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Conserved domains on  [gi|115532624|ref|NP_001040827|]
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tRNA N(3)-methylcytidine methyltransferase [Caenorhabditis elegans]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

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
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
121-224 2.67e-16

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  121 ILEVGCGVGNTTFPLLQVNNSSsrlmLHSCDYAPNAIRVLKSQDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR----VTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGV 72
                          90       100
                  ....*....|....*....|....
gi 115532624  201 LSAIHPDNIKNALKNLVRLLKPGG 224
Cdd:pfam13649  73 LHHLPDPDLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
121-224 2.67e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  121 ILEVGCGVGNTTFPLLQVNNSSsrlmLHSCDYAPNAIRVLKSQDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR----VTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGV 72
                          90       100
                  ....*....|....*....|....
gi 115532624  201 LSAIHPDNIKNALKNLVRLLKPGG 224
Cdd:pfam13649  73 LHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
121-240 6.36e-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: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSssrlmLHSCDYAPNAIRVLKSQDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:COG2226   26 VLDLGCGTGRLALALAERGAR-----VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPD----GSFDLVISSFV 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115532624 201 LSaiHPDNIKNALKNLVRLLKPGGSLLLKDYGRYDLTQLR 240
Cdd:COG2226   97 LH--HLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
121-231 7.61e-10

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: 55.51  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSSSrlmlHSCDYAPNAIRVLKSQDAYD-PEKMNAFVWDITQPASQEapnVGSLDYIVCIY 199
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARV----TGVDISPVALELARKAAAALlADNVEVLKGDAEELPPEA---DESFDVIISDP 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532624 200 VLSAIHPDnIKNALKNLVRLLKPGGSLLLKDY 231
Cdd:cd02440   75 PLHHLVED-LARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
121-224 2.67e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  121 ILEVGCGVGNTTFPLLQVNNSSsrlmLHSCDYAPNAIRVLKSQDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR----VTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGV 72
                          90       100
                  ....*....|....*....|....
gi 115532624  201 LSAIHPDNIKNALKNLVRLLKPGG 224
Cdd:pfam13649  73 LHHLPDPDLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
122-226 3.53e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 72.79  E-value: 3.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  122 LEVGCGVGNTTFPLLQVNnssSRLMLHSCDYAPNAIRV----LKSQDAYDPEKMNAFVWDITQPASqeapnvGSLDYIVC 197
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL---PGLEYTGLDISPAALEAarerLAALGLLNAVRVELFQLDLGELDP------GSFDVVVA 71
                          90       100
                  ....*....|....*....|....*....
gi 115532624  198 IYVLSaiHPDNIKNALKNLVRLLKPGGSL 226
Cdd:pfam08242  72 SNVLH--HLADPRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
85-278 1.27e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 64.76  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624   85 YAHNENRFFKDrnWLLKEFPELnvedesnlqKEKIEILEVGCGVGNTTfPLLQVNNSSsrlmLHSCDYAPNAIRVLKSQD 164
Cdd:pfam13489   1 YAHQRERLLAD--LLLRLLPKL---------PSPGRVLDFGCGTGIFL-RLLRAQGFS----VTGVDPSPIAIERALLNV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  165 AYDPEkmnafvwditqPASQEAPNVGSLDYIVCIYVLSAIHpdNIKNALKNLVRLLKPGGSLLLKDYGRydltqlRFKKD 244
Cdd:pfam13489  65 RFDQF-----------DEQEAAVPAGKFDVIVAREVLEHVP--DPPALLRQIAALLKPGGLLLLSTPLA------SDEAD 125
                         170       180       190
                  ....*....|....*....|....*....|....
gi 115532624  245 RLIDGNLYCRGDGTLVYFFDMEELETLLAEHGLQ 278
Cdd:pfam13489 126 RLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFE 159
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
121-240 6.36e-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: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSssrlmLHSCDYAPNAIRVLKSQDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:COG2226   26 VLDLGCGTGRLALALAERGAR-----VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPD----GSFDLVISSFV 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115532624 201 LSaiHPDNIKNALKNLVRLLKPGGSLLLKDYGRYDLTQLR 240
Cdd:COG2226   97 LH--HLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
116-228 1.23e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.93  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 116 KEKIEILEVGCGVGNTTFPLLQVNNSssrlMLHSCDYAPNAIRVLKSQ-DAYDPEKMNAFVWDITQPasqEAPNVGSLDY 194
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARFGG----RVIGIDLSPEAIALARARaAKAGLGNVEFLVADLAEL---DPLPAESFDL 97
                         90       100       110
                 ....*....|....*....|....*....|....
gi 115532624 195 IVCIYVLSAIHPDNIKNALKNLVRLLKPGGSLLL 228
Cdd:COG0500   98 VVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
121-228 3.05e-10

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: 56.95  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSssrlmLHSCDYAPNAIRVLKsqDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:COG2227   28 VLDVGCGTGRLALALARRGAD-----VTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED----GSFDLVICSEV 96
                         90       100
                 ....*....|....*....|....*...
gi 115532624 201 LsaIHPDNIKNALKNLVRLLKPGGSLLL 228
Cdd:COG2227   97 L--EHLPDPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
121-231 7.61e-10

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: 55.51  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSSSrlmlHSCDYAPNAIRVLKSQDAYD-PEKMNAFVWDITQPASQEapnVGSLDYIVCIY 199
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARV----TGVDISPVALELARKAAAALlADNVEVLKGDAEELPPEA---DESFDVIISDP 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532624 200 VLSAIHPDnIKNALKNLVRLLKPGGSLLLKDY 231
Cdd:cd02440   75 PLHHLVED-LARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
122-228 1.04e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 51.90  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  122 LEVGCGVGNTTFPLLQVNNSssrlmLHSCDYAPNAIRVLKsqDAYDPEKMNAFVWDITQPASQEapnvGSLDYIVCIYVL 201
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-----VTGVDISPEMLELAR--EKAPREGLTFVVGDAEDLPFPD----NSFDLVLSSEVL 69
                          90       100
                  ....*....|....*....|....*..
gi 115532624  202 SaiHPDNIKNALKNLVRLLKPGGSLLL 228
Cdd:pfam08241  70 H--HVEDPERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
121-290 8.33e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.15  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSssrlmLHSCDYAPNAIRVLKSQDAYDpekmNAFVWDITQPASQEapnvGSLDYIVCIYV 200
Cdd:COG4976   50 VLDLGCGTGLLGEALRPRGYR-----LTGVDLSEEMLAKAREKGVYD----RLLVADLADLAEPD----GRFDLIVAADV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 201 LSaiHPDNIKNALKNLVRLLKPGGSLLLkDYGrydltqlrfkkdrlidgnlycRGDGTLVYFFDMEELETLLAEHGLqkk 280
Cdd:COG4976  117 LT--YLGDLAAVFAGVARALKPGGLFIF-SVE---------------------DADGSGRYAHSLDYVRDLLAAAGF--- 169
                        170
                 ....*....|
gi 115532624 281 vmHVDRRLIV 290
Cdd:COG4976  170 --EVPGLLVV 177
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
121-228 7.54e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.31  E-value: 7.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQ--------VNNSSSrlmlhSCDYAPNAIRVLKSQDAYDPEKMNAFVWDITQPAsqeapnvgsl 192
Cdd:COG2230   55 VLDIGCGWGGLALYLARrygvrvtgVTLSPE-----QLEYARERAAEAGLADRVEVRLADYRDLPADGQF---------- 119
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 115532624 193 DYIVCIYVLSAIHPDNIKNALKNLVRLLKPGGSLLL 228
Cdd:COG2230  120 DAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
121-228 1.45e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.89  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624 121 ILEVGCGVGNTTFPLLQVNNSSSrlmLHSCDYAPNAIRVLKSQDAY-DPEKMNAFVWDITQPAsqeapnvgslDYIVCIY 199
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGAR---VTGVDLSPEMLARARARLPNvRFVVADLRDLDPPEPF----------DLVVSNA 71
                         90       100
                 ....*....|....*....|....*....
gi 115532624 200 VLSaiHPDNIKNALKNLVRLLKPGGSLLL 228
Cdd:COG4106   72 ALH--WLPDHAALLARLAAALAPGGVLAV 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
116-231 5.71e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.71  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532624  116 KEKIEILEVGCGVGNTTFPLLQVNNSSSRlmLHSCDYAPNAIRV---LKSQDAYDpeKMNAFVWDITQPASQEAPNvgSL 192
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAE--VVGIDISEEAIEKareNAQKLGFD--NVEFEQGDIEELPELLEDD--KF 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 115532624  193 DYIVCIYVLSAIhPDNIKnALKNLVRLLKPGGSLLLKDY 231
Cdd:pfam13847  76 DVVISNCVLNHI-PDPDK-VLQEILRVLKPGGRLIISDP 112
 
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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