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Conserved domains on  [gi|255683413|ref|NP_766155|]
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tRNA N(3)-methylcytidine methyltransferase METTL2 [Mus musculus]

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.-
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
178-280 2.98e-18

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


:

Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 79.33  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  178 LEVGCGVGNTVFPILqtNNNPNLFVYCCDFSATAIEL----LKTNSQYDPSRCYAFVHDLCDEDqsypvpEDSLDVIVLI 253
Cdd:pfam08242   1 LEIGCGTGTLLRALL--EALPGLEYTGLDISPAALEAarerLAALGLLNAVRVELFQLDLGELD------PGSFDVVVAS 72
                          90       100
                  ....*....|....*....|....*..
gi 255683413  254 FVLSAIvpDKMQKAISKLSRLLKPGGV 280
Cdd:pfam08242  73 NVLHHL--ADPRAVLRNIRRLLKPGGV 97
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
178-280 2.98e-18

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 79.33  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  178 LEVGCGVGNTVFPILqtNNNPNLFVYCCDFSATAIEL----LKTNSQYDPSRCYAFVHDLCDEDqsypvpEDSLDVIVLI 253
Cdd:pfam08242   1 LEIGCGTGTLLRALL--EALPGLEYTGLDISPAALEAarerLAALGLLNAVRVELFQLDLGELD------PGSFDVVVAS 72
                          90       100
                  ....*....|....*....|....*..
gi 255683413  254 FVLSAIvpDKMQKAISKLSRLLKPGGV 280
Cdd:pfam08242  73 NVLHHL--ADPRAVLRNIRRLLKPGGV 97
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
176-295 8.84e-17

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: 76.57  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQTNNNpnlfVYCCDFSATAIELLKTNSQYDPSRCYAFVHDLCDedqsYPVPEDSLDVIVLIFV 255
Cdd:COG2226   25 RVLDLGCGTGRLALALAERGAR----VTGVDISPEMLELARERAAEAGLNVEFVVGDAED----LPFPDGSFDLVISSFV 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 255683413 256 LSAiVPDKmQKAISKLSRLLKPGGVMLLRDYGRYDMAQLR 295
Cdd:COG2226   97 LHH-LPDP-ERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
176-283 1.04e-13

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: 66.68  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQtnnNPNLFVYCCDFSATAIELLKTNSQYDPSRCYAFVHdlCDEDQSYPVPEDSLDVIVLIFV 255
Cdd:cd02440    1 RVLDLGCGTGALALALAS---GPGARVTGVDISPVALELARKAAAALLADNVEVLK--GDAEELPPEADESFDVIISDPP 75
                         90       100
                 ....*....|....*....|....*...
gi 255683413 256 LSAIVPDkMQKAISKLSRLLKPGGVMLL 283
Cdd:cd02440   76 LHHLVED-LARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
176-279 4.25e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.54  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQTNNNPNLfVYCCDFSATAIELLKTNSQYDPSRCyAFVHDlcDEDQSyPVPEDSLDVIVLIFV 255
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVGPEGR-VVGIDRSEAMLALAKERAAGLGPNV-EFVRG--DADGL-PFPDGSFDAVRSDRV 96
                         90       100
                 ....*....|....*....|....
gi 255683413 256 LSAIvPDKmQKAISKLSRLLKPGG 279
Cdd:PRK08317  97 LQHL-EDP-ARALAEIARVLRPGG 118
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
178-280 2.98e-18

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 79.33  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  178 LEVGCGVGNTVFPILqtNNNPNLFVYCCDFSATAIEL----LKTNSQYDPSRCYAFVHDLCDEDqsypvpEDSLDVIVLI 253
Cdd:pfam08242   1 LEIGCGTGTLLRALL--EALPGLEYTGLDISPAALEAarerLAALGLLNAVRVELFQLDLGELD------PGSFDVVVAS 72
                          90       100
                  ....*....|....*....|....*..
gi 255683413  254 FVLSAIvpDKMQKAISKLSRLLKPGGV 280
Cdd:pfam08242  73 NVLHHL--ADPRAVLRNIRRLLKPGGV 97
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
177-279 5.59e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 78.37  E-value: 5.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  177 ILEVGCGVGNTVFPILQtnnNPNLFVYCCDFSATAIELLKTNSQYDPSRCYAFVHDLCDedqsYPVPEDSLDVIVLIFVL 256
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR---RGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED----LPFPDGSFDLVVSSGVL 73
                          90       100
                  ....*....|....*....|...
gi 255683413  257 SAIVPDKMQKAISKLSRLLKPGG 279
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
176-295 8.84e-17

