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Conserved domains on  [gi|1519712244|gb|RPG81959|]
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methyltransferase domain-containing protein [Crocinitomicaceae bacterium TMED114]

Protein Classification

tRNA1(Val) (adenine(37)-N6)-methyltransferase( domain architecture ID 11467886)

tRNA(1)(Val) (adenine(37)-N(6))-methyltransferase is a class I SAM-dependent methyltransferase that specifically methylates the adenine in position 37 of tRNA(1)(Val)

CATH:  2.20.25.110
EC:  2.1.1.223
Gene Ontology:  GO:0016430|GO:1904047|GO:0008170|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 16-253 6.24e-61

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 191.90  E-value: 6.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  16 PFHFKSFSVEQDGAAMKVGMDGIVLGATTPVEGVHLAMDIGSGNGYVGLMLLQRmSAGSHVIGVEIEPEAARQSEENYAN 95
Cdd:COG4123     5 GFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQR-SPGARITGVEIQPEAAELARRNVAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  96 HPFEGRtASAWSGAIQSFVEAHPDqiGQVDLMVSNPPFFRDKP--KSPIQARNLARHDDTLKMGDLVKAASLLLKPGGRL 173
Cdd:COG4123    84 NGLEDR-ITVIHGDLKEFAAELPP--GSFDLVVSNPPYFKAGSgrKSPDEARAIARHEDALTLEDLIRAAARLLKPGGRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244 174 CTIWPYDRLEEWHSWAAGSEFHVLCTTHITTMAHLPCKRFTSEWTKQPCPaEPHQDKKLTLEGSAtLDYTEEYLRFIRPY 253
Cdd:COG4123   161 ALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRA-GLRILPPLVIHDED-GEYTPEVKALLRDF 238
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 16-253 6.24e-61

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 191.90  E-value: 6.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  16 PFHFKSFSVEQDGAAMKVGMDGIVLGATTPVEGVHLAMDIGSGNGYVGLMLLQRmSAGSHVIGVEIEPEAARQSEENYAN 95
Cdd:COG4123     5 GFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQR-SPGARITGVEIQPEAAELARRNVAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  96 HPFEGRtASAWSGAIQSFVEAHPDqiGQVDLMVSNPPFFRDKP--KSPIQARNLARHDDTLKMGDLVKAASLLLKPGGRL 173
Cdd:COG4123    84 NGLEDR-ITVIHGDLKEFAAELPP--GSFDLVVSNPPYFKAGSgrKSPDEARAIARHEDALTLEDLIRAAARLLKPGGRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244 174 CTIWPYDRLEEWHSWAAGSEFHVLCTTHITTMAHLPCKRFTSEWTKQPCPaEPHQDKKLTLEGSAtLDYTEEYLRFIRPY 253
Cdd:COG4123   161 ALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRA-GLRILPPLVIHDED-GEYTPEVKALLRDF 238
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 54-182 9.67e-09

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: 53.36  E-value: 9.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmSAGSHVIGVEIEPEAARQSEENYANHPFEGrtASA-WSGAIQSFVEahpdqiGQVDLMVSNPP 132
Cdd:pfam05175  37 DLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGLEN--GEVvASDVYSGVED------GKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1519712244 133 FFrdkpkspiqarnlARHDDTLKMGD-LVKAASLLLKPGGRLCTIW----PYDRL 182
Cdd:pfam05175 108 FH-------------AGLATTYNVAQrFIADAKRHLRPGGELWIVAnrflGYPPL 149
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-176 6.80e-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: 49.35  E-value: 6.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmsAGSHVIGVEIEPEAARQSEENYANHPFEGrtasaWSGAIQSFVEAHPDQIGQVDLMVSNPPF 133
Cdd:cd02440     4 DLGCGTGALALALASG--PGARVTGVDISPVALELARKAAAALLADN-----VEVLKGDAEELPPEADESFDVIISDPPL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519712244 134 FrdkpkspiqarnlARHDDtlkMGDLVKAASLLLKPGGRLCTI 176
Cdd:cd02440    77 H-------------HLVED---LARFLEEARRLLKPGGVLVLT 103
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 52-96 5.34e-04

