NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034631231|ref|XP_016861207|]
View 

tRNA N(3)-methylcytidine methyltransferase METTL6 isoform X1 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10549439)

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 tRNA N(3)-methylcytidine methyltransferase METTL6

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 1.64e-19

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


:

Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 81.26  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAI----EYVKQNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFV 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaarERLAALGLLNAVRVELFQLDLGELD------PGSFDVVVASNV 74

                          90       100
                  ....*....|....*....|...
gi 1034631231 160 LSavHPDKMHLVLQNIYKVLKPG 182
Cdd:pfam08242  75 LH--HLADPRAVLRNIRRLLKPG 95
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 1.64e-19

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 81.26  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAI----EYVKQNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFV 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaarERLAALGLLNAVRVELFQLDLGELD------PGSFDVVVASNV 74

                          90       100
                  ....*....|....*....|...
gi 1034631231 160 LSavHPDKMHLVLQNIYKVLKPG 182
Cdd:pfam08242  75 LH--HLADPRAVLRNIRRLLKPG 95
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 82-187 4.16e-17

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: 75.16  E-value: 4.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  82 TMLEAGCGVGNCLFPLLEeDPNIFAYACDFSPRAIEYVKQNPLYD-TERCKVFQCDLTKddlLDHVPPESVDVVMLIFVL 160
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALlADNVEVLKGDAEE---LPPEADESFDVIISDPPL 76

                          90       100
                  ....*....|....*....|....*..
gi 1034631231 161 SAVHPDkMHLVLQNIYKVLKPGKSVLF 187
Cdd:cd02440    77 HHLVED-LARFLEEARRLLKPGGVLVL 102
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-199 1.29e-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: 63.86  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTKDDLldhvPPESVDVVMLIFVLSAV 163
Cdd:COG2226    27 LDLGCGTGRLALALAERGARV--TGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPF----PDGSFDLVISSFVLHHL 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034631231 164 hPDKmHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLR 199
Cdd:COG2226   101 -PDP-ERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
82-189 2.14e-04

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 42.55  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  82 TMLEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTkdDLLDHVPPESVDVVMLIFVL- 160
Cdd:PRK06922  421 TIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKKKQNEGRSWNVIKGDAI--NLSSSFEKESVDTIVYSSILh 498

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034631231 161 ---SAVHPDKM---HLV----LQNIYKVLKPGKSVLFRD 189
Cdd:PRK06922  499 elfSYIEYEGKkfnHEVikkgLQSAYEVLKPGGRIIIRD 537
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 1.64e-19

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 81.26  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAI----EYVKQNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFV 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaarERLAALGLLNAVRVELFQLDLGELD------PGSFDVVVASNV 74

                          90       100
                  ....*....|....*....|...
gi 1034631231 160 LSavHPDKMHLVLQNIYKVLKPG 182
Cdd:pfam08242  75 LH--HLADPRAVLRNIRRLLKPG 95
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-182 7.54e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.83  E-value: 7.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEdPNIFAYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSAV 163
Cdd:pfam13649   2 LDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHL 76

                          90
                  ....*....|....*....
gi 1034631231 164 HPDKMHLVLQNIYKVLKPG 182
Cdd:pfam13649  77 PDPDLEAALREIARVLKPG 95
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 82-187 4.16e-17

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: 75.16  E-value: 4.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  82 TMLEAGCGVGNCLFPLLEeDPNIFAYACDFSPRAIEYVKQNPLYD-TERCKVFQCDLTKddlLDHVPPESVDVVMLIFVL 160
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALlADNVEVLKGDAEE---LPPEADESFDVIISDPPL 76

                          90       100
                  ....*....|....*....|....*..
gi 1034631231 161 SAVHPDkMHLVLQNIYKVLKPGKSVLF 187
Cdd:cd02440    77 HHLVED-LARFLEEARRLLKPGGVLVL 102
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-199 1.29e-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: 63.86  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTKDDLldhvPPESVDVVMLIFVLSAV 163
Cdd:COG2226    27 LDLGCGTGRLALALAERGARV--TGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPF----PDGSFDLVISSFVLHHL 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034631231 164 hPDKmHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLR 199
Cdd:COG2226   101 -PDP-ERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 78-187 7.08e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.01  E-value: 7.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  78 DQKLTMLEAGCGVGNCLFPLLEEDPNIFaYACDFSPRAIEYVKQN-PLYDTERCKVFQCDLTKddlLDHVPPESVDVVML 156
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARFGGRV-IGIDLSPEAIALARARaAKAGLGNVEFLVADLAE---LDPLPAESFDLVVA 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034631231 157 IFVLSAVHPDKMHLVLQNIYKVLKPGKSVLF 187
Cdd:COG0500   101 FGVLHHLPPEEREALLRELARALKPGGVLLL 131
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-190 1.26e-11