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: 76.57  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQTNNNpnlfVYCCDFSATAIELLKTNSQYDPSRCYAFVHDLCDedqsYPVPEDSLDVIVLIFV 255
Cdd:COG2226   25 RVLDLGCGTGRLALALAERGAR----VTGVDISPEMLELARERAAEAGLNVEFVVGDAED----LPFPDGSFDLVISSFV 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 255683413 256 LSAiVPDKmQKAISKLSRLLKPGGVMLLRDYGRYDMAQLR 295
Cdd:COG2226   97 LHH-LPDP-ERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
176-283 6.95e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 72.64  E-value: 6.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQTNNNPnlfVYCCDFSATAIELLKTN-SQYDPSRCYAFVHDLCDEDqsyPVPEDSLDVIVLIF 254
Cdd:COG0500   29 RVLDLGCGTGRNLLALAARFGGR---VIGIDLSPEAIALARARaAKAGLGNVEFLVADLAELD---PLPAESFDLVVAFG 102
                         90       100
                 ....*....|....*....|....*....
gi 255683413 255 VLSAIVPDKMQKAISKLSRLLKPGGVMLL 283
Cdd:COG0500  103 VLHHLPPEEREALLRELARALKPGGVLLL 131
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
176-283 1.04e-13

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: 66.68  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQtnnNPNLFVYCCDFSATAIELLKTNSQYDPSRCYAFVHdlCDEDQSYPVPEDSLDVIVLIFV 255
Cdd:cd02440    1 RVLDLGCGTGALALALAS---GPGARVTGVDISPVALELARKAAAALLADNVEVLK--GDAEELPPEADESFDVIISDPP 75
                         90       100
                 ....*....|....*....|....*...
gi 255683413 256 LSAIVPDkMQKAISKLSRLLKPGGVMLL 283
Cdd:cd02440   76 LHHLVED-LARFLEEARRLLKPGGVLVL 102
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
176-286 3.19e-12

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: 63.11  E-value: 3.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQTNNNpnlfVYCCDFSATAIELLKTNsqYDPSRCYAFVHDLCDedqsYPVPEDSLDVIVLIFV 255
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGAD----VTGVDISPEALEIARER--AAELNVDFVQGDLED----LPLEDGSFDLVICSEV 96
                         90       100       110
                 ....*....|....*....|....*....|.
gi 255683413 256 LSAiVPDkMQKAISKLSRLLKPGGVMLLRDY 286
Cdd:COG2227   97 LEH-LPD-PAALLRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
178-283 4.63e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.53  E-value: 4.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  178 LEVGCGVGNTVFPILQTNNNpnlfVYCCDFSATAIELLKTNSQYDPsrcYAFVH-DLCDedqsYPVPEDSLDVIVLIFVL 256
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR----VTGVDISPEMLELAREKAPREG---LTFVVgDAED----LPFPDNSFDLVLSSEVL 69
                          90       100
                  ....*....|....*....|....*..
gi 255683413  257 SAiVPDkMQKAISKLSRLLKPGGVMLL 283
Cdd:pfam08241  70 HH-VED-PERALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
176-336 7.16e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 63.22  E-value: 7.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  176 RILEVGCGVGNtVFPILQTNNnpnlfvyccdFSATAIELlktnSQYDPSRCYAFVHDLCDEDQSYPVPEDSLDVIVLIFV 255
Cdd:pfam13489  25 RVLDFGCGTGI-FLRLLRAQG----------FSVTGVDP----SPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  256 LSAiVPDkMQKAISKLSRLLKPGGVMLLRDYGRYDMAQLRFKKgqclsgNFYVRGDGTRVYFFTQGELDTLFTAAGLEKV 335
Cdd:pfam13489  90 LEH-VPD-PPALLRQIAALLKPGGLLLLSTPLASDEADRLLLE------WPYLRPRNGHISLFSARSLKRLLEEAGFEVV 161

                  .
gi 255683413  336 Q 336
Cdd:pfam13489 162 S 162
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
175-331 2.37e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.50  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  175 YRILEVGCGVGNTVFpILQTNNNPNLFVYCCDFSATAIELLKTNSQydpSRCYAFVH-DLCD-EDQSYPVPEDSLDVIVL 252
Cdd:pfam13847   5 MRVLDLGCGTGHLSF-ELAEELGPNAEVVGIDISEEAIEKARENAQ---KLGFDNVEfEQGDiEELPELLEDDKFDVVIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  253 IFVLSAIvPDKmQKAISKLSRLLKPGGVMLLRDY-----GRYDMAQLRFKKGQCLSGNfyvrgdgtrvyfFTQGELDTLF 327
Cdd:pfam13847  81 NCVLNHI-PDP-DKVLQEILRVLKPGGRLIISDPdslaeLPAHVKEDSTYYAGCVGGA------------ILKKKLYELL 146

                  ....
gi 255683413  328 TAAG 331
Cdd:pfam13847 147 EEAG 150
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
176-283 6.26e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.90  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQtnNNPNLFVYCCDFSATAIELLKTNSqydpSRCYAFVHDLCDEDqsypvPEDSLDVIVLIFV 255
Cdd:COG4106    4 RVLDLGCGTGRLTALLAE--RFPGARVTGVDLSPEMLARARARL----PNVRFVVADLRDLD-----PPEPFDLVVSNAA 72
                         90       100
                 ....*....|....*....|....*...
gi 255683413 256 LSAiVPDkMQKAISKLSRLLKPGGVMLL 283
Cdd:COG4106   73 LHW-LPD-HAALLARLAAALAPGGVLAV 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
176-333 1.48e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.85  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQtnnnpnlFVYCC---DFSATAIELLKTNSQYDPsrcyAFVHDLCDedqsYPVPEDSLDVIVL 252
Cdd:COG4976   49 RVLDLGCGTGLLGEALRP-------RGYRLtgvDLSEEMLAKAREKGVYDR----LLVADLAD----LAEPDGRFDLIVA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 253 IFVLSAIvpDKMQKAISKLSRLLKPGGVMLlrdygrydmaqlrfkkgqclsgnFYV-RGDGTRVYFFTQGELDTLFTAAG 331
Cdd:COG4976  114 ADVLTYL--GDLAAVFAGVARALKPGGLFI-----------------------FSVeDADGSGRYAHSLDYVRDLLAAAG 168

                 ..
gi 255683413 332 LE 333
Cdd:COG4976  169 FE 170
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
176-285 3.08e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.54  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQtnnNPNLFVYCCDFSATAIELLKTNSQYDPSRCYAFVH--DLCDEDqsypvPEDSLDVIVLI 253
Cdd:COG2230   54 RVLDIGCGWGGLALYLAR---RYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRlaDYRDLP-----ADGQFDAIVSI 125
                         90       100       110
                 ....*....|....*....|....*....|..
gi 255683413 254 FVLSAIVPDKMQKAISKLSRLLKPGGVMLLRD 285
Cdd:COG2230  126 GMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
PRK08317 PRK08317
hypothetical protein; Provisional
176-279 4.25e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.54  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGNTVFPILQTNNNPNLfVYCCDFSATAIELLKTNSQYDPSRCyAFVHDlcDEDQSyPVPEDSLDVIVLIFV 255
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVGPEGR-VVGIDRSEAMLALAKERAAGLGPNV-EFVRG--DADGL-PFPDGSFDAVRSDRV 96
                         90       100
                 ....*....|....*....|....
gi 255683413 256 LSAIvPDKmQKAISKLSRLLKPGG 279
Cdd:PRK08317  97 LQHL-EDP-ARALAEIARVLRPGG 118
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
176-283 5.43e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 40.27  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413  176 RILEVGCGVGntVFPILQTNNNPNLFVYCCDFSATAIELLKTNSQY-DPSRCYAFVHDLCDEdqsypVPEDSLDVIVL-- 252
Cdd:pfam05175  34 KVLDLGCGAG--VLGAALAKESPDAELTMVDINARALESARENLAAnGLENGEVVASDVYSG-----VEDGKFDLIISnp 106
                          90       100       110
                  ....*....|....*....|....*....|..
gi 255683413  253 -IFVLSAIVPDKMQKAISKLSRLLKPGGVMLL 283
Cdd:pfam05175 107 pFHAGLATTYNVAQRFIADAKRHLRPGGELWI 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
176-283 8.99e-04

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: 40.17  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683413 176 RILEVGCGVGntvfPILQT--NNNPNLFVYCCDFSATAIELLKTNSQ-YDPSRCYAFVHDLCDedqsyPVPEDSLDVIVL 252
Cdd:COG2813   52 RVLDLGCGYG----VIGLAlaKRNPEARVTLVDVNARAVELARANAAaNGLENVEVLWSDGLS-----GVPDGSFDLILS 122
                         90       100       110
                 ....*....|....*....|....*....|....
gi 255683413 253 ---IFVLSAIVPDKMQKAISKLSRLLKPGGVMLL 283
Cdd:COG2813  123 nppFHAGRAVDKEVAHALIADAARHLRPGGELWL 156
 
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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