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.85  E-value: 5.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1519712244  52 AMDIGSGNGYVGLMLLQRMSAGShVIGVEIEPEAARQSEENYANH 96
Cdd:TIGR02469  23 LWDIGAGTGSVTIEAARLVPNGR-VYAIERNPEALDLIERNLRRF 66
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-92 9.90e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 9.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1519712244  52 AMDIGSGNGYVGLMLLQRmsaGSHVIGVEIEPEAARQSEEN 92
Cdd:PRK14968   27 VLEVGTGSGIVAIVAAKN---GKKVVGVDINPYAVECAKCN 64
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 16-253 6.24e-61

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 191.90  E-value: 6.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  16 PFHFKSFSVEQDGAAMKVGMDGIVLGATTPVEGVHLAMDIGSGNGYVGLMLLQRmSAGSHVIGVEIEPEAARQSEENYAN 95
Cdd:COG4123     5 GFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQR-SPGARITGVEIQPEAAELARRNVAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  96 HPFEGRtASAWSGAIQSFVEAHPDqiGQVDLMVSNPPFFRDKP--KSPIQARNLARHDDTLKMGDLVKAASLLLKPGGRL 173
Cdd:COG4123    84 NGLEDR-ITVIHGDLKEFAAELPP--GSFDLVVSNPPYFKAGSgrKSPDEARAIARHEDALTLEDLIRAAARLLKPGGRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244 174 CTIWPYDRLEEWHSWAAGSEFHVLCTTHITTMAHLPCKRFTSEWTKQPCPaEPHQDKKLTLEGSAtLDYTEEYLRFIRPY 253
Cdd:COG4123   161 ALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRA-GLRILPPLVIHDED-GEYTPEVKALLRDF 238
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 54-173 1.16e-09

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: 56.35  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmSAGSHVIGVEIEPEAARQSEENYANHPFEGRTAsAWSGAIQSFVEahpdqiGQVDLMVSNPPF 133
Cdd:COG2813    55 DLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANGLENVEV-LWSDGLSGVPD------GSFDLILSNPPF 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1519712244 134 F--RDKPKSPIQArnlarhddtlkmgdLVKAASLLLKPGGRL 173
Cdd:COG2813   127 HagRAVDKEVAHA--------------LIADAARHLRPGGEL 154
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 54-182 9.67e-09

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: 53.36  E-value: 9.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmSAGSHVIGVEIEPEAARQSEENYANHPFEGrtASA-WSGAIQSFVEahpdqiGQVDLMVSNPP 132
Cdd:pfam05175  37 DLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGLEN--GEVvASDVYSGVED------GKFDLIISNPP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1519712244 133 FFrdkpkspiqarnlARHDDTLKMGD-LVKAASLLLKPGGRLCTIW----PYDRL 182
Cdd:pfam05175 108 FH-------------AGLATTYNVAQrFIADAKRHLRPGGELWIVAnrflGYPPL 149
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 54-173 3.91e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.84  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRMSaGSHVIGVEIEPEAARQSEENYANHPFEGRTAsawsgAIQSFVEAHPDQIGQVDLMVSNPPF 133
Cdd:COG2890   118 DLGTGSGAIALALAKERP-DARVTAVDISPDALAVARRNAERLGLEDRVR-----FLQGDLFEPLPGDGRFDLIVSNPPY 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519712244 134 FRDKPKSPIQArNLARHD------------DTLKMgdLVKAASLLLKPGGRL 173
Cdd:COG2890   192 IPEDEIALLPP-EVRDHEprlaldggedglDFYRR--IIAQAPRLLKPGGWL 240
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-176 6.80e-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: 49.35  E-value: 6.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmsAGSHVIGVEIEPEAARQSEENYANHPFEGrtasaWSGAIQSFVEAHPDQIGQVDLMVSNPPF 133
Cdd:cd02440     4 DLGCGTGALALALASG--PGARVTGVDISPVALELARKAAAALLADN-----VEVLKGDAEELPPEADESFDVIISDPPL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519712244 134 FrdkpkspiqarnlARHDDtlkMGDLVKAASLLLKPGGRLCTI 176
Cdd:cd02440    77 H-------------HLVED---LARFLEEARRLLKPGGVLVLT 103
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 53-204 2.29e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.95  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  53 MDIGSGNGYVGLMLLQRMSAGSHVIGVEIEPEAARQSEENYANHPFEGRTASAwsGAIQSFVEAHPDQigQVDLMVSNPP 132
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQ--GDIEELPELLEDD--KFDVVISNCV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519712244 133 F--FRDKPKSpiqarnlarhddtlkmgdLVKAASlLLKPGGRLCTIWPYDRLEEWHSWAAGSEFHVLCTTHITT 204
Cdd:pfam13847  84 LnhIPDPDKV------------------LQEILR-VLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAIL 138
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
53-133 1.02e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.98  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  53 MDIGSGNGY--VGLMLLQrmsaGSHVIGVEIEPEAARQSEENYANHpfegrtasawsGAIQSFVEA---HPDQIGQVDLM 127
Cdd:COG2263    50 LDLGCGTGMlaIGAALLG----AKKVVGVDIDPEALEIARENAERL-----------GVRVDFIRAdvtRIPLGGSVDTV 114