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: 60.80  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  54 TNFFKDRHWTTReFEELrsCREFEDQKLTMLEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNplYDTERCKVF 133
Cdd:COG2227     2 SDPDARDFWDRR-LAAL--LARLLPAGGRVLDVGCGTGRLALALARRGADV--TGVDISPEALEIARER--AAELNVDFV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034631231 134 QCDLTKDDLldhvPPESVDVVMLIFVLSavHPDKMHLVLQNIYKVLKPGKSVLFRDY 190
Cdd:COG2227    75 QGDLEDLPL----EDGSFDLVICSEVLE--HLPDPAALLRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-187 3.90e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 58.45  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNplYDTERCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSav 163
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARV--TGVDISPEMLELAREK--APREGLTFVVGDAEDLPFPD----NSFDLVLSSEVLH-- 70

                          90       100
                  ....*....|....*....|....
gi 1034631231 164 HPDKMHLVLQNIYKVLKPGKSVLF 187
Cdd:pfam08241  71 HVEDPERALREIARVLKPGGILII 94
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 81-190 1.11e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.89  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  81 LTMLEAGCGVGNCLFPLLEED-PNIFAYACDFSPRAIEYVKQN-PLYDTERCKVFQCDLTkdDLLDHVPPESVDVVMLIF 158
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENaQKLGFDNVEFEQGDIE--ELPELLEDDKFDVVISNC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034631231 159 VLSAV-HPDKmhlVLQNIYKVLKPGKSVLFRDY 190
Cdd:pfam13847  83 VLNHIpDPDK---VLQEILRVLKPGGRLIISDP 112
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-237 3.92e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 54.74  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  60 RHWTTREFEELRScREFEDQKLTM--LEAGCGVGNCLFPLLEEDPNIFAYacDFSPRAIEYVKQNPLYDTErckvfqcdl 137
Cdd:pfam13489   2 AHQRERLLADLLL-RLLPKLPSPGrvLDFGCGTGIFLRLLRAQGFSVTGV--DPSPIAIERALLNVRFDQF--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231 138 tkDDLLDHVPPESVDVVMLIFVLSAVHPdkMHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLRFKassklgENFYVRQDGT 217
Cdd:pfam13489  70 --DEQEAAVPAGKFDVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEADRLLL------EWPYLRPRNG 139

                         170       180
                  ....*....|....*....|
gi 1034631231 218 RSYFFTDDFLAQLFMDTGYE 237
Cdd:pfam13489 140 HISLFSARSLKRLLEEAGFE 159
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
74-182 5.89e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 54.23  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  74 REFEDQKLTMLEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNPLYDTerckVFQCDLTKDDlldhVPPESVDV 153
Cdd:COG4976    41 RLPPGPFGRVLDLGCGTGLLGEALRPRGYRL--TGVDLSEEMLAKAREKGVYDR----LLVADLADLA----EPDGRFDL 110

                          90       100
                  ....*....|....*....|....*....
gi 1034631231 154 VMLIFVLSavHPDKMHLVLQNIYKVLKPG 182
Cdd:COG4976   111 IVAADVLT--YLGDLAAVFAGVARALKPG 137
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
84-182 3.15e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.51  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAIEYVKQN-PlydterckvfQCDLTKDDLLDHVPPESVDVVMLIFVLSa 162
Cdd:COG4106     6 LDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARlP----------NVRFVVADLRDLDPPEPFDLVVSNAALH- 74

                          90       100
                  ....*....|....*....|
gi 1034631231 163 vHPDKMHLVLQNIYKVLKPG 182
Cdd:COG4106    75 -WLPDHAALLARLAAALAPG 93
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 82-182 2.24e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 46.46  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  82 TMLEAGCGVGNCLFPLLEEdPNIFAYACDFSPRAIEYVKQN----PLydTERCKVFQCDLTkddllDHVPPESVDVVMLI 157
Cdd:COG2230    54 RVLDIGCGWGGLALYLARR-YGVRVTGVTLSPEQLEYARERaaeaGL--ADRVEVRLADYR-----DLPADGQFDAIVSI 125

                          90       100
                  ....*....|....*....|....*
gi 1034631231 158 FVLSAVHPDKMHLVLQNIYKVLKPG 182
Cdd:COG2230   126 GMFEHVGPENYPAYFAKVARLLKPG 150
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
82-189 2.14e-04

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 42.55  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631231  82 TMLEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTkdDLLDHVPPESVDVVMLIFVL- 160
Cdd:PRK06922  421 TIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKKKQNEGRSWNVIKGDAI--NLSSSFEKESVDTIVYSSILh 498

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034631231 161 ---SAVHPDKM---HLV----LQNIYKVLKPGKSVLFRD 189
Cdd:PRK06922  499 elfSYIEYEGKkfnHEVikkgLQSAYEVLKPGGRIIIRD 537
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH