY--------------KVAVSTYEDVLVPV-GFKAVSIEENPY 177
Cdd:pfam05724 131 PEMRPRYAKQMYELLPPGGRglLITLDYPQTDHEGPPFSvpaaelealfgggwKVAELEREDALVPEpRFKAWGVERLFE 210


                  ....*...
gi 922467209  178 SIATRKGK 185
Cdd:pfam05724 211 KVYVLTRK 218
 
Name Accession Description Interval E-value
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 48-185 2.33e-59

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 184.94  E-value: 2.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   48 DVVAMASPERFVVGLDISESALEKAAETYASSPKAKYFTFVKE-----------DFFTWRPNEL--FDLIFDYVVFCAIE 114
Cdd:pfam05724  51 DMVWLAEQGHFVVGVEISELAVEKFFAEAGLSPPITELSGFKEyssgnislycgDFFTLPREELgkFDLIYDRAALCALP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  115 PEMRPAWAKSMYELLKPDGE--LITLMYPITDHDGGPPY--------------KVAVSTYEDVLVPV-GFKAVSIEENPY 177
Cdd:pfam05724 131 PEMRPRYAKQMYELLPPGGRglLITLDYPQTDHEGPPFSvpaaelealfgggwKVAELEREDALVPEpRFKAWGVERLFE 210


                  ....*...
gi 922467209  178 SIATRKGK 185
Cdd:pfam05724 211 KVYVLTRK 218
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 59-136 2.91e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 58.79  E-value: 2.91e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922467209  59 VVGLDISESALEKAAETYASSPKAKYFTFVKEDFFTWRPNELFDLIFDYVVFCAIEPEMRPAWAKSMYELLKPDGELI 136
Cdd:COG2230   77 VTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-137 3.48e-06

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: 43.96  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  59 VVGLDISESALEKaAETYASSPKAKYFTFVKEDFFTWRPNElfDLIFDYVVF---CAIEPEMRPAWAKSMYELLKPDGEL 135
Cdd:cd02440   24 VTGVDISPVALEL-ARKAAAALLADNVEVLKGDAEELPPEA--DESFDVIISdppLHHLVEDLARFLEEARRLLKPGGVL 100


                 ..
gi 922467209 136 IT 137
Cdd:cd02440  101 VL 102
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 47-135 3.29e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 37.27  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209    47 ADVVAMASPERF-VVGLDISESALEKAAE-TYASS-----PKA---KYFTFVkEDFFTWRPNEL---------------- 100
Cdd:smart00138 122 AETLPKGREPDVkILATDIDLKALEKARAgIYPEReledlPKAllaRYFKEV-EDKYRVKPELKervrfakhnllaespp 200

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 922467209   101 ---FDLIFDYVVFCAIEPEMRPAWAKSMYELLKPDGEL 135
Cdd:smart00138 201 lgdFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYL 238
 
Name Accession Description Interval E-value
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 48-185 2.33e-59

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 184.94  E-value: 2.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   48 DVVAMASPERFVVGLDISESALEKAAETYASSPKAKYFTFVKE-----------DFFTWRPNEL--FDLIFDYVVFCAIE 114
Cdd:pfam05724  51 DMVWLAEQGHFVVGVEISELAVEKFFAEAGLSPPITELSGFKEyssgnislycgDFFTLPREELgkFDLIYDRAALCALP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  115 PEMRPAWAKSMYELLKPDGE--LITLMYPITDHDGGPPY--------------KVAVSTYEDVLVPV-GFKAVSIEENPY 177
Cdd:pfam05724 131 PEMRPRYAKQMYELLPPGGRglLITLDYPQTDHEGPPFSvpaaelealfgggwKVAELEREDALVPEpRFKAWGVERLFE 210


                  ....*...
gi 922467209  178 SIATRKGK 185
Cdd:pfam05724 211 KVYVLTRK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 59-133 1.02e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.73  E-value: 1.02e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922467209   59 VVGLDISESALEKAAETYASSPKAkyFTFVKEDFFTWR-PNELFDLIFDYVVFCAIEPEMRPAWAKSMYELLKPDG 133
Cdd:pfam13649  23 VTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPfPDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 59-136 2.91e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 58.79  E-value: 2.91e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922467209  59 VVGLDISESALEKAAETYASSPKAKYFTFVKEDFFTWRPNELFDLIFDYVVFCAIEPEMRPAWAKSMYELLKPDGELI 136
Cdd:COG2230   77 VTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 50-136 3.41e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.54  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  50 VAMASPERF-VVGLDISESALEKAAETYASSPKAKYfTFVKEDFFTWRPNEL--FDLIFDYVVFCAIEPEMRPAWAKSMY 126
Cdd:COG0500   42 LALAARFGGrVIGIDLSPEAIALARARAAKAGLGNV-EFLVADLAELDPLPAesFDLVVAFGVLHHLPPEEREALLRELA 120

                         90
                 ....*....|
gi 922467209 127 ELLKPDGELI 136
Cdd:COG0500  121 RALKPGGVLL 130
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
51-136 5.42e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.06  E-value: 5.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  51 AMASPERFVVGLDISESALEKAAETYASspkakyFTFVKEDFFTWRPNELFDLIFDYVVFCAIePEMRPAWAKsMYELLK 130
Cdd:COG4106   20 AERFPGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEPFDLVVSNAALHWL-PDHAALLAR-LAAALA 91


                 ....*.
gi 922467209 131 PDGELI 136
Cdd:COG4106   92 PGGVLA 97
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-135 3.42e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.98  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   45 RCADVVAMASPERFVVGLDISESALEKAAETYASspkAKYFTFVKEDFFTWRPNELFDLIFDYV----VFCAIepEMRPA 120
Cdd:pfam08242   9 TLLRALLEALPGLEYTGLDISPAALEAARERLAA---LGLLNAVRVELFQLDLGELDPGSFDVVvasnVLHHL--ADPRA 83

                          90
                  ....*....|....*
gi 922467209  121 WAKSMYELLKPDGEL 135
Cdd:pfam08242  84 VLRNIRRLLKPGGVL 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 51-168 7.29e-07

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: 46.53  E-value: 7.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  51 AMASPERFVVGLDISESALEKAAETYASSPKAkyFTFVKEDFFTWR-PNELFDLIFDYVVFCAIEPemRPAWAKSMYELL 129
Cdd:COG2226   39 ALAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPfPDGSFDLVISSFVLHHLPD--PERALAEIARVL 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 922467209 130 KPDGELItlmypITDHDggPPykvAVSTYEDVLVPVGFK 168
Cdd:COG2226  115 KPGGRLV-----VVDFS--PP---DLAELEELLAEAGFE 143
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 55-147 7.96e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.64  E-value: 7.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   55 PERFVVGLDISESALEKAAETyASSPKAKYFTFVKEDFF---TWRPNELFDLIFDYVVFCAIePEMRPAWaKSMYELLKP 131
Cdd:pfam13847  27 PNAEVVGIDISEEAIEKAREN-AQKLGFDNVEFEQGDIEelpELLEDDKFDVVISNCVLNHI-PDPDKVL-QEILRVLKP 103

                          90
                  ....*....|....*.
gi 922467209  132 DGELItlmypITDHDG 147
Cdd:pfam13847 104 GGRLI-----ISDPDS 114
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
57-136 8.28e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 47.30  E-value: 8.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  57 RFVVGLDISESALEKAAEtyasspKAKYFTFVKEDFFTWR-PNELFDLI--FDyvVFCAIEpEMRPAwAKSMYELLKPDG 133
Cdd:COG4976   69 YRLTGVDLSEEMLAKARE------KGVYDRLLVADLADLAePDGRFDLIvaAD--VLTYLG-DLAAV-FAGVARALKPGG 138


                 ...
gi 922467209 134 ELI 136
Cdd:COG4976  139 LFI 141
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 59-136 3.14e-06

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: 44.62  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  59 VVGLDISESALEKAAETYASSPkakyFTFVKEDFFTW-RPNELFDLIFDYVVFCAI-EPEmrpAWAKSMYELLKPDGELI 136
Cdd:COG2227   49 VTGVDISPEALEIARERAAELN----VDFVQGDLEDLpLEDGSFDLVICSEVLEHLpDPA---ALLRELARLLKPGGLLL 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-137 3.48e-06

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: 43.96  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  59 VVGLDISESALEKaAETYASSPKAKYFTFVKEDFFTWRPNElfDLIFDYVVF---CAIEPEMRPAWAKSMYELLKPDGEL 135
Cdd:cd02440   24 VTGVDISPVALEL-ARKAAAALLADNVEVLKGDAEELPPEA--DESFDVIISdppLHHLVEDLARFLEEARRLLKPGGVL 100


                 ..
gi 922467209 136 IT 137
Cdd:cd02440  101 VL 102
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 57-137 2.67e-05

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 43.63  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  57 RFVVGLDISESALEKAAETYASSPKAKYFTFVKEDFFTW-----RPNELFDLIFdyvvfcaIEPemrPAWAKS------- 124
Cdd:COG1092  240 KSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWlrelaREGERFDLII-------LDP---PAFAKSkkdlfda 309

                         90       100
                 ....*....|....*....|...
gi 922467209 125 ----------MYELLKPDGELIT 137
Cdd:COG1092  310 qrdykdlnrlALKLLAPGGILVT 332
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-136 3.39e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.11  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   59 VVGLDISESALEKAAETYASSPkakyFTFVKEDF----FtwrPNELFDLIFDYVVFCAIEpEMRPAWaKSMYELLKPDGE 134
Cdd:pfam08241  21 VTGVDISPEMLELAREKAPREG----LTFVVGDAedlpF---PDNSFDLVLSSEVLHHVE-DPERAL-REIARVLKPGGI 91


                  ..
gi 922467209  135 LI 136
Cdd:pfam08241  92 LI 93
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 47-135 3.29e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 37.27  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209    47 ADVVAMASPERF-VVGLDISESALEKAAE-TYASS-----PKA---KYFTFVkEDFFTWRPNEL---------------- 100
Cdd:smart00138 122 AETLPKGREPDVkILATDIDLKALEKARAgIYPEReledlPKAllaRYFKEV-EDKYRVKPELKervrfakhnllaespp 200

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 922467209   101 ---FDLIFDYVVFCAIEPEMRPAWAKSMYELLKPDGEL 135
Cdd:smart00138 201 lgdFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYL 238
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 59-136 6.16e-03

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 36.10  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209   59 VVGLDISESALEKAAE-TYASSP--------KAKYFTFVKEDFFTWRPNEL-------------------FDLIFDYVVF 110
Cdd:pfam01739  66 ILATDIDLSVLEKARAgVYPEREleglpeelLRRYFEKTAGGGYTVKPEIKsmvlfeylnlldeypplgdFDVIFCRNVL 145

                          90       100
                  ....*....|....*....|....*.
gi 922467209  111 CAIEPEMRPAWAKSMYELLKPDGELI 136
Cdd:pfam01739 146 IYFDEETQRKILNRFAEKLKPGGYLF 171
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
51-136 9.20e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 35.78  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922467209  51 AMASPERFVVGLDISESALEKAAETYASSPKAKYFTFVKEDFFTWRPNELFDLIFDYVVFCA-IEPEMRPAWAKSMYELL 129
Cdd:COG4076   53 AARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVIISEMLDTAlLDEGQVPILNHARKRLL 132


                 ....*..
gi 922467209 130 KPDGELI 136
Cdd:COG4076  133 KPGGRII 139
 
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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