                  ....*.
gi 1519712244 128 VSNPPF 133
Cdd:COG2263   115 VMNPPF 120
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-171 2.02e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 45.25  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmsAGSHVIGVEIEPEAARQSEENYANHPFEGRtasawsgAIQSFVEAHPDQIGQVDLMVSNPPF 133
Cdd:pfam13649   3 DLGCGTGRLTLALARR--GGARVTGVDLSPEMLERARERAAEAGLNVE-------FVQGDAEDLPFPDGSFDLVVSSGVL 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1519712244 134 FRDKPKSPIQA-RNLARHddtlkmgdlvkaasllLKPGG 171
Cdd:pfam13649  74 HHLPDPDLEAAlREIARV----------------LKPGG 96
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 55-102 2.67e-06

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 46.33  E-value: 2.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1519712244  55 IGSGNGYVGLMLLQRMSAGSHVIGVEIEPEAARQSEENYANHPFEGRT 102
Cdd:COG4122    23 IGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRI 70
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 54-194 5.04e-06

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: 44.98  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmsaGSHVIGVEIEPEAARQSEENYANHPFEGRTasawsgaIQSFVEAHPDQIGQVDLMVSNP-- 131
Cdd:COG2226    28 DLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLNVEF-------VVGDAEDLPFPDGSFDLVISSFvl 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519712244 132 PFFRDKPKSpiqARNLARhddtlkmgdlvkaaslLLKPGGRLCTI-WPYDRLEEWHSWAAGSEF 194
Cdd:COG2226    98 HHLPDPERA---LAEIAR----------------VLKPGGRLVVVdFSPPDLAELEELLAEAGF 142
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 62-186 1.05e-05

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 44.55  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  62 VGLMLLQRMSAGSHVIGVEIEPEAARQSEEN---YANHPFEGRTASAwsgaiqsfvEAHPDQIGQVDLMVSNPPFFRdkp 138
Cdd:COG1041    37 TGTILIEAGLLGRRVIGSDIDPKMVEGARENlehYGYEDADVIRGDA---------RDLPLADESVDAIVTDPPYGR--- 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1519712244 139 kspiQARNLARHDDTLkMGDLVKAASLLLKPGGRLCTIWPYDRLEEWH 186
Cdd:COG1041   105 ----SSKISGEELLEL-YEKALEEAARVLKPGGRVVIVTPRDIDELLE 147
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 52-177 1.67e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.52  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  52 AMDIGSGNGYVGLMLLQRmsAGSHVIGVEIEPEA-----ARQSEENYANHPFegrtasawsgAIQSFVEAHPDQIGQVDL 126
Cdd:COG0500    30 VLDLGCGTGRNLLALAAR--FGGRVIGIDLSPEAialarARAAKAGLGNVEF----------LVADLAELDPLPAESFDL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519712244 127 MVsnppffrdkpkspiqARNLARHDDTLKMGDLVKAASLLLKPGGRLCTIW 177
Cdd:COG0500    98 VV---------------AFGVLHHLPPEEREALLRELARALKPGGVLLLSA 133
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-173 2.09e-05

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: 43.08  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRmsaGSHVIGVEIEPEAARQSEENYANHPFEgrtasawsgAIQSFVEAHPDQIGQVDLMVSNppf 133
Cdd:COG2227    30 DVGCGTGRLALALARR---GADVTGVDISPEALEIARERAAELNVD---------FVQGDLEDLPLEDGSFDLVICS--- 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1519712244 134 frdkpkspiqarnlarhdDTL----KMGDLVKAASLLLKPGGRL 173
Cdd:COG2227    95 ------------------EVLehlpDPAALLRELARLLKPGGLL 120
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
54-173 8.92e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.58  E-value: 8.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLMLLQRMSaGSHVIGVEIEPEAARQSEENYANHPFEGRTASAWSgaiqsfveahPDqiGQVDLMVSNP-- 131
Cdd:COG4106     7 DLGCGTGRLTALLAERFP-GARVTGVDLSPEMLARARARLPNVRFVVADLRDLD----------PP--EPFDLVVSNAal 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1519712244 132 PFFRDKPKspiQARNLARHddtlkmgdlvkaasllLKPGGRL 173
Cdd:COG4106    74 HWLPDHAA---LLARLAAA----------------LAPGGVL 96
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 52-96 5.34e-04

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.85  E-value: 5.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1519712244  52 AMDIGSGNGYVGLMLLQRMSAGShVIGVEIEPEAARQSEENYANH 96
Cdd:TIGR02469  23 LWDIGAGTGSVTIEAARLVPNGR-VYAIERNPEALDLIERNLRRF 66
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-92 9.90e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 9.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1519712244  52 AMDIGSGNGYVGLMLLQRmsaGSHVIGVEIEPEAARQSEEN 92
Cdd:PRK14968   27 VLEVGTGSGIVAIVAAKN---GKKVVGVDINPYAVECAKCN 64
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 54-173 1.72e-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: 38.87  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  54 DIGSGNGYVGLML-LQRMSAgsHVIGVEIEPEAARQSEENYANHPFEGRTAsawsgAIQS-FVEAHPDQigQVDLMVSNP 131
Cdd:TIGR00536 120 DLGTGSGCIALALaYEFPNA--EVIAVDISPDALAVAEENAEKNQLEHRVE-----FIQSnLFEPLAGQ--KIDIIVSNP 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519712244 132 PF-----FRDKP----KSPIQArnLARHDDTLK-MGDLVKAASLLLKPGGRL 173
Cdd:TIGR00536 191 PYideedLADLPnvvrFEPLLA--LVGGDDGLNiLRQIIELAPDYLKPNGFL 240
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
44-133 2.48e-03

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 38.39  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  44 TPVEGVHLaMDIGSGNGYVGLMLLQRMSAGSHVIGVEIEPEAARQSEENYA--NHPFEGRTasawsgaiQSFVEahPDQI 121
Cdd:COG0827   112 TKKEGLRI-LDPAVGTGNLLTTVLNQLKKKVNAYGVEVDDLLIRLAAVLANlqGHPVELFH--------QDALQ--PLLI 180

                          90
                  ....*....|..
gi 1519712244 122 GQVDLMVSNPPF 133
Cdd:COG0827   181 DPVDVVISDLPV 192
PRK14967 PRK14967
putative methyltransferase; Provisional
 52-173 5.81e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 36.95  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712244  52 AMDIGSGNGYVGLMLlQRMSAGsHVIGVEIEPEAARQSEENYANHpfeGRTASAWSGaiqSFVEAHPDqiGQVDLMVSNP 131
Cdd:PRK14967   40 VLDLCTGSGALAVAA-AAAGAG-SVTAVDISRRAVRSARLNALLA---GVDVDVRRG---DWARAVEF--RPFDVVVSNP 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1519712244 132 PFFRDKPKSPiQARNLAR-----HDDTLKMGDLVKAASLLLKPGGRL 173
Cdd:PRK14967  110 PYVPAPPDAP-PSRGPARawdagPDGRAVLDRLCDAAPALLAPGGSL 155
 
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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